|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
354-878 |
4.05e-167 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 496.51 E-value: 4.05e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 354 IENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRA------FAIPPNIDVLLCEQEVVATD-KTAIN 426
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELepdsgeVSIPKGLRIGYLPQEPPLDDdLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 427 TILEADVRRTEMLKKADELEKQFVAGDlTVQEELNDTFAELKAIGAYSAEARARRILAGLGFSKEMQDRPTNKFSGGWRM 506
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPD-EDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 507 RVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSMFKK 586
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 587 MYVQKRREMIKEYEKQEKRLRELKAhgqskkaaekkqkeSLTRKQEK-NKSKQQKQDED--EGPQELLARPKEYIVKFRF 663
Cdd:COG0488 240 QRAERLEQEAAAYAKQQKKIAKEEE--------------FIRRFRAKaRKAKQAQSRIKalEKLEREEPPRRDKTVEIRF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 664 PEPSQLQPPILGVHNVTFAFPSqKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGRFD 743
Cdd:COG0488 306 PPPERLGKKVLELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 744 QHSgEHLTAEESAAEYLQRLF-NLPHEKARKALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNL 822
Cdd:COG0488 385 QHQ-EELDPDKTVLDELRDGApGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 823 DIESIDALAEAINEYEGGVIIVSHDERLIRETGCTLYVIEDQTINEIVGEFDDYRK 878
Cdd:COG0488 464 DIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
351-878 |
2.04e-141 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 436.98 E-value: 2.04e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 351 DIKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRAF-AIPPNIDVLLCEQEVVATDKTAINTIL 429
Cdd:PLN03073 177 DIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIdGIPKNCQILHVEQEVVGDDTTALQCVL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 EADVRRTEMLK-------KADELEKQFVAGDL-----------TVQEELNDTFAELKAIGAYSAEARARRILAGLGFSKE 491
Cdd:PLN03073 257 NTDIERTQLLEeeaqlvaQQRELEFETETGKGkgankdgvdkdAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 492 MQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 572 KKLQYYKGNYSMFKKMYVQKRREMIKEYEKQEKRlrelKAHGQSKKAAEKKQKESLTRKQEKNKSKQQKQDEDEgpqelL 651
Cdd:PLN03073 417 QKLVTYKGDYDTFERTREEQLKNQQKAFESNERS----RSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDA-----V 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 652 ARPKEYivKFRFPEPS-QLQPPILGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE 730
Cdd:PLN03073 488 VNDPDY--KFEFPTPDdRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGT 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 731 QRKNHRLHVGRFDQHSGEHLTAEESAAEYLQRLF-NLPHEKARKALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSA 809
Cdd:PLN03073 566 VFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFpGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKK 645
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 810 PDVLILDEPTNNLDIESIDALAEAINEYEGGVIIVSHDERLIRETGCTLYVIEDQTINEIVGEFDDYRK 878
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
366-882 |
7.85e-94 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 309.41 E-value: 7.85e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 366 LFVNANLLIAHGRRYGLVGPNGHGKTTLL----RHIATRA--FAIPPNIDVLLCEQEVVATDKTAINTILEADvrrteml 439
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLallkNEISADGgsYTFPGNWQLAWVNQETPALPQPALEYVIDGD------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 440 KKADELEKQfvagdLTVQEELNDTFA------ELKAIGAYSAEARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARA 513
Cdd:PRK10636 89 REYRQLEAQ-----LHDANERNDGHAiatihgKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 514 LYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSMFKKMYVQKRR 593
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 594 EMIKEYEKQEKRLrelkAHGQSKKaaekkqkesltrkqEKNKSKQQKQDEDEGPQELLARpKEYIV--------KFRFPE 665
Cdd:PRK10636 244 QQQAMYESQQERV----AHLQSYI--------------DRFRAKATKAKQAQSRIKMLER-MELIApahvdnpfHFSFRA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 666 PSQLQPPILGVHNVTFAFPSQKPL-FIKVDfgIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGRFDQ 744
Cdd:PRK10636 305 PESLPNPLLKMEKVSAGYGDRIILdSIKLN--LVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 745 HSGEHLTAEESAAEYLQRLF-NLPHEKARKALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:PRK10636 383 HQLEFLRADESPLQHLARLApQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 824 IESIDALAEAINEYEGGVIIVSHDERLIRETGCTLYVIEDQTINEIVGEFDDYRKEVLD 882
Cdd:PRK10636 463 LDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSD 521
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
366-876 |
1.61e-72 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 248.27 E-value: 1.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 366 LFVNANLLIAHGRRYGLVGPNGHGKTTLLRhIATRAF-------AIPPNIDVLLCEQEVVA-TDKTAINTILEADvrrTE 437
Cdd:PRK15064 16 LFENISVKFGGGNRYGLIGANGCGKSTFMK-ILGGDLepsagnvSLDPNERLGKLRQDQFAfEEFTVLDTVIMGH---TE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 438 MLKKADELEKQFVAGDLTVQE-----ELNDTFAELkaiGAYSAEARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLAR 512
Cdd:PRK15064 92 LWEVKQERDRIYALPEMSEEDgmkvaDLEVKFAEM---DGYTAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 513 ALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSMFKKMYVQKR 592
Cdd:PRK15064 169 ALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQAR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 593 REMIKEYEKQEKRLRELKahgqskkaaekkqkeSLTRKQEKNKSK------QQKQDEDEGPQELLA--RPKEYIvkfRFP 664
Cdd:PRK15064 249 ERLLADNAKKKAQIAELQ---------------SFVSRFSANASKakqatsRAKQIDKIKLEEVKPssRQNPFI---RFE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 665 EPSQLQPPILGVHNVTFAFPsQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGRFDQ 744
Cdd:PRK15064 311 QDKKLHRNALEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 745 HSGEHLTAEESAAEYLQRLFNLPH-EKA-RKALGSfgLVSHAHTIK--MKDLSGGQKARVALAELCLSAPDVLILDEPTN 820
Cdd:PRK15064 390 DHAYDFENDLTLFDWMSQWRQEGDdEQAvRGTLGR--LLFSQDDIKksVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTN 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 821 NLDIESIDALAEAINEYEGGVIIVSHDerliRETGCTL--YVIE--DQTINEIVGEFDDY 876
Cdd:PRK15064 468 HMDMESIESLNMALEKYEGTLIFVSHD----REFVSSLatRIIEitPDGVVDFSGTYEEY 523
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
377-847 |
4.29e-66 |
|
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: 231.36 E-value: 4.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 377 GRRYGLVGPNGHGKTTLLRHIA--TRAF---AIP-PNIDVLLCEQEVVATDKTAINTILEADVRRT-EMLKKADELEKQF 449
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAgvDKDFngeARPqPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIkDALDRFNEISAKY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 450 VAGD------LTVQEELNDtfaELKAIGAYSAEAR------ARRILAGlgfskemqDRPTNKFSGGWRMRVSLARALYLE 517
Cdd:TIGR03719 111 AEPDadfdklAAEQAELQE---IIDAADAWDLDSQleiamdALRCPPW--------DADVTKLSGGERRRVALCRLLLSK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 518 PTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSmfkkMYVQKRREMIK 597
Cdd:TIGR03719 180 PDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS----SWLEQKQKRLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 598 EYEKQE----KRL-RELKAHGQSKKAAEKKQKESLTRKQEKNKSKQQKQDEDegpQELlarpkeYIvkfrfPEPSQLQPP 672
Cdd:TIGR03719 256 QEEKEEsarqKTLkRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNET---AEI------YI-----PPGPRLGDK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGRFDQhSGEHLTA 752
Cdd:TIGR03719 322 VIEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ-SRDALDP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 753 EES-------AAEYLQ---RLFNlphekARKALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNL 822
Cdd:TIGR03719 400 NKTvweeisgGLDIIKlgkREIP-----SRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
490 500
....*....|....*....|....*
gi 24641342 823 DIESIDALAEAINEYEGGVIIVSHD 847
Cdd:TIGR03719 475 DVETLRALEEALLNFAGCAVVISHD 499
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
366-875 |
2.16e-61 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 220.21 E-value: 2.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 366 LFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafaippniDVLLCEQEVV-ATDktAINTILEADVRR--------- 435
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG---------EVLLDDGRIIyEQD--LIVARLQQDPPRnvegtvydf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 436 -TEMLKKADELEKQFVAGDLTVQEELNDT----FAELKAI----GAYSAEARARRILAGLGFSKEMqdrPTNKFSGGWRM 506
Cdd:PRK11147 87 vAEGIEEQAEYLKRYHDISHLVETDPSEKnlneLAKLQEQldhhNLWQLENRINEVLAQLGLDPDA---ALSSLSGGWLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 507 RVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYsmfkK 586
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNY----D 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 587 MYVQKRREMIKEYEKQ--------------------------EKRLRELKAHGQSKKAaekkqkesltRKQEKNKSKQQK 640
Cdd:PRK11147 240 QYLLEKEEALRVEELQnaefdrklaqeevwirqgikarrtrnEGRVRALKALRRERSE----------RREVMGTAKMQV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 641 QDEDEGPQellarpkeyIVkfrfpepsqlqppiLGVHNVTFAFPsQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLL 720
Cdd:PRK11147 310 EEASRSGK---------IV--------------FEMENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 721 LGELEPQEGEQRKNHRLHVGRFDQHSGE---HLTAEESAAE----------------YLQRlFNLPHEKARkalgsfglv 781
Cdd:PRK11147 366 LGQLQADSGRIHCGTKLEVAYFDQHRAEldpEKTVMDNLAEgkqevmvngrprhvlgYLQD-FLFHPKRAM--------- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 782 shahtIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGGVIIVSHDERLIRETGCTLYVI 861
Cdd:PRK11147 436 -----TPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIF 510
|
570
....*....|....*
gi 24641342 862 E-DQTINEIVGEFDD 875
Cdd:PRK11147 511 EgNGKIGRYVGGYHD 525
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
381-847 |
5.58e-54 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 197.26 E-value: 5.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIA--TRAF---AIP-PNIDVLLCEQE-VVATDKTAINTILEADVRRTEMLKKADELEKQFvAGD 453
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAgvDKEFegeARPaPGIKVGYLPQEpQLDPEKTVRENVEEGVAEVKAALDRFNEIYAAY-AEP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 454 LTVQEELNDTFAELKAI----GAYSAEAR------ARRILAGlgfskemqDRPTNKFSGGWRMRVSLARALYLEPTLLML 523
Cdd:PRK11819 116 DADFDALAAEQGELQEIidaaDAWDLDSQleiamdALRCPPW--------DAKVTKLSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 524 DEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSmfkkMYVQKRREMIKEYEKQE 603
Cdd:PRK11819 188 DEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS----SWLEQKAKRLAQEEKQE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 604 ----KRL-REL-------KAhgqskkaaekkqkesltrKQEKNKSKQQKQDedegpqELLArpKEYIVKfrfPEPSQLQ- 670
Cdd:PRK11819 264 aarqKALkRELewvrqspKA------------------RQAKSKARLARYE------ELLS--EEYQKR---NETNEIFi 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 --PPILG-----VHNVTFAFpSQKPLFIKVDF-----GIdltsrVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLH 738
Cdd:PRK11819 315 ppGPRLGdkvieAENLSKSF-GDRLLIDDLSFslppgGI-----VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 739 VGRFDQhSGEHLTAEES-------AAEYLQ---RLFNlphekARKALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLS 808
Cdd:PRK11819 389 LAYVDQ-SRDALDPNKTvweeisgGLDIIKvgnREIP-----SRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQ 462
|
490 500 510
....*....|....*....|....*....|....*....
gi 24641342 809 APDVLILDEPTNNLDIESIDALAEAINEYEGGVIIVSHD 847
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHD 501
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
676-865 |
2.14e-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: 171.09 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGRFDQhsgehltaees 755
Cdd:cd03221 3 LENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 aaeylqrlfnlphekarkalgsfglvshahtikmkdLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAIN 835
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 24641342 836 EYEGGVIIVSHDERLIRETGCTLYVIEDQT 865
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
352-573 |
1.04e-44 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 157.61 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRafaippnidvllceqevvatdktaintilea 431
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGE------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 dvrrtemlKKADElekqfvaGDLTVQEELNdtfaelkaIGAYSaeararrilaglgfskemqdrptnKFSGGWRMRVSLA 511
Cdd:cd03221 50 --------LEPDE-------GIVTWGSTVK--------IGYFE------------------------QLSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 512 RALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKK 573
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
352-853 |
1.72e-43 |
|
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: 165.85 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFV--NANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNID----VLLCEQEVVAtdktai 425
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMG---LLPHGGRisgeVLLDGRDLLE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 426 ntiLEADVRRTEMLKKADELEKQFVAgdLTVQEELNDTFaELKAIGAYSAEARARRILAGLGFsKEMQDRPTNKFSGGWR 505
Cdd:COG1123 76 ---LSEALRGRRIGMVFQDPMTQLNP--VTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 506 MRVSLARALYLEPTLLMLDEPTNHLDL---NAVIWLDNYLQGWK-KTLLIVSHDQSFLDNVCNEIIHLDQKKlqyykgny 581
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVttqAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGR-------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 582 smfkkmyvqkrremIKEYEKQEKRLRElkahgqskkaaekkqkesltrkqeknkskqqkqdedegPQELLARPKEYIVKF 661
Cdd:COG1123 221 --------------IVEDGPPEEILAA--------------------------------------PQALAAVPRLGAARG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 662 RFPEPSQLQPPILGVHNVTFAFPSQKPLFIK-VDfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE------ 730
Cdd:COG1123 249 RAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRaVD-DVSLTlrrgETLGLVGESGSGKSTLARLLLGLLRPTSGSilfdgk 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 731 --------QRKNHRLHVGRFDQHSG----EHLTAEESAAEYLQRLFNLP----HEKARKALGSFGLVSHA-----HTikm 789
Cdd:COG1123 328 dltklsrrSLRELRRRVQMVFQDPYsslnPRMTVGDIIAEPLRLHGLLSraerRERVAELLERVGLPPDLadrypHE--- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 790 kdLSGGQKARVALAELCLSAPDVLILDEPTNNLDIeSI-----DALAEAINEYEGGVIIVSHDERLIRE 853
Cdd:COG1123 405 --LSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVqaqilNLLRDLQRELGLTYLFISHDLAVVRY 470
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
352-582 |
8.35e-41 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 157.92 E-value: 8.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRhiatrafaippnidvLLCEQevvatdktaintiLEA 431
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLK---------------LLAGE-------------LEP 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 D---VRRTEMLKKA------DELEkqfvaGDLTVQEELNDTFAELKaigaysaEARARRILAGLGFSKEMQDRPTNKFSG 502
Cdd:COG0488 368 DsgtVKLGETVKIGyfdqhqEELD-----PDKTVLDELRDGAPGGT-------EQEVRGYLGRFLFSGDDAFKPVGVLSG 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 503 GWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYS 582
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYD 515
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
672-863 |
7.57e-37 |
|
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: 137.61 E-value: 7.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRKNHRLHVGR 741
Cdd:COG4133 1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEvlwngepirdAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQHSG--EHLTAEESAAeYLQRLFNL--PHEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDE 817
Cdd:COG4133 80 LGHADGlkPELTVRENLR-FWAALYGLraDREAIDEALEAVGLAGLADL-PVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24641342 818 PTNNLDIESIDALAEAINEY--EGG-VIIVSHDERLIRetGCTLYVIED 863
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHlaRGGaVLLTTHQPLELA--AARVLDLGD 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
671-847 |
1.00e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILGVHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE------QRKNHRLHVG---- 740
Cdd:COG1121 4 MPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTvrlfgkPPRRARRRIGyvpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 741 RFDQHSGEHLTAEESAAEYLQR---LFNLP----HEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVL 813
Cdd:COG1121 83 RAEVDWDFPITVRDVVLMGRYGrrgLFRRPsradREAVDEALERVGLEDLADR-PIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 24641342 814 ILDEPTNNLDIESIDALAEAINEY--EG-GVIIVSHD 847
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHD 198
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
676-863 |
1.08e-31 |
|
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: 122.96 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQ-KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKNHRLHVGRFD 743
Cdd:cd03225 2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlvdgkdltklSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 744 QHSgEH----LTAEESAAeYLQRLFNLPHEKARK----ALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLIL 815
Cdd:cd03225 82 QNP-DDqffgPTVEEEVA-FGLENLGLPEEEIEErveeALELVGLEGLRDR-SPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24641342 816 DEPTNNLDIESIDALAEAINEY--EG-GVIIVSHDERLIRETGCTLYVIED 863
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
352-594 |
1.90e-31 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 123.43 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRafaIPPnidvllceqevvatDKTAInTILEA 431
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL---LKP--------------DSGSI-LIDGE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEmlkkaDELEKQ-FVAGD-------LTVQEELnDTFAELKAIGAYSAEARARRILAGLGFSKEMqDRPTNKFSGG 503
Cdd:COG4555 64 DVRKEP-----REARRQiGVLPDerglydrLTVRENI-RYFAELYGLFDEELKKRIEELIELLGLEEFL-DRRVGELSTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 504 WRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK---KTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYkGN 580
Cdd:COG4555 137 MKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKkegKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ-GS 215
|
250
....*....|....
gi 24641342 581 YSMFKKMYVQKRRE 594
Cdd:COG4555 216 LDELREEIGEENLE 229
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
676-850 |
2.13e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 122.86 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSqkplFIKVDfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRKNHRLHVGR 741
Cdd:COG1131 3 VRGLTKRYGD----KTALD-GVSLTvepgEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgedvarDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQHSG--EHLTAEEsAAEYLQRLFNLPHEKARK----ALGSFGLVSHAHTiKMKDLSGGQKARVALAeLCLSA-PDVLI 814
Cdd:COG1131 78 VPQEPAlyPDLTVRE-NLRFFARLYGLPRKEARErideLLELFGLTDAADR-KVGTLSGGMKQRLGLA-LALLHdPELLI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24641342 815 LDEPTNNLDIESIDALAEAINEY--EG-GVIIVSHD----ERL 850
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHYleeaERL 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
676-866 |
1.28e-30 |
|
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: 120.52 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrLHVGRFDqhsgehlTAEES 755
Cdd:COG1122 3 LENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGE------VLVDGKD-------ITKKN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 AAEYLQR-----------LFN---------------LPHEKARK----ALGSFGLVSHAHTIkMKDLSGGQKARVALAel 805
Cdd:COG1122 70 LRELRRKvglvfqnpddqLFAptveedvafgpenlgLPREEIRErveeALELVGLEHLADRP-PHELSGGQKQRVAIA-- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 806 clSA----PDVLILDEPTNNLDIESIDALAEAINEY--EG-GVIIVSHDERLIRETGCTLYVIEDQTI 866
Cdd:COG1122 147 --GVlamePEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
676-863 |
3.84e-30 |
|
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: 116.58 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSqKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrLHVGRFDqhsgehltaees 755
Cdd:cd00267 2 IENLSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE------ILIDGKD------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 aaeylqrLFNLPHEKARKalgSFGLVSHahtikmkdLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAIN 835
Cdd:cd00267 63 -------IAKLPLEELRR---RIGYVPQ--------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|.
gi 24641342 836 EY-EGG--VIIVSHDERLIRETGCTLYVIED 863
Cdd:cd00267 125 ELaEEGrtVIIVTHDPELAELAADRVIVLKD 155
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
676-863 |
5.93e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.99 E-value: 5.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRlhvgRFDQHSGE------- 748
Cdd:COG4619 3 LEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK----PLSAMPPPewrrqva 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 749 HLTAE-----ESAAEYLQRLFNLPH-----EKARKALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEP 818
Cdd:COG4619 78 YVPQEpalwgGTVRDNLPFPFQLRErkfdrERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24641342 819 TNNLDIESIDALAEAINEY----EGGVIIVSHDERLIRETGCTLYVIED 863
Cdd:COG4619 158 TSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
676-852 |
2.80e-29 |
|
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: 114.79 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIKvdfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrlhvGRFDQHSgehlt 751
Cdd:cd03228 3 FKNVSFSYPGRPKPVLK---DVSLTikpgEKVAIVGPSGSGKSTLLKLLLRLYDPTSGE---------ILIDGVD----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 752 aeesaaeylqrLFNLPHEKARKAlgsFGLVS-HAH----TIKmkD--LSGGQKARVALAELCLSAPDVLILDEPTNNLDI 824
Cdd:cd03228 66 -----------LRDLDLESLRKN---IAYVPqDPFlfsgTIR--EniLSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190
....*....|....*....|....*....|
gi 24641342 825 ESIDALAEAINEYEGG--VIIVSHDERLIR 852
Cdd:cd03228 130 ETEALILEALRALAKGktVIVIAHRLSTIR 159
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
676-886 |
1.03e-28 |
|
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: 115.34 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRKNHRLHVGRFDQH 745
Cdd:COG4555 4 VENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSilidgedvrkEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 746 SG--EHLTAEESAaEYLQRLFNLPHEKARKA----LGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPT 819
Cdd:COG4555 83 RGlyDRLTVRENI-RYFAELYGLFDEELKKRieelIELLGLEEFLDR-RVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 820 NNLDIESIDALAEAINEY---EGGVIIVSHDERLIRETGCTLYVI------EDQTINEIVGEF--DDYRKEVLDSLGE 886
Cdd:COG4555 161 NGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILhkgkvvAQGSLDELREEIgeENLEDAFVALIGS 238
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
693-820 |
1.28e-28 |
|
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: 111.97 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKNHRLHVGRFDQHSGE--HLTAEESAAEY 759
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltddERKSLRKEIGYVFQDPQLfpRLTVRENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 760 LQRLFNLPHEK---ARKALGSFGLVSHAHTI---KMKDLSGGQKARVALAELCLSAPDVLILDEPTN 820
Cdd:pfam00005 84 LLLKGLSKREKdarAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
676-847 |
1.99e-28 |
|
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: 113.78 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQR------KNHRLHVGRFDQHSG-E 748
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSiD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 749 H---LTAEESAAEYLQRLFNLPH-------EKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEP 818
Cdd:cd03235 81 RdfpISVRDVVLMGLYGHKGLFRrlskadkAKVDEALERVGLSELADR-QIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190
....*....|....*....|....*....|..
gi 24641342 819 TNNLDIESIDALAEAINEY--EG-GVIIVSHD 847
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELrrEGmTILVVTHD 191
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
369-571 |
6.60e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.85 E-value: 6.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPnidvllceqevvaTDKTAinTILEADVRR--TEMLKK----A 442
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG---LLRP-------------TSGEV--RVLGEDVARdpAEVRRRigyvP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 443 DELekqFVAGDLTVQEELnDTFAELKAIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVSLARALYLEPTLLM 522
Cdd:COG1131 80 QEP---ALYPDLTVRENL-RFFARLYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24641342 523 LDEPTNHLDLNAVIWLDNYLQGWK---KTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAaegKTVLLSTHYLEEAERLCDRVAIIDK 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
673-847 |
1.33e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 112.44 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSqKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----QRKNHRLHVGRF------ 742
Cdd:COG1120 1 MLEAENLSVGYGG-RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldGRDLASLSRRELarriay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 743 ---DQHSGEHLTAEESAA----EYLQRLFNLP---HEKARKALGSFGLVSHAHTIkMKDLSGGQKARVALAELCLSAPDV 812
Cdd:COG1120 80 vpqEPPAPFGLTVRELVAlgryPHLGLFGRPSaedREAVEEALERTGLEHLADRP-VDELSGGERQRVLIARALAQEPPL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 24641342 813 LILDEPTNNLDI----ESIDALAEAINEYEGGVIIVSHD 847
Cdd:COG1120 159 LLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD 197
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
352-574 |
6.16e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.14 E-value: 6.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNI-DVLLceqevvatDKTAINTILE 430
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAD---LDPPTSgEIYL--------DGKPLSAMPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 ADVRRTEMLKKAdelEKQFVAGdlTVQEELNDTFaelKAIGAYSAEARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSL 510
Cdd:COG4619 70 PEWRRQVAYVPQ---EPALWGG--TVRDNLPFPF---QLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 511 ARALYLEPTLLMLDEPTNHLDLN---AVI-WLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPEntrRVEeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
352-576 |
1.60e-26 |
|
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: 108.57 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTIS-AKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKtaintile 430
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN--GLLKPTSGEVLVDGKDITKKNL-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 ADVRRT--------EMlkkadelekQFVAGdlTVQEELndTFAeLKAIGAYSAEARAR--RILAGLGFSkEMQDRPTNKF 500
Cdd:COG1122 71 RELRRKvglvfqnpDD---------QLFAP--TVEEDV--AFG-PENLGLPREEIRERveEALELVGLE-HLADRPPHEL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK---KTLLIVSHDQSFLDNVCNEIIHLDQKKLQY 576
Cdd:COG1122 136 SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
676-866 |
2.69e-26 |
|
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: 106.33 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFikvdfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRKNHRLHVGR 741
Cdd:cd03230 3 VRNLSKRYGKKTALD-----DISLTvekgEIYGLLGPNGAGKTTLIKIILGLLKPDSGEikvlgkdikkEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQHSG--EHLTAEEsaaeylqrlfNLphekarkalgsfglvshahtikmkDLSGGQKARVALAELCLSAPDVLILDEPT 819
Cdd:cd03230 78 LPEEPSlyENLTVRE----------NL------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24641342 820 NNLDIESIDALAEAINEY--EGG-VIIVSHDERLIrETGCT-LYVIEDQTI 866
Cdd:cd03230 124 SGLDPESRREFWELLRELkkEGKtILLSSHILEEA-ERLCDrVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
649-852 |
4.02e-26 |
|
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: 114.93 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 649 ELLARPKEYIVKFRFPEPSQLQPPIlGVHNVTFAFPSQKPLFIKvdfGIDLT----SRVAIVGPNGVGKSTFLKLLLGEL 724
Cdd:COG2274 450 DILDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGDSPPVLD---NISLTikpgERVAIVGRSGSGKSTLLKLLLGLY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 725 EPQEGEqrknhrlhVgRFDQHSGEHLtaeeSAAEY-------LQ--RLFN-------------LPHEKARKALGSFGLvs 782
Cdd:COG2274 526 EPTSGR--------I-LIDGIDLRQI----DPASLrrqigvvLQdvFLFSgtirenitlgdpdATDEEIIEAARLAGL-- 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 783 HAHTIKMKD------------LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHDE 848
Cdd:COG2274 591 HDFIEALPMgydtvvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRL 670
|
....
gi 24641342 849 RLIR 852
Cdd:COG2274 671 STIR 674
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
670-893 |
4.50e-26 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 107.76 E-value: 4.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 670 QPPILGVHNVTFAFPSQKPLfikvDfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE--------------Q 731
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVL----D-GVSLDvprgEILAIIGGSGSGKSVLLKLIIGLLRPDSGEilvdgqditglsekE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 732 RKNHRLHVGRFDQHSG--EHLTAEESAAEYLQRLFNLP----HEKARKALGSFGLVSHAHtiKM-KDLSGGQKARVALAE 804
Cdd:COG1127 77 LYELRRRIGMLFQGGAlfDSLTVFENVAFPLREHTDLSeaeiRELVLEKLELVGLPGAAD--KMpSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 805 -LCLSaPDVLILDEPTNNLDIESIDALAEAINE----YEGGVIIVSHDERLIRETGCTLYVIEDQTIneivgEFDDYRKE 879
Cdd:COG1127 155 aLALD-PEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADRVAVLADGKI-----IAEGTPEE 228
|
250
....*....|....
gi 24641342 880 VLDSlgevvNNPSV 893
Cdd:COG1127 229 LLAS-----DDPWV 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
670-868 |
4.67e-26 |
|
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: 113.71 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 670 QPPILGVHNVTFAFPSQKPLFIKvdfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNH---------- 735
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGRPVLD---GLSLTlppgERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldedd 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 736 -RLHVGRFDQHSgeHLTAEeSAAEYLqRLFN--LPHEKARKALGSFGLvsHAHTIKMKD------------LSGGQKARV 800
Cdd:COG4987 407 lRRRIAVVPQRP--HLFDT-TLRENL-RLARpdATDEELWAALERVGL--GDWLAALPDgldtwlgeggrrLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 801 ALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHDERLIrETGCTLYVIEDQTINE 868
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGL-ERMDRILVLEDGRIVE 549
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
676-847 |
4.71e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 105.60 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPsQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrlhVgRFDQHSGEHLTAEES 755
Cdd:cd03214 2 VENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE--------I-LLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 AaeylQRLFNLPhekarKALGSFGLVSHAHTIkMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDI----ESIDALA 831
Cdd:cd03214 72 A----RKIAYVP-----QALELLGLAHLADRP-FNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLR 141
|
170
....*....|....*.
gi 24641342 832 EAINEYEGGVIIVSHD 847
Cdd:cd03214 142 RLARERGKTVVMVLHD 157
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
353-573 |
6.00e-26 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 104.63 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 353 KIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEvvatdktaintilead 432
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA--GLLKPTSGEILIDGKD---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 433 vrrtemlkkadelekqfvagdltvqeelndtfaelkaIGAYSAEARARRIlaGLGFSkemqdrptnkFSGGWRMRVSLAR 512
Cdd:cd00267 63 -------------------------------------IAKLPLEELRRRI--GYVPQ----------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 513 ALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK---TLLIVSHDQSFLDNVCNEIIHLDQKK 573
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
353-573 |
9.48e-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: 106.01 E-value: 9.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 353 KIENFTISAKGND--LFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTAINtile 430
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLN--GLLGPTSGEVLVDGKDLTKLSLKELR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 advRRTEMLkkadeL---EKQFVAgdLTVQEELNdtFA-ELKAIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGWRM 506
Cdd:cd03225 75 ---RKVGLV-----FqnpDDQFFG--PTVEEEVA--FGlENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 507 RVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK---KTLLIVSHDQSFLDNVCNEIIHLDQKK 573
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
648-875 |
1.05e-25 |
|
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: 112.54 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 648 QELLARPKEYI----VKFRFPEPSQLQppilgVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGE 723
Cdd:COG4988 312 FALLDAPEPAApagtAPLPAAGPPSIE-----LEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 724 LEPQEGEQRKNH-----------RLHVGRFDQHSgeHL----------------TAEE--------SAAEYLQRLFNLPH 768
Cdd:COG4988 387 LPPYSGSILINGvdlsdldpaswRRQIAWVPQNP--YLfagtirenlrlgrpdaSDEEleaaleaaGLDEFVAALPDGLD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 769 EKarkaLGSFGLvshahtikmkDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSH 846
Cdd:COG4988 465 TP----LGEGGR----------GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITH 530
|
250 260
....*....|....*....|....*....
gi 24641342 847 DERLIRETGCTLyVIEDQTINEiVGEFDD 875
Cdd:COG4988 531 RLALLAQADRIL-VLDDGRIVE-QGTHEE 557
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
678-863 |
2.96e-25 |
|
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: 104.88 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQK-PLFI--KVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQR---------KNHRL------HV 739
Cdd:cd03255 5 NLSKTYGGGGeKVQAlkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisklSEKELaafrrrHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GR-FDQHSG-EHLTAEES---AAEYLQRLFNLPHEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLI 814
Cdd:cd03255 85 GFvFQSFNLlPDLTALENvelPLLLAGVPKKERRERAEELLERVGLGDRLNH-YPSELSGGQQQRVAIARALANDPKIIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24641342 815 LDEPTNNLDIES----IDALAEaINEYEG-GVIIVSHDERLIRETGCTLYvIED 863
Cdd:cd03255 164 ADEPTGNLDSETgkevMELLRE-LNKEAGtTIVVVTHDPELAEYADRIIE-LRD 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
353-577 |
1.19e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 101.74 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 353 KIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRhiatrafaippnidvllceqevvatdktAINTILEAD 432
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLK----------------------------TLAGLLKPS 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 433 vrrtemlkkadelekqfvAGDLTVQEelndtfaelKAIGAYSAEARARRI------LAGLGFSkEMQDRPTNKFSGGWRM 506
Cdd:cd03214 53 ------------------SGEILLDG---------KDLASLSPKELARKIayvpqaLELLGLA-HLADRPFNELSGGERQ 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 507 RVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK----KTLLIVSHDQSFLDNVCNEIIHLDQKKLQYY 577
Cdd:cd03214 105 RVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLArergKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
674-854 |
1.30e-24 |
|
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: 102.05 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAfPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRlHVGRFDQHSGEH---- 749
Cdd:TIGR01189 1 LAARNLACS-RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-PLAEQRDEPHENilyl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 750 -----LTAEESAAEYLQ---RLFNLPHEKARKALGSFGLVSHAHTIkMKDLSGGQKARVALAELCLSAPDVLILDEPTNN 821
Cdd:TIGR01189 79 ghlpgLKPELSALENLHfwaAIHGGAQRTIEDALAAVGLTGFEDLP-AAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 24641342 822 LDIESIDALAEAINEY---EGGVIIVSHDERLIRET 854
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHlarGGIVLLTTHQDLGLVEA 193
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
352-576 |
2.07e-24 |
|
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: 101.89 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRrYGLVGPNGHGKTTLLRHIATrafAIPPNI-DVLLCEQEVVAtdktaintile 430
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILAT---LTPPSSgTIRIDGQDVLK----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 advRRTEMLKKADELEKQF-VAGDLTVQEELnDTFAELKAIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVS 509
Cdd:cd03264 66 ---QPQKLRRRIGYLPQEFgVYPNFTVREFL-DYIAWLKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 510 LARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQ--GWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQY 576
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSelGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
352-573 |
2.46e-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: 101.79 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNI-DVLLCEQEVvatdktainTILE 430
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG---LLPPSAgEVLWNGEPI---------RDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 ADVRRtEMLKKADELEkqfVAGDLTVQEELnDTFAELKaiGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVSL 510
Cdd:COG4133 71 EDYRR-RLAYLGHADG---LKPELTVRENL-RFWAALY--GLRADREAIDEALEAVGLA-GLADLPVRQLSAGQKRRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 511 ARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK---TLLIVSHDQSFLDNVcnEIIHLDQKK 573
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQPLELAAA--RVLDLGDFK 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
677-853 |
4.03e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.67 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 677 HNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKN---HRLHVGR- 741
Cdd:COG2884 5 ENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngqdlsrlKRREipyLRRRIGVv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 F-DQHSGEHLTAEESAAEYLqRLFNLPHEKARK----ALGSFGLVSHAHtiKMKD-LSGGQKARVALAELCLSAPDVLIL 815
Cdd:COG2884 85 FqDFRLLPDRTVYENVALPL-RVTGKSRKEIRRrvreVLDLVGLSDKAK--ALPHeLSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24641342 816 DEPTNNLDIES---IDALAEAINEYEGGVIIVSHDERLIRE 853
Cdd:COG2884 162 DEPTGNLDPETsweIMELLEEINRRGTTVLIATHDLELVDR 202
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
676-851 |
7.91e-24 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 100.02 E-value: 7.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE--------QRKNHRLHVGRFDQHSG 747
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSillngkpiKAKERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 748 EHLTAEESAAEYLQRLFNLP--HEKARKALGSFGLvshaHTIKMK---DLSGGQKARVALAELCLSAPDVLILDEPTNNL 822
Cdd:cd03226 82 YQLFTDSVREELLLGLKELDagNEQAETVLKDLDL----YALKERhplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190
....*....|....*....|....*....|..
gi 24641342 823 DIESIDALAEAINEY--EGGVIIV-SHDERLI 851
Cdd:cd03226 158 DYKNMERVGELIRELaaQGKAVIViTHDYEFL 189
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
676-878 |
1.34e-23 |
|
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: 100.27 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFikvdfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGE--------------QRKNHRL 737
Cdd:cd03261 3 LRGLTKSFGGRTVLK-----GVDLDVRrgeiLAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidgedisglseaELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 HVGRFDQHSG--EHLTAEESAAEYLQRLFNLPH----EKARKALGSFGLvSHAHTIKMKDLSGGQKARVALAELCLSAPD 811
Cdd:cd03261 78 RMGMLFQSGAlfDSLTVFENVAFPLREHTRLSEeeirEIVLEKLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 812 VLILDEPTNNLDIESIDALAEAIN----EYEGGVIIVSHDERLIRETGCTLYVIEDQTInEIVGEFDDYRK 878
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIADRIAVLYDGKI-VAEGTPEELRA 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
369-528 |
2.64e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 96.95 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLceqevvatDKTAINTILEADVRRT-EMLKKADELEk 447
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIA--GLLSPTEGTILL--------DGQDLTDDERKSLRKEiGYVFQDPQLF- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 448 qfvaGDLTVQEELnDTFAELKAIGAYSAEARARRILAGLG---FSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLD 524
Cdd:pfam00005 72 ----PRLTVRENL-RLGLLLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLD 146
|
....
gi 24641342 525 EPTN 528
Cdd:pfam00005 147 EPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
671-850 |
3.46e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.96 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILGVHNVTFAFPSQKPLFIKVDfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE--------------QR 732
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALR-GVSLSieagEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvlidgqdisslserEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 733 KNHRL-HVGrF-DQHSG--EHLTAEES---AAEYLQRLFNLPHEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAEL 805
Cdd:COG1136 81 ARLRRrHIG-FvFQFFNllPELTALENvalPLLLAGVSRKERRERARELLERVGLGDRLDH-RPSQLSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24641342 806 CLSAPDVLILDEPTNNLDIES----IDALAEAINEYEGGVIIVSHDERL 850
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPEL 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
674-845 |
4.46e-23 |
|
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: 98.03 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQKPLfikVDFGIDLTSRV-AIVGPNGVGKSTFLKLLLGELEPQEG----------EQRKNHRLHVGRF 742
Cdd:cd03264 1 LQLENLTKRYGKKRAL---DGVSLTLGPGMyGLLGPNGAGKTTLMRILATLTPPSSGtiridgqdvlKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 743 DQHSG--EHLTAEEsAAEYLQRLFNLPHEKARK----ALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILD 816
Cdd:cd03264 78 PQEFGvyPNFTVRE-FLDYIAWLKGIPSKEVKArvdeVLELVNLGDRAKK-KIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190
....*....|....*....|....*....|
gi 24641342 817 EPTNNLDIESIDALAEAINEY-EGGVIIVS 845
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELgEDRIVILS 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
676-852 |
5.64e-23 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 104.65 E-value: 5.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGR-------------F 742
Cdd:PRK11147 6 IHGAWLSF-SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdpprnvegtvY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 743 D------QHSGEHLTA-----EESAAEYLQRLFN--------LPHE-------KARKALGSFGLVSHAhtiKMKDLSGGQ 796
Cdd:PRK11147 85 DfvaegiEEQAEYLKRyhdisHLVETDPSEKNLNelaklqeqLDHHnlwqlenRINEVLAQLGLDPDA---ALSSLSGGW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 797 KARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGGVIIVSHDERLIR 852
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIR 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
703-846 |
8.21e-23 |
|
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: 97.29 E-value: 8.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEGEQR-------KNH--RLHVGRFDQHSG--EHLTAEEsAAEYLQRLFNLPHEKA 771
Cdd:cd03268 29 YGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqKNIeaLRRIGALIEAPGfyPNLTARE-NLRLLARLLGIRKKRI 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 772 RKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAI---NEYEGGVIIVSH 846
Cdd:cd03268 108 DEVLDVVGLKDSAKK-KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELIlslRDQGITVLISSH 184
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
352-555 |
9.13e-23 |
|
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: 98.58 E-value: 9.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtRAfaIPPNI-DVLLCEQEVvatdktaintile 430
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-GL--LKPSSgEVLLDGRDL------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 ADVRRTEMLKK----ADELEkqfVAGDLTVQeelnDT-----FAELKAIGAYSAE--ARARRILAGLGFSkEMQDRPTNK 499
Cdd:COG1120 66 ASLSRRELARRiayvPQEPP---APFGLTVR----ELvalgrYPHLGLFGRPSAEdrEAVEEALERTGLE-HLADRPVDE 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 500 FSGGWRMRVSLARALYLEPTLLMLDEPTNHLDL-NAVIWLD-----NYLQGwkKTLLIVSHD 555
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLaHQLEVLEllrrlARERG--RTVVMVLHD 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
352-574 |
9.46e-23 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 95.93 E-value: 9.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNidvllcEQEVvatdktainTILEA 431
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG---LLKPD------SGEI---------KVLGK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEMLKKAD---ELEKQFVAGDLTVQEELndtfaelkaigaysaeararrilaglgfskemqdrptnKFSGGWRMRV 508
Cdd:cd03230 63 DIKKEPEEVKRRigyLPEEPSLYENLTVRENL--------------------------------------KLSGGMKQRL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 509 SLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK---KTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:cd03230 105 ALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
664-853 |
1.16e-22 |
|
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: 103.14 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 664 PEPSQLQ-----PPILGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKN---- 734
Cdd:TIGR02857 307 PLAGKAPvtaapASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNgvpl 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 735 -------HRLHVGRFDQHSgeHLTA------------EESAAEYLQRLfnlphekARKALGSF--GLVSHAHTIKMKD-- 791
Cdd:TIGR02857 387 adadadsWRDQIAWVPQHP--FLFAgtiaenirlarpDASDAEIREAL-------ERAGLDEFvaALPQGLDTPIGEGga 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 792 -LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHDERLIRE 853
Cdd:TIGR02857 458 gLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALAAL 522
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
682-853 |
2.12e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 682 AFPSQkPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGRFDQHSGEH----LTAEESAA 757
Cdd:NF040873 1 GYGGR-PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPdslpLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 758 -------EYLQRLFNLPHEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDAL 830
Cdd:NF040873 80 mgrwarrGLWRRLTRDDRAAVDDALERVGLADLAGR-QLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|....*.
gi 24641342 831 AEAINEYEG---GVIIVSHDERLIRE 853
Cdd:NF040873 159 IALLAEEHArgaTVVVVTHDLELVRR 184
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
677-855 |
4.10e-22 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 95.39 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 677 HNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKN----HRLH---VGRFDQHSG-- 747
Cdd:TIGR02673 5 HNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAgedvNRLRgrqLPLLRRRIGvv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 748 -------EHLTAEESAAEYLQ---RLFNLPHEKARKALGSFGLVSHAHTIKMKdLSGGQKARVALAELCLSAPDVLILDE 817
Cdd:TIGR02673 85 fqdfrllPDRTVYENVALPLEvrgKKEREIQRRVGAALRQVGLEHKADAFPEQ-LSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24641342 818 PTNNLD---IESIDALAEAINEYEGGVIIVSHDERLIRETG 855
Cdd:TIGR02673 164 PTGNLDpdlSERILDLLKRLNKRGTTVIVATHDLSLVDRVA 204
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
678-847 |
5.52e-22 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 100.74 E-value: 5.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSqKPLF--IKVDFGIDltSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRK--NHRLHVGRFDQHSGEHLT-- 751
Cdd:PRK15064 6 NITMQFGA-KPLFenISVKFGGG--NRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdpNERLGKLRQDQFAFEEFTvl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 752 -----------------------AEESAAEYLqRLFNLPHE-----------KARKALGSFGLVSHAHTIKMKDLSGGQK 797
Cdd:PRK15064 83 dtvimghtelwevkqerdriyalPEMSEEDGM-KVADLEVKfaemdgytaeaRAGELLLGVGIPEEQHYGLMSEVAPGWK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24641342 798 ARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGGVIIVSHD 847
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHD 211
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
665-846 |
5.95e-22 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 94.92 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 665 EPSQLQPPILGVHNVTFAfPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQR----KNHRLHVG 740
Cdd:PRK13543 3 EPLHTAPPLLAAHALAFS-RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQidgkTATRGDRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 741 RFDQHSGE--HLTAEESAAEYLQRLFNLPHEKARK----ALGSFGLVSHAHTIkMKDLSGGQKARVALAELCLSAPDVLI 814
Cdd:PRK13543 82 RFMAYLGHlpGLKADLSTLENLHFLCGLHGRRAKQmpgsALAIVGLAGYEDTL-VRQLSAGQKKRLALARLWLSPAPLWL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 24641342 815 LDEPTNNLDIESIDALAEAINEY---EGGVIIVSH 846
Cdd:PRK13543 161 LDEPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
352-574 |
6.64e-22 |
|
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: 94.59 E-value: 6.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNidvllceqEVVATDKTAINTILEA 431
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILG---LIKPD--------SGEITFDGKSYQKNIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEMLkkadeLEKQFVAGDLTVQEELndtfaELKAIGAYSAEARARRILAGLGFsKEMQDRPTNKFSGGWRMRVSLA 511
Cdd:cd03268 70 ALRRIGAL-----IEAPGFYPNLTARENL-----RLLARLLGIRKKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 512 RALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK---TLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
673-869 |
7.45e-22 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 95.27 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKpLFIKVDFGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE--------------QRKN 734
Cdd:cd03257 1 LLEVKNLSVSFPTGG-GSVKALDDVSFSikkgETLGLVGESGSGKSTLARAILGLLKPTSGSiifdgkdllklsrrLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 735 HRLHVGRFDQHSGE----HLTAEESAAEYLQRLFNLPHEKARKALGSFGLVSHAHTIKMKD-----LSGGQKARVALAE- 804
Cdd:cd03257 80 RRKEIQMVFQDPMSslnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIARa 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 805 LCLSaPDVLILDEPTNNLDIES----IDALAEAINEYEGGVIIVSHDERLIRETGCTLYVIEDQTINEI 869
Cdd:cd03257 160 LALN-PKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
352-571 |
1.11e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 95.26 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTIS--AKGNDLFV--NANLLIAHGRRYGLVGPNGHGKTTLLRhiatrafaippnidvLLCEQEVVATDKTAINT 427
Cdd:COG1124 2 LEVRNLSVSygQGGRRVPVlkDVSLEVAPGESFGLVGESGSGKSTLLR---------------ALAGLERPWSGEVTFDG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 428 ILEADVRRTEMLKKAdelekQFVAGD--------LTVQEELndtfAE-LKAIGAYSAEARARRILAGLGFSKEMQDRPTN 498
Cdd:COG1124 67 RPVTRRRRKAFRRRV-----QMVFQDpyaslhprHTVDRIL----AEpLRIHGLPDREERIAELLEQVGLPPSFLDRYPH 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 499 KFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLN--AVIWldNYLQGWKK----TLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:COG1124 138 QLSGGQRQRVAIARALILEPELLLLDEPTSALDVSvqAEIL--NLLKDLREerglTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
703-847 |
2.21e-21 |
|
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: 93.72 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRKNHRLHVGRFDQHSG--EHLTAEESAaEYLQRLFNLPHEK 770
Cdd:cd03263 31 FGLLGHNGAGKTTTLKMLTGELRPTSGTayingysirtDRKAARQSLGYCPQFDAlfDELTVREHL-RFYARLKGLPKSE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 771 ARKA----LGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIV 844
Cdd:cd03263 110 IKEEvellLRVLGLTDKANK-RARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGrsIILT 188
|
...
gi 24641342 845 SHD 847
Cdd:cd03263 189 THS 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
693-853 |
2.67e-21 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 93.66 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNH---RLHVGRFDQHSG--EHLTAEES--- 755
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSvlfdgeditGLPPHeiaRLGIGRTFQIPRlfPELTVLENvmv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 AAEYLQRLFNLPH----------EKARKALGSFGLVSHAHTIkMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIE 825
Cdd:cd03219 99 AAQARTGSGLLLArarreerearERAEELLERVGLADLADRP-AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180 190
....*....|....*....|....*....|.
gi 24641342 826 SIDALAE---AINEYEGGVIIVSHDERLIRE 853
Cdd:cd03219 178 ETEELAElirELRERGITVLLVEHDMDVVMS 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
676-883 |
3.33e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 93.71 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIKVDfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKNHRLHVG 740
Cdd:COG1124 4 VRNLSVSYGQGGRRVPVLK-DVSLEvapgESFGLVGESGSGKSTLLRALAGLERPWSGEvtfdgrpvtrrRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 741 RFDQHSGE----HLTAEESAAEYLqRLFNLPHEKAR--KALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLI 814
Cdd:COG1124 83 MVFQDPYAslhpRHTVDRILAEPL-RIHGLPDREERiaELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 815 LDEPTNNLDI----ESIDALAEAINEYEGGVIIVSHDERLIR---------ETGCtlyVIEDQTINEIVGEF-DDYRKEV 880
Cdd:COG1124 162 LDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAhlcdrvavmQNGR---IVEELTVADLLAGPkHPYTREL 238
|
...
gi 24641342 881 LDS 883
Cdd:COG1124 239 LAA 241
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
674-854 |
4.49e-21 |
|
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: 91.12 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFP-SQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKN----HRLHVGRFDQHSGe 748
Cdd:cd03246 1 LEVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDgadiSQWDPNELGDHVG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 749 hltaeesaaeYL-Q--RLFnlphekarkalgsfglvshAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIE 825
Cdd:cd03246 80 ----------YLpQddELF-------------------SGSIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190
....*....|....*....|....*....|..
gi 24641342 826 SIDALAEAINEYEGG---VIIVSHDERLIRET 854
Cdd:cd03246 131 GERALNQAIAALKAAgatRIVIAHRPETLASA 162
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
678-854 |
7.72e-21 |
|
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: 91.70 E-value: 7.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKN-------HRLHVGRFDQHSG--- 747
Cdd:cd03292 5 NVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRKIGvvf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 748 ------EHLTAEESAAEYLqRLFNLPHEKARK----ALGSFGLVSHAHTIKMKdLSGGQKARVALAELCLSAPDVLILDE 817
Cdd:cd03292 85 qdfrllPDRNVYENVAFAL-EVTGVPPREIRKrvpaALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24641342 818 PTNNLDIES---IDALAEAINEYEGGVIIVSHDERLIRET 854
Cdd:cd03292 163 PTGNLDPDTtweIMNLLKKINKAGTTVVVATHAKELVDTT 202
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
676-863 |
7.75e-21 |
|
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: 90.71 E-value: 7.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPsQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrlhvGRFDqhsGEHLTAEes 755
Cdd:cd03229 3 LKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS---------ILID---GEDLTDL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 aaeylqrlfNLPHEKARKALG----SFGLVSHAhTIK---MKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIE--- 825
Cdd:cd03229 68 ---------EDELPPLRRRIGmvfqDFALFPHL-TVLeniALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPItrr 137
|
170 180 190
....*....|....*....|....*....|....*....
gi 24641342 826 SIDALAEAINEYEG-GVIIVSHDERLIRETGCTLYVIED 863
Cdd:cd03229 138 EVRALLKSLQAQLGiTVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
676-853 |
1.01e-20 |
|
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: 92.25 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKN---HRLHVGR 741
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSvlidgtdinklKGKAlrqLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 -FDQHsgeHLTAEESAAE-----------YLQRLFNLPHE----KARKALGSFGLVSHAHTiKMKDLSGGQKARVALAEL 805
Cdd:cd03256 83 iFQQF---NLIERLSVLEnvlsgrlgrrsTWRSLFGLFPKeekqRALAALERVGLLDKAYQ-RADQLSGGQQQRVAIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24641342 806 CLSAPDVLILDEPTNNLDIES----IDALAEAINEYEGGVIIVSHDERLIRE 853
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQVDLARE 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
374-576 |
1.14e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 91.28 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 374 IAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNIDVLLCEQEVVATDKTAINtileadvRRTEMLKKADELEKQfvagd 453
Cdd:cd03266 28 VKPGEVTGLLGPNGAGKTTTLRMLAG---LLEPDAGFATVDGFDVVKEPAEAR-------RRLGFVSDSTGLYDR----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 454 LTVQEELnDTFAELKAIGAYSAEARARRILAGLGFsKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLN 533
Cdd:cd03266 93 LTARENL-EYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24641342 534 AVIWLDNYLQGWK---KTLLIVSHDQSFLDNVCNEIIHLDQKKLQY 576
Cdd:cd03266 171 ATRALREFIRQLRalgKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
352-576 |
1.27e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPP---NIDVLLCEQEVVATD------K 422
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG---LLPPtsgTVRLFGKPPRRARRRigyvpqR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 423 TAINTILEADVRrtemlkkadelekQFVA-GdltvqeelndTFAELKAIGAYSAE--ARARRILAGLGFSkEMQDRPTNK 499
Cdd:COG1121 84 AEVDWDFPITVR-------------DVVLmG----------RYGRRGLFRRPSRAdrEAVDEALERVGLE-DLADRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 500 FSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK---KTLLIVSHDQSFLDNVCNEIIHLDQKKLQY 576
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRregKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
352-557 |
1.29e-20 |
|
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: 91.04 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVvatdktainTILEA 431
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA--GLERPDSGEILIDGRDV---------TGVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEMLKkadelekQFVA--GDLTVQEelNDTFA-ELKAIGAYSAEARARRILAGLGFSKEMqDRPTNKFSGGWRMRV 508
Cdd:cd03259 70 ERRNIGMVF-------QDYAlfPHLTVAE--NIAFGlKLRGVPKAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24641342 509 SLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQG----WKKTLLIVSHDQS 557
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQE 192
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
678-846 |
2.01e-20 |
|
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: 90.73 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG-------EQRKNH----RLHVGRFDQH 745
Cdd:cd03245 7 NVSFSYPNQEIPALDnVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsvlldgtDIRQLDpadlRRNIGYVPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 746 SgeHL---TAEESAAeylqrLFNLPHEKAR--KALGSFGLVS----HAHTIKMK------DLSGGQKARVALAELCLSAP 810
Cdd:cd03245 87 V--TLfygTLRDNIT-----LGAPLADDERilRAAELAGVTDfvnkHPNGLDLQigergrGLSGGQRQAVALARALLNDP 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 24641342 811 DVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSH 846
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITH 197
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
351-574 |
2.47e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 96.44 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 351 DIKIEN--FTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLceqevvatDKTAINTI 428
Cdd:COG2274 473 DIELENvsFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL--GLYEPTSGRILI--------DGIDLRQI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 429 LEADVRRtemlkkadelekQFvaGDLTVQEEL-NDTFAELKAIGAYSA-EARARRIL--AGL---------GFSKEMQDR 495
Cdd:COG2274 543 DPASLRR------------QI--GVVLQDVFLfSGTIRENITLGDPDAtDEEIIEAArlAGLhdfiealpmGYDTVVGEG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 496 PTNkFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLN--AVIW--LDNYLQGWkkTLLIVSHDQSFLDNvCNEIIHLDQ 571
Cdd:COG2274 609 GSN-LSGGQRQRLAIARALLRNPRILILDEATSALDAEteAIILenLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDK 684
|
...
gi 24641342 572 KKL 574
Cdd:COG2274 685 GRI 687
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
351-570 |
2.48e-20 |
|
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: 91.41 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 351 DIKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPnidvllcEQEVVATDKTAINTIle 430
Cdd:TIGR03873 1 GLRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAG---ALRP-------DAGTVDLAGVDLHGL-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 adVRRTEMLKKADELEKQFVAGDLTVQE--ELNDTfAELKAIGAYSAE--ARARRILAGLGFSkEMQDRPTNKFSGGWRM 506
Cdd:TIGR03873 69 --SRRARARRVALVEQDSDTAVPLTVRDvvALGRI-PHRSLWAGDSPHdaAVVDRALARTELS-HLADRDMSTLSGGERQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 507 RVSLARALYLEPTLLMLDEPTNHLDLNA---VIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLD 570
Cdd:TIGR03873 145 RVHVARALAQEPKLLLLDEPTNHLDVRAqleTLALVRELAATGVTVVAALHDLNLAASYCDHVVVLD 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
687-845 |
3.07e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 687 KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGeqrknhRLHVGRFDQHSGEH------------LTAEE 754
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAG------TIKLDGGDIDDPDVaeachylghrnaMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 755 SAAEYLQ---RLFNLPHEKARKALGSFGLvSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALA 831
Cdd:PRK13539 89 TVAENLEfwaAFLGGEELDIAAALEAVGL-APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
170
....*....|....*.
gi 24641342 832 EAINEY--EGGVIIVS 845
Cdd:PRK13539 168 ELIRAHlaQGGIVIAA 183
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
369-567 |
5.97e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 94.58 E-value: 5.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNI-DVLLCEQEVVATDKTAINTileadvRRTEMlkkadelek 447
Cdd:COG1123 283 DVSLTLRRGETLGLVGESGSGKSTLARLLLG---LLRPTSgSILFDGKDLTKLSRRSLRE------LRRRV--------- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 448 QFVAGD--------LTVQEELndtfAE-LKAIGAYSAEARARRILAGL---GFSKEMQDRPTNKFSGGWRMRVSLARALY 515
Cdd:COG1123 345 QMVFQDpysslnprMTVGDII----AEpLRLHGLLSRAERRERVAELLervGLPPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 516 LEPTLLMLDEPTNHLD-------LNAviwLDNYLQGWKKTLLIVSHDQSFLDNVCNEII 567
Cdd:COG1123 421 LEPKLLILDEPTSALDvsvqaqiLNL---LRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
672-868 |
6.41e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 94.20 E-value: 6.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQ---EGEQRKNHRLHVGRFDQHSG 747
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVPAVDgVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 748 EH--------------LTAEESAAEYLqRLFNLPHEKAR-KALGSFGLVSHAHTIKMK--DLSGGQKARVALAELCLSAP 810
Cdd:COG1123 83 RRigmvfqdpmtqlnpVTVGDQIAEAL-ENLGLSRAEARaRVLELLEAVGLERRLDRYphQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 811 DVLILDEPTNNLD----IESIDALAEAINEYEGGVIIVSHDERLIRETGCTLYVIEDQTINE 868
Cdd:COG1123 162 DLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVE 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
352-574 |
7.35e-20 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 89.49 E-value: 7.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNA----NLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTaint 427
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAIL--GLLKPTSGSIIFDGKDLLKLSRR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 428 ilEADVRRTEMlkkadelekQFVAGD--------LTVQEELNDTfaeLKAIGAYSAEARARRI----LAGLGFSKEMQDR 495
Cdd:cd03257 76 --LRKIRRKEI---------QMVFQDpmsslnprMTIGEQIAEP---LRIHGKLSKKEARKEAvlllLVGVGLPEEVLNR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 496 PTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-------LNAviwLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIH 568
Cdd:cd03257 142 YPHELSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqaqiLDL---LKKLQEELGLTLLFITHDLGVVAKIADRVAV 218
|
....*.
gi 24641342 569 LDQKKL 574
Cdd:cd03257 219 MYAGKI 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
689-845 |
1.07e-19 |
|
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: 88.32 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 689 LFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHR-LHVGRFDQHSGEHLTAEE-------SAAEYL 760
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYLGHApgikttlSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 761 QRLFNL-PHEKARKALGSFGLVSHAHtIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEY-- 837
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNGFED-RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHca 173
|
....*...
gi 24641342 838 EGGVIIVS 845
Cdd:cd03231 174 RGGMVVLT 181
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
648-850 |
1.16e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.08 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 648 QELLARPKEYIVKfrfPEPSQLQPPILGVH--NVTFAFPSQKPLfIKvdfGIDLT----SRVAIVGPNGVGKSTFLKLLL 721
Cdd:COG1132 315 FELLDEPPEIPDP---PGAVPLPPVRGEIEfeNVSFSYPGDRPV-LK---DISLTippgETVALVGPSGSGKSTLVNLLL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 722 GELEPQEGEqrknhrlhVgRFDQHSGEHLTAEEsaaeyLQR----------LFNL----------PH-------EKARKA 774
Cdd:COG1132 388 RFYDPTSGR--------I-LIDGVDIRDLTLES-----LRRqigvvpqdtfLFSGtirenirygrPDatdeeveEAAKAA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 775 lgsfglvsHAHTI--KMKD------------LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG 840
Cdd:COG1132 454 --------QAHEFieALPDgydtvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKG 525
|
250
....*....|..
gi 24641342 841 --VIIVSHdeRL 850
Cdd:COG1132 526 rtTIVIAH--RL 535
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
664-848 |
1.35e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 93.58 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 664 PEPSQLQPPILGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrLHVGRFD 743
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE------VTLDGVP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 744 QHSGEHLTAEESAAEYLQR--LF------NL-------PHEKARKALGSFGLVSH-------AHTIKMKD---LSGGQKA 798
Cdd:TIGR02868 399 VSSLDQDEVRRRVSVCAQDahLFdttvreNLrlarpdaTDEELWAALERVGLADWlralpdgLDTVLGEGgarLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24641342 799 RVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHDE 848
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHHL 530
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
352-853 |
1.38e-19 |
|
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: 93.33 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLrHIATRAFAIPPN-----IDVLLCE-------QEVVA 419
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLM-HVLRGMDQYEPTsgriiYHVALCEkcgyverPSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 420 TD-KTAINTILEADV---------RRTEMLKKADELEKQF-VAGDLTVqeeLNDTFAELKAIGaYSAEARARRILAGLGF 488
Cdd:TIGR03269 80 EPcPVCGGTLEPEEVdfwnlsdklRRRIRKRIAIMLQRTFaLYGDDTV---LDNVLEALEEIG-YEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 489 SKeMQDRPTN---KFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-LNAVIWLDNYLQGWKK---TLLIVSHDQSFLDN 561
Cdd:TIGR03269 156 VQ-LSHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLVHNALEEAVKAsgiSMVLTSHWPEVIED 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 562 VCNEIIHLDqkklqyyKGnysmfkkmyvqkrrEMIKEYEkqekrlrelkahgqskkaaekkqkesltrkqeknkskqqkq 641
Cdd:TIGR03269 235 LSDKAIWLE-------NG--------------EIKEEGT----------------------------------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 642 dedegPQELLARPKEYIVKFRFPEPSQLQPPILGVHNVTFAFPSQKPLFIKVDFGIDLTSRVA----IVGPNGVGKSTFL 717
Cdd:TIGR03269 253 -----PDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGeifgIVGTSGAGKTTLS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 718 KLLLGELEPQEGE-----------QRKNHRLHVGRFDQHSG---------EHLTAEESAAEYLQrlFNLPHEKA-RKALG 776
Cdd:TIGR03269 328 KIIAGVLEPTSGEvnvrvgdewvdMTKPGPDGRGRAKRYIGilhqeydlyPHRTVLDNLTEAIG--LELPDELArMKAVI 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 777 SFGLV----SHAHTI--KMKD-LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAI----NEYEGGVIIVS 845
Cdd:TIGR03269 406 TLKMVgfdeEKAEEIldKYPDeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVS 485
|
....*...
gi 24641342 846 HDERLIRE 853
Cdd:TIGR03269 486 HDMDFVLD 493
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
696-847 |
2.65e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 88.68 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHR-----------LHVGRFDQHSgeHL----TAEESA 756
Cdd:PRK13548 20 DVSLTLRpgevVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelaRRRAVLPQHS--SLsfpfTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 757 AEYLQRLFNLPHEKAR---KALGSFGLVSHAHtikmKD---LSGGQKARVALAE-LC-LSAPD----VLILDEPTNNLDI 824
Cdd:PRK13548 98 AMGRAPHGLSRAEDDAlvaAALAQVDLAHLAG----RDypqLSGGEQQRVQLARvLAqLWEPDgpprWLLLDEPTSALDL 173
|
170 180
....*....|....*....|....*..
gi 24641342 825 ----ESIDALAEAINEYEGGVIIVSHD 847
Cdd:PRK13548 174 ahqhHVLRLARQLAHERGLAVIVVLHD 200
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
674-847 |
5.56e-19 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 86.76 E-value: 5.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQKPLFIKVDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNHRLHVg 740
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALE-DISLSVEegefVALVGPSGCGKSTLLRIIAGLERPTSGEvlvdgepvtGPGPDRGYV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 741 rFDQHS-GEHLTAEESAAeYLQRLFNLPH----EKARKALGSFGLVSHAHtiKM-KDLSGGQKARVALAELCLSAPDVLI 814
Cdd:cd03293 79 -FQQDAlLPWLTVLDNVA-LGLELQGVPKaearERAEELLELVGLSGFEN--AYpHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 24641342 815 LDEPTNNLDI---ESI-DALAEAINEYEGGVIIVSHD 847
Cdd:cd03293 155 LDEPFSALDAltrEQLqEELLDIWRETGKTVLLVTHD 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
348-581 |
5.69e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 91.49 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 348 QAVDIkiENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRhiaTRAFAIPPNidvllcEQEVVATDKTAINT 427
Cdd:PRK15064 318 NALEV--ENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLR---TLVGELEPD------SGTVKWSENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 428 IleadvrrtemlkkADELEKQFvAGDLTV--------QEELNDTfaelkAIgaysaearaRRILAGLGFSKEMQDRPTNK 499
Cdd:PRK15064 387 Y-------------AQDHAYDF-ENDLTLfdwmsqwrQEGDDEQ-----AV---------RGTLGRLLFSQDDIKKSVKV 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 500 FSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKG 579
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSG 518
|
..
gi 24641342 580 NY 581
Cdd:PRK15064 519 TY 520
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
678-850 |
6.81e-19 |
|
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: 86.90 E-value: 6.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKNHRLHVGRFDQH- 745
Cdd:cd03253 5 NVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSilidgqdirevTLDSLRRAIGVVPQDt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 746 ------------------SGEHLTAEESAAEYLQRLFNLPhEKARKALGSFGLvshahtikmkDLSGGQKARVALAELCL 807
Cdd:cd03253 85 vlfndtigynirygrpdaTDEEVIEAAKAAQIHDKIMRFP-DGYDTIVGERGL----------KLSGGEKQRVAIARAIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24641342 808 SAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHdeRL 850
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAH--RL 196
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
671-853 |
1.12e-18 |
|
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: 86.63 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILGVHNVTfafpsqkplfikVDFG-------IDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE--------- 730
Cdd:COG0411 2 DPLLEVRGLT------------KRFGglvavddVSLEvergEIVGLIGPNGAGKTTLFNLITGFYRPTSGRilfdgrdit 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 731 QRKNH---RLHVGR-FdQHSG--EHLTAEE---------SAAEYLQRLFNLP---------HEKARKALGSFGLVSHAHT 786
Cdd:COG0411 70 GLPPHriaRLGIARtF-QNPRlfPELTVLEnvlvaaharLGRGLLAALLRLPrarreereaRERAEELLERVGLADRADE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 787 iKMKDLSGGQKARVALAeLCL-SAPDVLILDEPTNNLDIESIDALAE---AINEYEG-GVIIVSHDERLIRE 853
Cdd:COG0411 149 -PAGNLSYGQQRRLEIA-RALaTEPKLLLLDEPAAGLNPEETEELAElirRLRDERGiTILLIEHDMDLVMG 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
352-571 |
1.60e-18 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 84.16 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVvaTDKTAINTILEA 431
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA--GLEEPDSGSILIDGEDL--TDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRrtemlkkadelekqFVAGD------LTVQEelNDTFaelkaigaysaeararrilaGLgfskemqdrptnkfSGGWR 505
Cdd:cd03229 77 RIG--------------MVFQDfalfphLTVLE--NIAL--------------------GL--------------SGGQQ 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 506 MRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYL----QGWKKTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:cd03229 107 QRVALARALAMDPDVLLLDEPTSALDPITRREVRALLkslqAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
671-846 |
4.13e-18 |
|
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: 84.75 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILGVHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEP---QE----GEQRKNH-----RLH 738
Cdd:COG1119 1 DPLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtygNDvrlfGERRGGEdvwelRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 739 VG--------RFDQH--------SG--------EHLTAEEsaaeylqrlfnlpHEKARKALGSFGLVSHAHTiKMKDLSG 794
Cdd:COG1119 80 IGlvspalqlRFPRDetvldvvlSGffdsiglyREPTDEQ-------------RERARELLELLGLAHLADR-PFGTLSQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 795 GQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEY--EGG--VIIVSH 846
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAptLVLVTH 201
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
352-574 |
4.54e-18 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 83.69 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFV----NANLLIAHGRRYGLVGPNGHGKTTLLRHIATRAFaiPPNIDVLLCEQEVVATDKTAInt 427
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PTSGEVRVDGTDISKLSEKEL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 428 ileADVRRTEMlkkadelekQFV------AGDLTVQEelNDTFA-ELKAIGAYSAEARARRILAGLGFSKEMQDRPtNKF 500
Cdd:cd03255 77 ---AAFRRRHI---------GFVfqsfnlLPDLTALE--NVELPlLLAGVPKKERRERAEELLERVGLGDRLNHYP-SEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLDL-NAVIWLD-----NYLQGwkKTLLIVSHDQSfLDNVCNEIIHLDQKKL 574
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSeTGKEVMEllrelNKEAG--TTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
352-574 |
4.86e-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: 83.96 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPnidvllceqevvatdktainTILEA 431
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTT---LLKP--------------------TSGRA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEMLKKADELEKQ--FVAGDLTVQEELNDT-----FAELKAIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGW 504
Cdd:cd03265 58 TVAGHDVVREPREVRRRigIVFQDLSVDDELTGWenlyiHARLYGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 505 RMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK----TLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:cd03265 137 RRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefgmTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
674-850 |
5.06e-18 |
|
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: 82.20 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLlGELEPqegeqrknhrLHVGRFDQHSGEHLtae 753
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWP----------WGSGRIGMPEGEDL--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 754 esaaeylqrLFnLPhekaRKALGSFGlvshahTIK-------MKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIES 826
Cdd:cd03223 67 ---------LF-LP----QRPYLPLG------TLReqliypwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....
gi 24641342 827 IDALAEAINEYEGGVIIVSHDERL 850
Cdd:cd03223 127 EDRLYQLLKELGITVISVGHRPSL 150
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
676-847 |
6.22e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 84.79 E-value: 6.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG------------EQRKNHRLHVGRF 742
Cdd:TIGR04520 3 VENVSFSYPESEKPALKnVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGkvtvdgldtldeENLWEIRKKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 743 DQHSGEHL---TAEESAAEYLQRLfNLPHEKARK----ALGSFGLVSHAHTIKMKdLSGGQKARVALAELCLSAPDVLIL 815
Cdd:TIGR04520 83 FQNPDNQFvgaTVEDDVAFGLENL-GVPREEMRKrvdeALKLVGMEDFRDREPHL-LSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 24641342 816 DEPTNNLD-------IESIDALAEainEYEGGVIIVSHD 847
Cdd:TIGR04520 161 DEATSMLDpkgrkevLETIRKLNK---EEGITVISITHD 196
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
369-574 |
6.35e-18 |
|
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: 83.41 E-value: 6.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLceqevvatDKTAINTILEADVRRtemlkkadelEKQ 448
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLA--GLYKPTSGSVLL--------DGTDIRQLDPADLRR----------NIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGDLTVqeeLNDTFAELKAIGAYSAEARarRIL-----AGL---------GFSKEMQDRPTNkFSGGWRMRVSLARAL 514
Cdd:cd03245 82 YVPQDVTL---FYGTLRDNITLGAPLADDE--RILraaelAGVtdfvnkhpnGLDLQIGERGRG-LSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 515 YLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK--KTLLIVSHDQSFLDnVCNEIIHLDQKKL 574
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLgdKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
667-852 |
6.65e-18 |
|
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: 83.64 E-value: 6.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 667 SQLQPPILGVHNVTFAFPS-QKPLFI--KVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQR-KNHRL----- 737
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTgAGELTIlkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlAGQDLfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 ---------HVGRFDQ--HSGEHLTAEESAAeylqrlfnLP---------HEKARKALGSFGL---VSHAHtikmKDLSG 794
Cdd:COG4181 82 dararlrarHVGFVFQsfQLLPTLTALENVM--------LPlelagrrdaRARARALLERVGLghrLDHYP----AQLSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 795 GQKARVALAELCLSAPDVLILDEPTNNLDI---ESIDALAEAINEyEGGV--IIVSHDERLIR 852
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAatgEQIIDLLFELNR-ERGTtlVLVTHDPALAA 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
678-847 |
7.89e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 84.81 E-value: 7.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE--------------QRKNHRLHV 739
Cdd:TIGR04521 5 NVSYIYQPGTPFEKKALDDVSLTiedgEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTvtidgrditakkkkKLKDLRKKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHSgEHLTAEESAAE---YLQRLFNLP----HEKARKALGSFGLvshAHTIKMK---DLSGGQKARVALAELCLSA 809
Cdd:TIGR04521 85 GLVFQFP-EHQLFEETVYKdiaFGPKNLGLSeeeaEERVKEALELVGL---DEEYLERspfELSGGQMRRVAIAGVLAME 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24641342 810 PDVLILDEPTNNLDIESIDALAEAINEY--EGG--VIIVSHD 847
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLhkEKGltVILVTHS 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
687-846 |
8.30e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 687 KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQR-KNHRLHVGRFDQHS-----GEH------LTAEE 754
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwQGEPIRRQRDEYHQdllylGHQpgikteLTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 755 SAAeYLQRLFNLPH-EKARKALGSFGLVSHAHtIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEA 833
Cdd:PRK13538 94 NLR-FYQRLHGPGDdEALWEALAQVGLAGFED-VPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
170
....*....|....*.
gi 24641342 834 INEY--EGG-VIIVSH 846
Cdd:PRK13538 172 LAQHaeQGGmVILTTH 187
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
696-853 |
8.66e-18 |
|
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: 82.96 E-value: 8.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNH----RLHVGRFDQHSG--EHLTAEESA 756
Cdd:cd03262 18 GIDLTvkkgEVVVIIGPSGSGKSTLLRCINLLEEPDSGTiiidglkltDDKKNinelRQKVGMVFQQFNlfPHLTVLENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 757 AEYLQRLFNLP----HEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAE-LCLSaPDVLILDEPTNNLDIESIDALA 831
Cdd:cd03262 98 TLAPIKVKGMSkaeaEERALELLEKVGLADKADA-YPAQLSGGQQQRVAIARaLAMN-PKVMLFDEPTSALDPELVGEVL 175
|
170 180
....*....|....*....|....*
gi 24641342 832 EAINE--YEG-GVIIVSHDERLIRE 853
Cdd:cd03262 176 DVMKDlaEEGmTMVVVTHEMGFARE 200
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
677-884 |
9.17e-18 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 88.38 E-value: 9.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 677 HNVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG-------EQRKNH----RLHVGRFDQ 744
Cdd:TIGR03375 467 RNVSFAYPGQETPALDnVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGsvlldgvDIRQIDpadlRRNIGYVPQ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 745 HSgehltaeesaaeylqRLF------NL----PH---EKARKALGSFGLV----SHAHTIKMK------DLSGGQKARVA 801
Cdd:TIGR03375 547 DP---------------RLFygtlrdNIalgaPYaddEEILRAAELAGVTefvrRHPDGLDMQigergrSLSGGQRQAVA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 802 LAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHD-------ERLIretgctlyVIEDQTineIVGe 872
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGktLVLVTHRtslldlvDRII--------VMDNGR---IVA- 679
|
250
....*....|..
gi 24641342 873 fDDYRKEVLDSL 884
Cdd:TIGR03375 680 -DGPKDQVLEAL 690
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
696-853 |
9.76e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 83.50 E-value: 9.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLT----SRVAIVGPNGVGKSTFLKLLLGeLE-PQEGE-------------QRKNHRLHVGR-FdQHSG--EHLTAEE 754
Cdd:COG1126 19 GISLDvekgEVVVIIGPSGSGKSTLLRCINL-LEePDSGTitvdgedltdskkDINKLRRKVGMvF-QQFNlfPHLTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 755 SAAEYLQRLFNLP----HEKARKALGSFGLVSHAHtiKM-KDLSGGQKARVALAE-LCLSaPDVLILDEPTNNLDIESID 828
Cdd:COG1126 97 NVTLAPIKVKKMSkaeaEERAMELLERVGLADKAD--AYpAQLSGGQQQRVAIARaLAME-PKVMLFDEPTSALDPELVG 173
|
170 180 190
....*....|....*....|....*....|...
gi 24641342 829 -------ALAEaineyEG-GVIIVSHDERLIRE 853
Cdd:COG1126 174 evldvmrDLAK-----EGmTMVVVTHEMGFARE 201
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
670-888 |
1.02e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.99 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 670 QPPILGVHNVTFAFPSQKPLFIKVDfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRlHVGRFDQH 745
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALD-DVSLTvaagEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-PVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 746 SG---------EHLTAEE-----------SAAEYlqrlfnlpHEKARKALGSFGLVSHAHtiKM-KDLSGGQKARVALAE 804
Cdd:COG1116 82 RGvvfqepallPWLTVLDnvalglelrgvPKAER--------RERARELLELVGLAGFED--AYpHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 805 LCLSAPDVLILDEPTNNLDI---ESIDALAEAINEYEG-GVIIVSHDerlIREtgcTLY--------------VIEDQTI 866
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDAltrERLQDELLRLWQETGkTVLFVTHD---VDE---AVFladrvvvlsarpgrIVEEIDV 225
|
250 260 270
....*....|....*....|....*....|.
gi 24641342 867 N-------EIVG--EFDDYRKEVLDSLGEVV 888
Cdd:COG1116 226 DlprprdrELRTspEFAALRAEILDLLREEA 256
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
671-851 |
1.34e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.24 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILGVHNVTFAFPSQKPLFiKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGRFDQHSgeHL 750
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLS-DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKL--YL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 751 TAeeSAAEYLQRLFNL-PHEKARKALGSFGLVSHAHTIK--MKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESI 827
Cdd:PRK09544 79 DT--TLPLTVNRFLRLrPGTKKEDILPALKRVQAGHLIDapMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*...
gi 24641342 828 DALAEAIN----EYEGGVIIVSHDERLI 851
Cdd:PRK09544 157 VALYDLIDqlrrELDCAVLMVSHDLHLV 184
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
377-847 |
1.72e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 87.17 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 377 GRRYGLVGPNGHGKTTLLRHIATRafaIPPNidvlLCEQEvvatDKTAINTILEAdVRRTEM-----------LKKA--- 442
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGE---LIPN----LGDYE----EEPSWDEVLKR-FRGTELqnyfkklyngeIKVVhkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 443 ---DELEKQFvagDLTVQEELNDTfAELKAIGAYSAEARARRILaglgfskemqDRPTNKFSGGWRMRVSLARALYLEPT 519
Cdd:PRK13409 167 qyvDLIPKVF---KGKVRELLKKV-DERGKLDEVVERLGLENIL----------DRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 520 LLMLDEPTNHLD----LNAVIWLDNYLQGwkKTLLIVSHDQSFLDNVCnEIIHLdqkklQYYK-GNYSMFKKMYvqKRRE 594
Cdd:PRK13409 233 FYFFDEPTSYLDirqrLNVARLIRELAEG--KYVLVVEHDLAVLDYLA-DNVHI-----AYGEpGAYGVVSKPK--GVRV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 595 MIKEYekqekrLR-ELKahgqskkaaekkqkesltrkqEKNkskqqkqdedegpqeLLARPKEYIVKFRFPEPSQLQPPI 673
Cdd:PRK13409 303 GINEY------LKgYLP---------------------EEN---------------MRIRPEPIEFEERPPRDESERETL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQKplfIKVDFG-IDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVG----RFDQhsge 748
Cdd:PRK13409 341 VEYPDLTKKLGDFS---LEVEGGeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKpqyiKPDY---- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 749 hltaEESAAEYLqrlfnlphEKARKALGS----------FGLvshaHTI---KMKDLSGGQKARVALAeLCLSAP-DVLI 814
Cdd:PRK13409 414 ----DGTVEDLL--------RSITDDLGSsyykseiikpLQL----ERLldkNVKDLSGGELQRVAIA-ACLSRDaDLYL 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 24641342 815 LDEPTNNLDIESIDALAEAIN----EYEGGVIIVSHD 847
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRriaeEREATALVVDHD 513
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
352-571 |
1.79e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.88 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrafaippnidvlLCEQEVVATDKTAINTIlEA 431
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCIN-------------LLEQPEAGTIRVGDITI-DT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEMLKKADELEKQ--FVAGDL------TVQEELNDTFAELKAIGAYSAEARARRILAGLGFS-KEmqDRPTNKFSG 502
Cdd:PRK11264 70 ARSLSQQKGLIRQLRQHvgFVFQNFnlfphrTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAgKE--TSYPRRLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 503 GWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGW---KKTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDVADRAIFMDQ 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
674-846 |
2.19e-17 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 80.82 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrLHVGRFDQHsgehlTA 752
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKnLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGE------ITLDGVPVS-----DL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 753 EESAAEYLQRLFNLPHEKARKALGSFGlvshahtikmKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAE 832
Cdd:cd03247 70 EKALSSLISVLNQRPYLFDTTLRNNLG----------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170
....*....|....*.
gi 24641342 833 AINEY--EGGVIIVSH 846
Cdd:cd03247 140 LIFEVlkDKTLIWITH 155
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
353-574 |
2.20e-17 |
|
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: 81.81 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 353 KIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPP---NIDV----LLCEQEVVA--TDKT 423
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILG---LLKPtsgSIRVfgkpLEKERKRIGyvPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 424 AINTILEADVRrtemlkkadelekQFVAGDLtvqeelndtFAELKAIGAYSAE--ARARRILAGLGFSkEMQDRPTNKFS 501
Cdd:cd03235 78 SIDRDFPISVR-------------DVVLMGL---------YGHKGLFRRLSKAdkAKVDEALERVGLS-ELADRQIGELS 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 502 GGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK---KTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRregMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
676-847 |
2.77e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.47 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFpSQKPLfikVDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRlhvgRFDQHSGEHL- 750
Cdd:COG4559 4 AENLSVRL-GGRTL---LD-DVSLTLRpgelTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGR----PLAAWSPWELa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 751 ----------------TAEESAAeyLQRlfnLPH--------EKARKALGSFGLVSHAHTIkMKDLSGGQKARVALA--- 803
Cdd:COG4559 75 rrravlpqhsslafpfTVEEVVA--LGR---APHgssaaqdrQIVREALALVGLAHLAGRS-YQTLSGGEQQRVQLArvl 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 804 ----ELCLSAPDVLILDEPTNNLDI-------ESIDALAEAineyEGGVIIVSHD 847
Cdd:COG4559 149 aqlwEPVDGGPRWLFLDEPTSALDLahqhavlRLARQLARR----GGGVVAVLHD 199
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
352-574 |
3.45e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 81.78 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRafaIPPNI-DVLLCEQEVVATDKTAintiLE 430
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL---LRPDSgEVLIDGEDISGLSEAE----LY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 ADVRRTEMLKkadelekQFVA--GDLTVQEelNDTFAeLKAIGAYSAEARARRILAGLGFS--KEMQDRPTNKFSGGWRM 506
Cdd:cd03261 74 RLRRRMGMLF-------QSGAlfDSLTVFE--NVAFP-LREHTRLSEEEIREIVLEKLEAVglRGAEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 507 RVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTL----LIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
676-865 |
3.62e-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: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQkPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNHRLHVGR-FDQH 745
Cdd:cd03259 3 LKGLSKTYGSV-RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvtGVPPERRNIGMvFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 746 SG-EHLTAEESAAeYLQRLFNLPHEKARK----ALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTN 820
Cdd:cd03259 82 ALfPHLTVAENIA-FGLKLRGVPKAEIRArvreLLELVGLEGLLNR-YPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24641342 821 NLDIESIDALAEAIneyeggviivshdERLIRETGCT-LYVIEDQT 865
Cdd:cd03259 160 ALDAKLREELREEL-------------KELQRELGITtIYVTHDQE 192
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
648-854 |
3.89e-17 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 85.96 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 648 QELLA-RPKEyivkfrfPEPSQLQPP--ILGVHNVTFAFP-SQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGE 723
Cdd:COG4618 309 NELLAaVPAE-------PERMPLPRPkgRLSVENLTVVPPgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 724 LEPQEGeqrknhrlHVgRFDQHSGEHLTAEE-----------------SAAEYLQRLFNLPHEK----ARKA-------- 774
Cdd:COG4618 382 WPPTAG--------SV-RLDGADLSQWDREElgrhigylpqdvelfdgTIAENIARFGDADPEKvvaaAKLAgvhemilr 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 775 --------LGSFGLVshahtikmkdLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINE--YEGG-VII 843
Cdd:COG4618 453 lpdgydtrIGEGGAR----------LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlkARGAtVVV 522
|
250
....*....|.
gi 24641342 844 VSHDERLIRET 854
Cdd:COG4618 523 ITHRPSLLAAV 533
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
691-847 |
4.93e-17 |
|
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: 80.80 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 691 IKVDFGIDlTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHvgrFDQHSGEHLTAEESAAEYL-QRLFNLPHE 769
Cdd:cd03297 15 LKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL---FDSRKKINLPPQQRKIGLVfQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 770 KARKALgSFGLVSHAHTiKMKD---------------------LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESID 828
Cdd:cd03297 91 NVRENL-AFGLKRKRNR-EDRIsvdelldllgldhllnrypaqLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180
....*....|....*....|...
gi 24641342 829 ALAEAINE----YEGGVIIVSHD 847
Cdd:cd03297 169 QLLPELKQikknLNIPVIFVTHD 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
696-851 |
4.94e-17 |
|
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: 80.26 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLTSR----VAIVGPNGVGKSTFLKLLLG--ELEPQEGEQRknhrlhvgrFDqhsGEHLTAEEsaaeylqrlfnlPHE 769
Cdd:cd03217 18 GVNLTIKkgevHALMGPNGSGKSTLAKTIMGhpKYEVTEGEIL---------FK---GEDITDLP------------PEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 770 KARKALG-SFGLVSHAHTIKMKDL--------SGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEY--E 838
Cdd:cd03217 74 RARLGIFlAFQYPPEIPGVKNADFlryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreE 153
|
170
....*....|....
gi 24641342 839 G-GVIIVSHDERLI 851
Cdd:cd03217 154 GkSVLIITHYQRLL 167
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
352-573 |
5.42e-17 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 79.35 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIEN--FTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLrHIATRaFAIPPNIDVLLceqevvatDKTAINTIL 429
Cdd:cd03228 1 IEFKNvsFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLL-KLLLR-LYDPTSGEILI--------DGVDLRDLD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 EADVRRTemlkkadelekqfVAgdlTVQEE---LNDTFAElkaigaysaeararrilaglgfskemqdrptNKFSGGWRM 506
Cdd:cd03228 71 LESLRKN-------------IA---YVPQDpflFSGTIRE-------------------------------NILSGGQRQ 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 507 RVSLARALYLEPTLLMLDEPTNHLD--LNAVIW--LDNYLQGwkKTLLIVSHDQSFLDNvCNEIIHLDQKK 573
Cdd:cd03228 104 RIAIARALLRDPPILILDEATSALDpeTEALILeaLRALAKG--KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
676-845 |
5.78e-17 |
|
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: 80.87 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIKVDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEG----------EQRKNHRLHVGR 741
Cdd:cd03266 4 ADALTKRFRDVKKTVQAVD-GVSFTVKpgevTGLLGPNGAGKTTTLRMLAGLLEPDAGfatvdgfdvvKEPAEARRRLGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQHSG--EHLTAEESAaEYLQRLFNLPHEKARKALGS-FGLVSHAHTI--KMKDLSGGQKARVALAELCLSAPDVLILD 816
Cdd:cd03266 83 VSDSTGlyDRLTARENL-EYFAGLYGLKGDELTARLEElADRLGMEELLdrRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190
....*....|....*....|....*....|.
gi 24641342 817 EPTNNLDIESIDALAEAINEY--EGGVIIVS 845
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLraLGKCILFS 192
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
335-574 |
7.97e-17 |
|
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: 84.81 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 335 QVQKSAGQKAALEQAVDIKIENFTIS-AKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLC 413
Cdd:COG4988 320 PAAPAGTAPLPAAGPPSIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL--GFLPPYSGSILIN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 414 EQEVVATDKTAIN----------TILEADVRRTEMLKKADelekqfvAGDltvqEELNDtfaelkAIgaysAEARARRIL 483
Cdd:COG4988 398 GVDLSDLDPASWRrqiawvpqnpYLFAGTIRENLRLGRPD-------ASD----EELEA------AL----EAAGLDEFV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 484 AGL--GFSKEMQDRPTNkFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLN--AVIW--LDNYLQGwkKTLLIVSHDQS 557
Cdd:COG4988 457 AALpdGLDTPLGEGGRG-LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLAKG--RTVILITHRLA 533
|
250
....*....|....*..
gi 24641342 558 FLDNvCNEIIHLDQKKL 574
Cdd:COG4988 534 LLAQ-ADRILVLDDGRI 549
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
673-853 |
1.26e-16 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 80.42 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG---------------EQRKnHRL 737
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGsillegtditklrgkKLRK-LRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 HVGRFDQHSG--EHLTAEE-------SAAEYLQRLFNL--PHEKAR--KALGSFGLVSHAHTiKMKDLSGGQKARVALAE 804
Cdd:TIGR02315 80 RIGMIFQHYNliERLTVLEnvlhgrlGYKPTWRSLLGRfsEEDKERalSALERVGLADKAYQ-RADQLSGGQQQRVAIAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24641342 805 LCLSAPDVLILDEPTNNLDIES----IDALAEaINEYEGGVIIVS-HDERLIRE 853
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTskqvMDYLKR-INKEDGITVIINlHQVDLAKK 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
377-847 |
2.24e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 83.68 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 377 GRRYGLVGPNGHGKTTLLRHIATrafAIPPNidvlLCEQEvvatDKTAINTILEAdVRRTEM---LKK------------ 441
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSG---ELKPN----LGDYD----EEPSWDEVLKR-FRGTELqdyFKKlangeikvahkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 442 --ADELEKQFvagDLTVQEELNDTfAELKAIGAYSAEARARRILaglgfskemqDRPTNKFSGGWRMRVSLARALYLEPT 519
Cdd:COG1245 167 qyVDLIPKVF---KGTVRELLEKV-DERGKLDELAEKLGLENIL----------DRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 520 LLMLDEPTNHLD----LNAVIWLDNYLQGwKKTLLIVSHDQSFLDNVcNEIIHLdqkklqYY--KGNYSMFKKMY-Vqkr 592
Cdd:COG1245 233 FYFFDEPSSYLDiyqrLNVARLIRELAEE-GKYVLVVEHDLAILDYL-ADYVHI------LYgePGVYGVVSKPKsV--- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 593 REMIKEYekqekrlreLKAHgqskkaaekkqkesLtrkQEKNkskqqkqdedegpqeLLARPKEYIVKFRFPEPSQLQPP 672
Cdd:COG1245 302 RVGINQY---------LDGY--------------L---PEEN---------------VRIRDEPIEFEVHAPRREKEEET 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKplfIKVDFG-IDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHV----------GR 741
Cdd:COG1245 341 LVEYPDLTKSYGGFS---LEVEGGeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYkpqyispdydGT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQHSGEHLTAEESA----AEYLQRLfNLPH--EKarkalgsfglvshahtiKMKDLSGGQKARVALAeLCLSAP-DVLI 814
Cdd:COG1245 418 VEEFLRSANTDDFGSsyykTEIIKPL-GLEKllDK-----------------NVKDLSGGELQRVAIA-ACLSRDaDLYL 478
|
490 500 510
....*....|....*....|....*....|....*..
gi 24641342 815 LDEPTNNLDIESIDALAEAIN----EYEGGVIIVSHD 847
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAIRrfaeNRGKTAMVVDHD 515
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
352-607 |
2.37e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 83.45 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRafaippnidvllcEQEvvatDKTAInTILEA 431
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQ-------------EQP----DSGTI-EIGET 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 dVRRTEMLKKADELEkqfvaGDLTVQEELNDTFAELKaIGAYSAEARArrILAGLGFSKEMQDRPTNKFSGGWRMRVSLA 511
Cdd:TIGR03719 385 -VKLAYVDQSRDALD-----PNKTVWEEISGGLDIIK-LGKREIPSRA--YVGRFNFKGSDQQKKVGQLSGGERNRVHLA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 512 RALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLD-QKKLQYYKGNYSmfkkMYVQ 590
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEgDSHVEWFEGNFS----EYEE 531
|
250
....*....|....*..
gi 24641342 591 KRREMIKEYEKQEKRLR 607
Cdd:TIGR03719 532 DKKRRLGEDADQPHRIK 548
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
676-847 |
2.59e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 79.15 E-value: 2.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFiKVDFGIDLTSRVAIVGPNGVGKSTFLKLL-----LGELEPQEGE-------------QRKNHRL 737
Cdd:cd03260 3 LRDLNVYYGDKHALK-DISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEvlldgkdiydldvDVLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 HVGR-FDQHSGEHLTAEESAAeYLQRLFNL-----PHEKARKALGSFGLvshahTIKMKD------LSGGQKARVALAEL 805
Cdd:cd03260 82 RVGMvFQKPNPFPGSIYDNVA-YGLRLHGIklkeeLDERVEEALRKAAL-----WDEVKDrlhalgLSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24641342 806 CLSAPDVLILDEPTNNLDIESIDALAEAINEY--EGGVIIVSHD 847
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
674-846 |
2.67e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 78.48 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQKPLfIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKN-------HRLHVGRFDQHS 746
Cdd:cd03269 1 LEVENVTKRFGRVTAL-DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgkpldiaARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 747 GehLTAEESAAE---YLQRLFNLPHEKARKA----LGSFGLVSHAHtIKMKDLSGGQKARVALAELCLSAPDVLILDEPT 819
Cdd:cd03269 80 G--LYPKMKVIDqlvYLAQLKGLKKEEARRRidewLERLELSEYAN-KRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190
....*....|....*....|....*....|
gi 24641342 820 NNLDIESIDALAEAINEYEGG---VIIVSH 846
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAgktVILSTH 186
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
693-901 |
3.06e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.90 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRKNHRLHVGR-FDQHSG--EHLTAEESaAEY 759
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEvrvlgyvpfkRRKEFARRIGVvFGQRSQlwWDLPAIDS-FRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 760 LQRLFNLPHEKARKALGSFglvshAHTIKMKD--------LSGGQKARvalAELCLS---APDVLILDEPTNNLDIESID 828
Cdd:COG4586 120 LKAIYRIPDAEYKKRLDEL-----VELLDLGElldtpvrqLSLGQRMR---CELAAAllhRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 829 ALAEAINEY--EGGVIIV--SHD--------ERLI-----RetgctlyVIEDQTINEIVGEFDDYRKEVLDsLGEVVNNP 891
Cdd:COG4586 192 AIREFLKEYnrERGTTILltSHDmddiealcDRVIvidhgR-------IIYDGSLEELKERFGPYKTIVLE-LAEPVPPL 263
|
250
....*....|
gi 24641342 892 SVVANAAVLQ 901
Cdd:COG4586 264 ELPRGGEVIE 273
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
678-847 |
3.68e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 78.64 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFikvDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---QRKNH-RLHVGR------FDQHS- 746
Cdd:COG3840 6 DLTYRYGDFPLRF---DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRilwNGQDLtALPPAErpvsmlFQENNl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 747 GEHLTAEESAAEYLQ---RLFNLPHEKARKALGSFGLvshahtIKMKD-----LSGGQKARVALAELCLSAPDVLILDEP 818
Cdd:COG3840 83 FPHLTVAQNIGLGLRpglKLTAEQRAQVEQALERVGL------AGLLDrlpgqLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190
....*....|....*....|....*....|...
gi 24641342 819 TNNLDI----ESIDALAEAINEYEGGVIIVSHD 847
Cdd:COG3840 157 FSALDPalrqEMLDLVDELCRERGLTVLMVTHD 189
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
369-569 |
3.92e-16 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 78.55 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafaippnID------VLLCEQEVVATDKTAIntileADVRRTEMlkka 442
Cdd:COG1136 26 GVSLSIEAGEFVAIVGPSGSGKSTLLNILGG--------LDrptsgeVLIDGQDISSLSEREL-----ARLRRRHI---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 443 delekQFVA------GDLTVQE--ELNdtfAELKAIGAYSAEARARRILAGLGFSKEMQDRPtNKFSGGWRMRVSLARAL 514
Cdd:COG1136 89 -----GFVFqffnllPELTALEnvALP---LLLAGVSRKERRERARELLERVGLGDRLDHRP-SQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 515 YLEPTLLMLDEPTNHLD-------LNAviwLDNYLQGWKKTLLIVSHDQsFLDNVCNEIIHL 569
Cdd:COG1136 160 VNRPKLILADEPTGNLDsktgeevLEL---LRELNRELGTTIVMVTHDP-ELAARADRVIRL 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
692-852 |
4.46e-16 |
|
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: 77.65 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 692 KVDFGIDLTsrvAIVGPNGVGKSTFLKLLL----GELEPQ------------EGEQRKNHRLHvgrFDQHSGEHLTAEES 755
Cdd:cd03240 17 EIEFFSPLT---LIVGQNGAGKTTIIEALKyaltGELPPNskggahdpklirEGEVRAQVKLA---FENANGKKYTITRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 AAEYLQRLFnLPHEKARKALgsfglvshahtIKMKD-LSGGQKA------RVALAELCLSAPDVLILDEPTNNLDIESID 828
Cdd:cd03240 91 LAILENVIF-CHQGESNWPL-----------LDMRGrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIE 158
|
170 180
....*....|....*....|....*....
gi 24641342 829 -ALAEAINEYEGG----VIIVSHDERLIR 852
Cdd:cd03240 159 eSLAEIIEERKSQknfqLIVITHDEELVD 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
692-859 |
5.50e-16 |
|
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: 78.14 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 692 KVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRKNHRLHVGR-FDQHSgeHLTAEESAAE-- 758
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEvrvaglvpwkRRKKFLRRIGVvFGQKT--QLWWDLPVIDsf 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 759 -YLQRLFNLPHEKARKALGSFG-LVSHAHTIK--MKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAI 834
Cdd:cd03267 117 yLLAAIYDLPPARFKKRLDELSeLLDLEELLDtpVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFL 196
|
170 180 190
....*....|....*....|....*....|....*...
gi 24641342 835 NEY----EGGVIIVSHD----ERLIR-----ETGCTLY 859
Cdd:cd03267 197 KEYnrerGTTVLLTSHYmkdiEALARrvlviDKGRLLY 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
352-571 |
7.02e-16 |
|
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: 77.57 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtraFAIPPNIDVLLCEQEVVATDKTAINTILea 431
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN---LLEEPDSGTIIIDGLKLTDDKKNINELR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 dvRRTEMLKKADELEKQfvagdLTVQEelNDTFAELKAIG--AYSAEARARRILAGLGFSKEMQDRPtNKFSGGWRMRVS 509
Cdd:cd03262 76 --QKVGMVFQQFNLFPH-----LTVLE--NITLAPIKVKGmsKAEAEERALELLEKVGLADKADAYP-AQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 510 LARALYLEPTLLMLDEPTNHLD---LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
369-571 |
8.07e-16 |
|
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: 77.86 E-value: 8.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNI-DVLLCEQEVVATDKTAINtilEADVRRTemlkkadelek 447
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISG---FLRPTSgSVLFDGEDITGLPPHEIA---RLGIGRT----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 448 qF----VAGDLTVQEEL--------NDTFAELKAIGAYS-AEARARRILAGLGFSKEMqDRPTNKFSGGWRMRVSLARAL 514
Cdd:cd03219 81 -FqiprLFPELTVLENVmvaaqartGSGLLLARARREEReARERAEELLERVGLADLA-DRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 515 YLEPTLLMLDEPT---NHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:cd03219 159 ATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQ 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
656-852 |
8.71e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.08 E-value: 8.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 656 EYI-VKFRFPEPSQLQPPIL-GV---HNVTFAFPSQ--KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQE 728
Cdd:TIGR00958 456 EYLdRKPNIPLTGTLAPLNLeGLiefQDVSFSYPNRpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 729 GE---------QRKNHRLH--VGRFDQH----SGehlTAEESAAEYLQRLfnlPHEKARKAlgsfGLVSHAHTIKMKD-- 791
Cdd:TIGR00958 536 GQvlldgvplvQYDHHYLHrqVALVGQEpvlfSG---SVRENIAYGLTDT---PDEEIMAA----AKAANAHDFIMEFpn 605
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 792 ------------LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGGVIIVSHDERLIR 852
Cdd:TIGR00958 606 gydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVE 678
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
691-863 |
1.20e-15 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 79.39 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 691 IKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLhvgRFDQHSGEHLTAEESAAEYL---QRLFnlP 767
Cdd:TIGR02142 14 LDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT---LFDSRKGIFLPPEKRRIGYVfqeARLF--P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 768 HEKAR--------KALGSFGLVSHAHTIKM-----------KDLSGGQKARVALAELCLSAPDVLILDEPTNNLDI---- 824
Cdd:TIGR02142 89 HLSVRgnlrygmkRARPSERRISFERVIELlgighllgrlpGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprky 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 24641342 825 ESIDALAEAINEYEGGVIIVSHDERLIRETGCTLYVIED 863
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLED 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
674-848 |
1.21e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.75 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQkPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQ---EGEQRKN---------HRLHVG- 740
Cdd:COG4136 2 LSLENLTITLGGR-PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNgrrltalpaEQRRIGi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 741 RF-DQHSGEHLtaeeSAAEYLqrLFNLPHE---KARK-----ALGSFGLVSHAHtikmKD---LSGGQKARVALAELCLS 808
Cdd:COG4136 81 LFqDDLLFPHL----SVGENL--AFALPPTigrAQRRarveqALEEAGLAGFAD----RDpatLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24641342 809 APDVLILDEPTNNLDI---ESIDALA-EAINEYEGGVIIVSHDE 848
Cdd:COG4136 151 EPRALLLDEPFSKLDAalrAQFREFVfEQIRQRGIPALLVTHDE 194
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
669-847 |
1.60e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.75 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 669 LQPPILGVHNVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNH-----------R 736
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYALKdVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 737 LHVGRFDQHSGEHL---TAEESAAeylqrlFNL-----PH----EKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAE 804
Cdd:PRK13635 81 RQVGMVFQNPDNQFvgaTVQDDVA------FGLenigvPReemvERVDQALRQVGMEDFLNR-EPHRLSGGQKQRVAIAG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24641342 805 LCLSAPDVLILDEPTNNLD----IESIDALAEAINEYEGGVIIVSHD 847
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHD 200
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
362-575 |
3.04e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.55 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 362 KGNDLFVNANLLIAhgrrygLVGPNGHGKTTLLRHIAtraFAIPPnidvllCEQEVVATDKTaINTILEADVRrtemLKK 441
Cdd:PRK10619 22 KGVSLQANAGDVIS------IIGSSGSGKSTFLRCIN---FLEKP------SEGSIVVNGQT-INLVRDKDGQ----LKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 442 ADELEKQFVAGDLTVQEEL-----------NDTFAELKAIGAYSAEARARRI--LAGLGFSKEMQDRPTNKFSGGWRMRV 508
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVFQHfnlwshmtvleNVMEAPIQVLGLSKQEARERAVkyLAKVGIDERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 509 SLARALYLEPTLLMLDEPTNHLD---LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQ 575
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
341-574 |
3.37e-15 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 79.81 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 341 GQKAALEQAVDIKIENFTISAKGNDLFV--NANLLIAHGRRYGLVGPNGHGKTTLLrHIATRAfaIPPNI-DVLLceqev 417
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYPGAGRPVldGLSLTLPPGERVAIVGPSGSGKSTLL-ALLLRF--LDPQSgSITL----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 418 vatDKTAINTILEADVRRTemlkkadelekqfVAGdltVQEE---LNDTFAE-LKaIGAYSA-EARARRILAGLGFSKEM 492
Cdd:COG4987 395 ---GGVDLRDLDEDDLRRR-------------IAV---VPQRphlFDTTLREnLR-LARPDAtDEELWAALERVGLGDWL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 493 QDRP----TN------KFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-------LNAviwLDNYLQGwkKTLLIVSHD 555
Cdd:COG4987 455 AALPdgldTWlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDaateqalLAD---LLEALAG--RTVLLITHR 529
|
250
....*....|....*....
gi 24641342 556 QSFLDNVcNEIIHLDQKKL 574
Cdd:COG4987 530 LAGLERM-DRILVLEDGRI 547
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
678-850 |
4.51e-15 |
|
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: 75.73 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQR-----------KNHRLHVGRFDQH 745
Cdd:cd03251 5 NVTFRYPGDGPPVLRdISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdytlASLRRQIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 746 SgeHL---TAEESAAeYLQRlfNLPHEKARKALGsfglVSHAHTIKMK--------------DLSGGQKARVALAELCLS 808
Cdd:cd03251 85 V--FLfndTVAENIA-YGRP--GATREEVEEAAR----AANAHEFIMElpegydtvigergvKLSGGQRQRIAIARALLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24641342 809 APDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHdeRL 850
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNrtTFVIAH--RL 197
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
352-575 |
4.63e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.09 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTIS-AKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNI-DVLLCEQEVVATDKTAIntil 429
Cdd:COG2884 2 IRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG---EERPTSgQVLVNGQDLSRLKRREI---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 eADVRRT--------EMLKkadelekqfvagDLTVQEelNDTFAeLKAIGAYSAEARAR--RILAGLGFSKEMQDRPtNK 499
Cdd:COG2884 75 -PYLRRRigvvfqdfRLLP------------DRTVYE--NVALP-LRVTGKSRKEIRRRvrEVLDLVGLSDKAKALP-HE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 500 FSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-------------LNAViwldnylqgwKKTLLIVSHDQSFLDNVCNEI 566
Cdd:COG2884 138 LSGGEQQRVAIARALVNRPELLLADEPTGNLDpetsweimelleeINRR----------GTTVLIATHDLELVDRMPKRV 207
|
....*....
gi 24641342 567 IHLDQKKLQ 575
Cdd:COG2884 208 LELEDGRLV 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
354-565 |
4.69e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.22 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 354 IENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRhiatrafaippnidvLLCEQEVVATDKTAINTILEA-- 431
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLK---------------LMLGQLQADSGRIHCGTKLEVay 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 -DVRRTEMlkkadELEKqfvagdlTVQEELNDTFAELKAIGaysaeaRARRILAGLG---FSKEMQDRPTNKFSGGWRMR 507
Cdd:PRK11147 387 fDQHRAEL-----DPEK-------TVMDNLAEGKQEVMVNG------RPRHVLGYLQdflFHPKRAMTPVKALSGGERNR 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 508 VSLARaLYLEPT-LLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNE 565
Cdd:PRK11147 449 LLLAR-LFLKPSnLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTE 506
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
703-847 |
4.81e-15 |
|
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: 75.91 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNhRLHVGRFDQH--SGEHLTAEESAAEYLQRLFNLPHEKAR--KALGSF 778
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYikADYEGTVRDLLSSITKDFYTHPYFKTEiaKPLQIE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 779 GLVSHahtiKMKDLSGGQKARVALAeLCLSAP-DVLILDEPTNNLDIESIDALAEAINEY----EGGVIIVSHD 847
Cdd:cd03237 107 QILDR----EVPELSGGELQRVAIA-ACLSKDaDIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHD 175
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
352-575 |
1.01e-14 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 74.63 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtraFAIPPN---IDVLlcEQEVVATDKTAINTI 428
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII---GLLRPDsgeILVD--GQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 429 LeadvRRTEMLkkadelekqFVAG----DLTVQEelNDTFA--ELKAIGAYSAEARARRILA--GLgfsKEMQDRPTNKF 500
Cdd:COG1127 81 R----RRIGML---------FQGGalfdSLTVFE--NVAFPlrEHTDLSEAEIRELVLEKLElvGL---PGAADKMPSEL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTL----LIVSHDQSFLDNVCNEIIHLDQKKLQ 575
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsVVVTHDLDSAFAIADRVAVLADGKII 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
354-574 |
1.46e-14 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 73.45 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 354 IENFTISAKGNDLFV-NANLLIAHGRRYGLVGPNGHGKTTLLRhiatrafaippnidvLLCeqevvATDKTAINTILEAD 432
Cdd:cd03226 2 IENISFSYKKGTEILdDLSLDLYAGEIIALTGKNGAGKTTLAK---------------ILA-----GLIKESSGSILLNG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 433 VRRtemlkKADELEKQ--FVAGDLTVQEELNDTFAELK--AIGAYSAEARARRILAGLGFSKEMQDRPTNkFSGGWRMRV 508
Cdd:cd03226 62 KPI-----KAKERRKSigYVMQDVDYQLFTDSVREELLlgLKELDAGNEQAETVLKDLDLYALKERHPLS-LSGGQKQRL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 509 SLARALYLEPTLLMLDEPTNHLD---LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:cd03226 136 AIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
674-852 |
1.74e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.54 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLL--L-----GELE-PQEGE-----QRKnhRLHVG 740
Cdd:COG4178 363 LALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIagLwpygsGRIArPAGARvlflpQRP--YLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 741 RFDQ-----HSGEHLTAEEsAAEYLQRLfNLPHekarkalgsfgLVSHAHTIKMKD--LSGGQKARVALAELCLSAPDVL 813
Cdd:COG4178 441 TLREallypATAEAFSDAE-LREALEAV-GLGH-----------LAERLDEEADWDqvLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24641342 814 ILDEPTNNLDIESIDALAEAINEYEGGVIIVS--HDERLIR 852
Cdd:COG4178 508 FLDEATSALDEENEAALYQLLREELPGTTVISvgHRSTLAA 548
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
676-847 |
1.96e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.96 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKplfikvdfgidLTsrvAIVGPNGVGKSTFLKLLLGELEPQEGE-----------------------QR 732
Cdd:COG4604 17 LDDVSLTIPKGG-----------IT---ALIGPNGAGKSTLLSMISRLLPPDSGEvlvdgldvattpsrelakrlailRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 733 KNH---RLHV------GRFdQHSGEHLTAEEsaaeylqrlfnlpHEKARKALGSFGLVSHAHtiKMKD-LSGGQKAR--V 800
Cdd:COG4604 83 ENHinsRLTVrelvafGRF-PYSKGRLTAED-------------REIIDEAIAYLDLEDLAD--RYLDeLSGGQRQRafI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24641342 801 ALAeLClSAPDVLILDEPTNNLDI----ESIDALAEAINEYEGGVIIVSHD 847
Cdd:COG4604 147 AMV-LA-QDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
676-823 |
2.08e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 74.26 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE--------QRKNH---RLHVGRFD 743
Cdd:PRK13632 10 VENVSFSYPNSENNALKnVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEikidgitiSKENLkeiRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 744 QHSGEH---LTAEESAAEYLQRLfNLPHEKARKAlgsfgLVSHAHTIKMKD--------LSGGQKARVALAELCLSAPDV 812
Cdd:PRK13632 90 QNPDNQfigATVEDDIAFGLENK-KVPPKKMKDI-----IDDLAKKVGMEDyldkepqnLSGGQKQRVAIASVLALNPEI 163
|
170
....*....|.
gi 24641342 813 LILDEPTNNLD 823
Cdd:PRK13632 164 IIFDESTSMLD 174
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
672-847 |
2.12e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.40 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKNHRLHV 739
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFTLKdVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEifynnqaitddNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHSGEHLTAEESAAEYLQRLFN--LPHEK----ARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVL 813
Cdd:PRK13648 86 GIVFQNPDNQFVGSIVKYDVAFGLENhaVPYDEmhrrVSEALKQVDMLERADY-EPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 24641342 814 ILDEPTNNLDIESIDALAEAINEY--EGGVIIVS--HD 847
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVksEHNITIISitHD 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
352-554 |
2.22e-14 |
|
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: 73.97 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRafaIPP--NIDVLLCEQEVVATDktaintIl 429
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGD---LPPtyGNDVRLFGERRGGED------V- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 eADVRR------TEMLkkadelekQFVAGDLTVqEE-----LNDTfaelkaIGAYSA-----EARARRILAGLGFSkEMQ 493
Cdd:COG1119 74 -WELRKriglvsPALQ--------LRFPRDETV-LDvvlsgFFDS------IGLYREptdeqRERARELLELLGLA-HLA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 494 DRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNA----VIWLDNYLQGWKKTLLIVSH 554
Cdd:COG1119 137 DRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
648-851 |
2.38e-14 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 77.00 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 648 QELLARPKEYIVKFRFPEPSQlqppILGVHNVTFAFP-SQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEP 726
Cdd:TIGR01842 295 NELLANYPSRDPAMPLPEPEG----HLSVENVTIVPPgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 727 QEGeqrkNHRLHVGRFDQHS----GEHL--------TAEESAAEYLQRLF-NLPHEK---ARKALGSfglvsHAHTIKMK 790
Cdd:TIGR01842 371 TSG----SVRLDGADLKQWDretfGKHIgylpqdveLFPGTVAENIARFGeNADPEKiieAAKLAGV-----HELILRLP 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 791 D------------LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYE---GGVIIVSHDERLI 851
Cdd:TIGR01842 442 DgydtvigpggatLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLL 517
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
369-574 |
2.63e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.59 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVVATdktaintilEADVRrtEMLKKADELEKQ 448
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCI--NKLEEITSGDLIVDGLKVNDP---------KVDER--LIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 F-VAGDLTVQEelNDTFAELKAIGAYSAEAR--ARRILAGLGFSKEMQDRPtNKFSGGWRMRVSLARALYLEPTLLMLDE 525
Cdd:PRK09493 86 FyLFPHLTALE--NVMFGPLRVRGASKEEAEkqARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24641342 526 PTNHLD---LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:PRK09493 163 PTSALDpelRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
349-555 |
3.17e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 73.59 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 349 AVDIKIENFTISAKGNDLFV--NANLLIAHGRRYGLVGPNGHGKTTLLRHIA-----TRAfaippniDVLLCEQEVVATD 421
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTAldDVSLTVAAGEFVALVGPSGCGKSTLLRLIAglekpTSG-------EVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 422 ktaintileADVRrtemlkkadelekqFVAGD------LTVQEelNDTFAeLKAIGAYSAE--ARARRILAGLGFSKEMQ 493
Cdd:COG1116 80 ---------PDRG--------------VVFQEpallpwLTVLD--NVALG-LELRGVPKAErrERARELLELVGLAGFED 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 494 DRPtNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD------LNAV---IWLDNylqgwKKTLLIVSHD 555
Cdd:COG1116 134 AYP-HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDaltrerLQDEllrLWQET-----GKTVLFVTHD 198
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
381-578 |
3.74e-14 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 72.33 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIA--TRAFA--IPPNiDVLLceqevvatDKTAINTILEADVRRTEMLKKADELekqFVagDLTV 456
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAglEKPDGgtIVLN-GTVL--------FDSRKKINLPPQQRKIGLVFQQYAL---FP--HLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 457 QEelNDTFAeLKAIGAYSAEARARRILAGLGFSKeMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVI 536
Cdd:cd03297 93 RE--NLAFG-LKRKRNREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24641342 537 WLDNYLQGWKKTL----LIVSHDQSFLDNVCNEIIHLDQKKLQYYK 578
Cdd:cd03297 169 QLLPELKQIKKNLnipvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
363-571 |
4.03e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.07 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 363 GNDLFVNA-NLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTAintileadVRRTEMLKK 441
Cdd:PRK13537 18 GDKLVVDGlSFHVQRGECFGLLGPNGAGKTTTLRMLL--GLTHPDAGSISLCGEPVPSRARHA--------RQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 442 ADELEKqfvagDLTVQEELNdTFAelKAIGAYSAEARARrILAGLGFSKEMQ--DRPTNKFSGGWRMRVSLARALYLEPT 519
Cdd:PRK13537 88 FDNLDP-----DFTVRENLL-VFG--RYFGLSAAAARAL-VPPLLEFAKLENkaDAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 520 LLMLDEPTNHLDLNA--VIW--LDNYLQGwKKTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:PRK13537 159 VLVLDEPTTGLDPQArhLMWerLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEE 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
369-575 |
4.34e-14 |
|
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: 72.65 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATD--KTAINTILeadvrrtemlkkadele 446
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIA--GFETPTSGEILLDGKDITNLPphKRPVNTVF----------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 447 kQFVA--GDLTVQEelNDTFA-ELKAIGAYSAEARARRILAGLGFsKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLML 523
Cdd:cd03300 79 -QNYAlfPHLTVFE--NIAFGlRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 524 DEPTNHLDL----NAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQ 575
Cdd:cd03300 155 DEPLGALDLklrkDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
673-872 |
4.71e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.30 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG-----------EQRKNHRLHVGR 741
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsvlirgepitkENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQHSGEHL---TAEESAAEYLQRLfNLPHE----KARKALGSFGLvSHAHTIKMKDLSGGQKARVALAELCLSAPDVLI 814
Cdd:PRK13652 83 VFQNPDDQIfspTVEQDIAFGPINL-GLDEEtvahRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 815 LDEPTNNLDIESIDALAEAIN----EYEGGVIIVSHDERLIRETGCTLYVIEDqtiNEIVGE 872
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNdlpeTYGMTVIFSTHQLDLVPEMADYIYVMDK---GRIVAY 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
670-864 |
4.96e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.36 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 670 QPPILGVHNVTFAFPSqkplFIKVDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEG--------------EQ 731
Cdd:COG3842 2 AMPALELENVSKRYGD----VTALD-DVSLSIEpgefVALLGPSGCGKTTLLRMIAGFETPDSGrilldgrdvtglppEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 732 RK------NHRLhvgrFDqhsgeHLTAEESAAEYLqRLFNLP----HEKARKALGSFGLVSHAHTiKMKDLSGGQKARVA 801
Cdd:COG3842 77 RNvgmvfqDYAL----FP-----HLTVAENVAFGL-RMRGVPkaeiRARVAELLELVGLEGLADR-YPHQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 802 LA-----ElclsaPDVLILDEPTNNLDIESIDALAEAINeyeggviivshdeRLIRETGCT-LYVIEDQ 864
Cdd:COG3842 146 LAralapE-----PRVLLLDEPLSALDAKLREEMREELR-------------RLQRELGITfIYVTHDQ 196
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
704-850 |
5.48e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.60 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 704 AIVGPNGVGKSTFLKLLLGELEPQEGE----QRKNHRLHVGRF-----------DQHSGEHLTaeesaaeYLQRLFNLPH 768
Cdd:COG4152 31 GLLGPNGAGKTTTIRIILGILAPDSGEvlwdGEPLDPEDRRRIgylpeerglypKMKVGEQLV-------YLARLKGLSK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 769 EKARKA----LGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEY-EGGVII 843
Cdd:COG4152 104 AEAKRRadewLERLGLGDRANK-KVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaAKGTTV 182
|
170
....*....|...
gi 24641342 844 V--SHD----ERL 850
Cdd:COG4152 183 IfsSHQmelvEEL 195
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
704-823 |
5.66e-14 |
|
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: 72.30 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 704 AIVGPNGVGKSTFLKLLLGELEPQE---------GEQRKNH--RLHVGRFDQHSG--EHLTAEESAAEYLQ-RLFNLPHE 769
Cdd:cd03234 37 AILGSSGSGKTTLLDAISGRVEGGGttsgqilfnGQPRKPDqfQKCVAYVRQDDIllPGLTVRETLTYTAIlRLPRKSSD 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 770 KARKALGSFGLVSH-AHTI----KMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:cd03234 117 AIRKKRVEDVLLRDlALTRiggnLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
369-564 |
7.10e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.22 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPN---IDVLLCEQEVVATDKTAINtileadvrRTEMLKKADEL 445
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG---VLEPTsgeVNVRVGDEWVDMTKPGPDG--------RGRAKRYIGIL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 446 EKQF-------VAGDLT--VQEELNDTFAELKAIgaysaeararRILAGLGFS----KEMQDRPTNKFSGGWRMRVSLAR 512
Cdd:TIGR03269 371 HQEYdlyphrtVLDNLTeaIGLELPDELARMKAV----------ITLKMVGFDeekaEEILDKYPDELSEGERHRVALAQ 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 513 ALYLEPTLLMLDEPTNHLD-LNAVIWLDNYLQGWK---KTLLIVSHDQSFLDNVCN 564
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDpITKVDVTHSILKAREemeQTFIIVSHDMDFVLDVCD 496
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
678-846 |
7.66e-14 |
|
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: 71.87 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrLHVGRFDQHSGEHLTAEESAA 757
Cdd:cd03254 7 NVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQ------ILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 758 EYLQ-------------RLFNLPH-----EKARKALGSFGLVSHA----HTI---KMKDLSGGQKARVALAELCLSAPDV 812
Cdd:cd03254 81 VVLQdtflfsgtimeniRLGRPNAtdeevIEAAKEAGAHDFIMKLpngyDTVlgeNGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 24641342 813 LILDEPTNNLDIESIDALAEAINEYEGG--VIIVSH 846
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAH 196
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
703-888 |
8.42e-14 |
|
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: 70.66 E-value: 8.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQ--EGEQRKN-HRLHVGRFDQHSGehltaeesaaeY-LQRLFNLPHEKARKALgsf 778
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINgRPLDKRSFRKIIG-----------YvPQDDILHPTLTVRETL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 779 glvshAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDieSIDALaeaineyeggvIIVSHDERLiRETGCTL 858
Cdd:cd03213 104 -----MFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD--SSSAL-----------QVMSLLRRL-ADTGRTI 164
|
170 180 190
....*....|....*....|....*....|
gi 24641342 859 YVIEDQTINEIVGEFDdyrKEVLDSLGEVV 888
Cdd:cd03213 165 ICSIHQPSSEIFELFD---KLLLLSQGRVI 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
664-847 |
8.59e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.40 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 664 PEPSQLQPPI-LGVHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRK-NHRLHVGR 741
Cdd:PRK11247 2 MNTARLNQGTpLLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQHsgehLTAEESaaeylqRLfnLP----------------HEKARKALGSFGLVSHAHTIKMKdLSGGQKARVALAEL 805
Cdd:PRK11247 81 EDTR----LMFQDA------RL--LPwkkvidnvglglkgqwRDAALQALAAVGLADRANEWPAA-LSGGQKQRVALARA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24641342 806 CLSAPDVLILDEPTNNLD----IESIDALAEAINEYEGGVIIVSHD 847
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
676-868 |
1.23e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFiKVDFGIDLTSRVAIVGPNGVGKSTFLKLL-------LGEL-----------EPQEGEQRKnHRL 737
Cdd:COG4161 5 LKNINCFYGSHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLniaghqfdfsqKPSEKAIRL-LRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 HVGR-FDQ-HSGEHLTAEESAAEYLQRLFNLPHEKAR----KALGSFGLVSHAHTIKMKdLSGGQKARVALAELCLSAPD 811
Cdd:COG4161 83 KVGMvFQQyNLWPHLTVMENLIEAPCKVLGLSKEQARekamKLLARLRLTDKADRFPLH-LSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 812 VLILDEPTNNLDIESIDALAEAINEY-EGGV--IIVSHDERLIRETGCTLYVIEDQTINE 868
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELsQTGItqVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
371-576 |
1.28e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.21 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 371 NLLIAHGRRYGLVGPNGHGKTTLLRhiatrafaippnidvLLCEQEVVATDKTAINTILEADvRRTEMLKKADEL--EKQ 448
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLK---------------ILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGDLTVQeelnDTFAELKAIgaYSAE-ARARRILAGLGFSKEMQ---DRPTNKFSGGWRMRVSLARALYLEPTLLMLD 524
Cdd:cd03267 105 QLWWDLPVI----DSFYLLAAI--YDLPpARFKKRLDELSELLDLEellDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 525 EPTNHLDLNAVIWLDNYLQGWKK----TLLIVSHDQSFLDNVCNEIIHLDQKKLQY 576
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRergtTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
677-868 |
1.41e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 71.28 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 677 HNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLlGELEPQEGEQRKNHRLHVGrfDQHSGEHLTAEESA 756
Cdd:PRK09493 5 KNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSGDLIVDGLKVN--DPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 757 AEYLQrlFNL-PH-----------------------EKARKALGSFGLVSHAHTIKmKDLSGGQKARVALAELCLSAPDV 812
Cdd:PRK09493 81 MVFQQ--FYLfPHltalenvmfgplrvrgaskeeaeKQARELLAKVGLAERAHHYP-SELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 813 LILDEPTNNLDIE-------SIDALAEaineyEG-GVIIVSHDERLIRETGCTLYVIEDQTINE 868
Cdd:PRK09493 158 MLFDEPTSALDPElrhevlkVMQDLAE-----EGmTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
677-875 |
1.57e-13 |
|
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: 71.03 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 677 HNVTFAFPSQK--PLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE------------------------ 730
Cdd:cd03249 4 KNVSFRYPSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEilldgvdirdlnlrwlrsqiglvs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 731 Q---------RKNHRLhvGRFDQHSGEhltAEESAAEYLQRLF--NLPHeKARKALGSFGlvshahtikmKDLSGGQKAR 799
Cdd:cd03249 84 QepvlfdgtiAENIRY--GKPDATDEE---VEEAAKKANIHDFimSLPD-GYDTLVGERG----------SQLSGGQKQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 800 VALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHdeRL--IRETGCtLYVIEDQTINEiVGEFDD 875
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH--RLstIRNADL-IAVLQNGQVVE-QGTHDE 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
363-555 |
1.57e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.96 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 363 GNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPnidvllceqevvatdktAINTILEADVRRTEMLKKA 442
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAG---VLRP-----------------TSGTVRRAGGARVAYVPQR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 443 DELEKQFvagDLTVQE--ELNdTFAELKAIGAYSAEARAR--RILAGLGFSkEMQDRPTNKFSGGWRMRVSLARALYLEP 518
Cdd:NF040873 64 SEVPDSL---PLTVRDlvAMG-RWARRGLWRRLTRDDRAAvdDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24641342 519 TLLMLDEPTNHLDLNAVIWLDNYLQGW---KKTLLIVSHD 555
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEharGATVVVVTHD 178
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
352-569 |
1.79e-13 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 73.86 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFV-NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPpnidvllcEQEVVATDKTAINTILE 430
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALrPVSFTVPPGERVALVGPSGAGKSTLLNLLL--GFVDP--------TEGSIAVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 ADVRRTemLKKADELeKQFVAGdlTVQEELndTFAELKAIGAYSAEARAR----RILAGL--GFSKEMQDRPTnKFSGGW 504
Cdd:TIGR02857 392 DSWRDQ--IAWVPQH-PFLFAG--TIAENI--RLARPDASDAEIREALERagldEFVAALpqGLDTPIGEGGA-GLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 505 RMRVSLARALYLEPTLLMLDEPTNHLD--LNAVIW--LDNYLQGwkKTLLIVSHDQSFLDNvCNEIIHL 569
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDaeTEAEVLeaLRALAQG--RTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
352-574 |
1.88e-13 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 69.17 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGND--LFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNidvllceQEVVATDKTAINTIL 429
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILG---LLRPT-------SGRVRLDGADISQWD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 EADVRRT-EMLKKADELekqfvagdltvqeeLNDTFAElkaigaysaeararrilaglgfskemqdrptNKFSGGWRMRV 508
Cdd:cd03246 71 PNELGDHvGYLPQDDEL--------------FSGSIAE-------------------------------NILSGGQRQRL 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 509 SLARALYLEPTLLMLDEPTNHLD------LNAVIwldNYLQGWKKTLLIVSHDQSFLdNVCNEIIHLDQKKL 574
Cdd:cd03246 106 GLARALYGNPRILVLDEPNSHLDvegeraLNQAI---AALKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
676-847 |
2.18e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 72.49 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPsQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHR-----LHVGR------FdQ 744
Cdd:COG1118 5 VRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnLPPRErrvgfvF-Q 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 745 HSG--EHLTAEESAAEYLQRLFNLPHEKARKA---LGSFGLVSHAHTiKMKDLSGGQKARVALA-----ElclsaPDVLI 814
Cdd:COG1118 83 HYAlfPHMTVAENIAFGLRVRPPSKAEIRARVeelLELVQLEGLADR-YPSQLSGGQRQRVALAralavE-----PEVLL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 24641342 815 LDEPTNNLDIESIDA----LAEAINEYEGGVIIVSHD 847
Cdd:COG1118 157 LDEPFGALDAKVRKElrrwLRRLHDELGGTTVFVTHD 193
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
352-555 |
2.23e-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: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNA----NLLIAHGRRYGLVGPNGHGKTTLLRHIA-----TRAfaippniDVLLCEQEVVatdk 422
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAlediSLSVEEGEFVALVGPSGCGKSTLLRIIAglerpTSG-------EVLVDGEPVT---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 423 taintilEADVRRTEMLKKADELEKqfvagdLTVQEelNDTFA-ELKAIGAYSAEARARRILAGLGFSKEMQDRPtNKFS 501
Cdd:cd03293 70 -------GPGPDRGYVFQQDALLPW------LTVLD--NVALGlELQGVPKAEARERAEELLELVGLSGFENAYP-HQLS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 502 GGWRMRVSLARALYLEPTLLMLDEPTNHLDlnAVI------WLDNYLQGWKKTLLIVSHD 555
Cdd:cd03293 134 GGMRQRVALARALAVDPDVLLLDEPFSALD--ALTreqlqeELLDIWRETGKTVLLVTHD 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
371-570 |
3.08e-13 |
|
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: 70.16 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 371 NLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTAIntileADVRRTEMlkkadelekQFV 450
Cdd:COG4181 32 SLEVEAGESVAIVGASGSGKSTLLGLLA--GLDRPTSGTVRLAGQDLFALDEDAR-----ARLRARHV---------GFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 451 ------AGDLTVQE------ELNdtfaelkaiGAYSAEARARRILAGLGFSKEMQDRPtNKFSGGWRMRVSLARALYLEP 518
Cdd:COG4181 96 fqsfqlLPTLTALEnvmlplELA---------GRRDARARARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 519 TLLMLDEPTNHLD-------------LNAViwldnylQGwkKTLLIVSHDQSfLDNVCNEIIHLD 570
Cdd:COG4181 166 AILFADEPTGNLDaatgeqiidllfeLNRE-------RG--TTLVLVTHDPA-LAARCDRVLRLR 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
352-569 |
3.52e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRhiATRAFAIPPNIDVLLCEQEVVATDKTAINtilea 431
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLR--AINGTLTPTAGTVLVAGDDVEALSARAAS----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 dvRRTemlkkADELEKQFVAGDLTVQE--ELNDTFAELKAIGAYSAEARA-RRILAGLGFSKeMQDRPTNKFSGGWRMRV 508
Cdd:PRK09536 77 --RRV-----ASVPQDTSLSFEFDVRQvvEMGRTPHRSRFDTWTETDRAAvERAMERTGVAQ-FADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 509 SLARALYLEPTLLMLDEPTNHLDLNAVIW---LDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHL 569
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLDINHQVRtleLVRRLVDDGKTAVAAIHDLDLAARYCDELVLL 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
352-555 |
3.73e-13 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 69.90 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIA---TRAFAIPPNIDVLLCEQEVVATDKTAINti 428
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlnDLIPGAPDEGEVLLDGKDIYDLDVDVLE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 429 leadVRRT-EML-KKADELEKQF---VAGDLTVQEELNDTFAElkaigaysaeARARRILAGLGFSKEMQDRPT-NKFSG 502
Cdd:cd03260 79 ----LRRRvGMVfQKPNPFPGSIydnVAYGLRLHGIKLKEELD----------ERVEEALRKAALWDEVKDRLHaLGLSG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 503 GWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK--TLLIVSHD 555
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
687-866 |
3.76e-13 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 69.50 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 687 KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGR----------FDQHS-GEHLTAEES 755
Cdd:TIGR01277 11 EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLapyqrpvsmlFQENNlFAHLTVRQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 AAEYLQ---RLFNLPHEKARKALGSFGLVSHAHTIKmKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD----IESID 828
Cdd:TIGR01277 91 IGLGLHpglKLNAEQQEKVVDAAQQVGIADYLDRLP-EQLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEMLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 24641342 829 ALAEAINEYEGGVIIVSHDERLIRETGCTLYVIEDQTI 866
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
705-823 |
4.05e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 705 IVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNH-RLHVGRFDQHsgEHLTAEESAAEYLQ---RLFNLPHEKA 771
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSislcgepvpSRARHaRQRVGVVPQF--DNLDPDFTVRENLLvfgRYFGLSAAAA 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 772 RKA---LGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:PRK13537 116 RALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
678-846 |
4.71e-13 |
|
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: 69.42 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQ--KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNHRLH-----VGR 741
Cdd:cd03248 16 NVTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQvlldgkpisQYEHKYLHskvslVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQHSGEHLTaeESAAEYLQRL-FNLPHEKARKAlgsfglvsHAHTIKMK--------------DLSGGQKARVALAELC 806
Cdd:cd03248 96 EPVLFARSLQ--DNIAYGLQSCsFECVKEAAQKA--------HAHSFISElasgydtevgekgsQLSGGQKQRVAIARAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24641342 807 LSAPDVLILDEPTNNLDIESIDALAEAINEY--EGGVIIVSH 846
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
674-818 |
4.82e-13 |
|
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: 69.04 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQKPLFIKVDFGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGeqrknHRLHVGRFDqhsgeh 749
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPkgelVAIVGPVGSGKSSLLSALLGELEKLSG-----SVSVPGSIA------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 750 LTAEESaaeYLQR-------LFNLPHEKAR--KALGSFGLVshahtikmKD------------------LSGGQKARVAL 802
Cdd:cd03250 70 YVSQEP---WIQNgtireniLFGKPFDEERyeKVIKACALE--------PDleilpdgdlteigekginLSGGQKQRISL 138
|
170
....*....|....*.
gi 24641342 803 AELCLSAPDVLILDEP 818
Cdd:cd03250 139 ARAVYSDADIYLLDDP 154
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
702-866 |
4.92e-13 |
|
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: 69.06 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 702 RVAIVGPNGVGKSTFLKLLLGELEPQEGeqrknhRLHVGRFDQHSGE-----------------HLTAEESAAEYLQ--- 761
Cdd:cd03298 26 ITAIVGPSGSGKSTLLNLIAGFETPQSG------RVLINGVDVTAAPpadrpvsmlfqennlfaHLTVEQNVGLGLSpgl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 762 RLFNLPHEKARKALGSFGLVShahtiKMK----DLSGGQKARVALAELCLSAPDVLILDEPTNNLD----IESIDALAEA 833
Cdd:cd03298 100 KLTAEDRQAIEVALARVGLAG-----LEKrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|...
gi 24641342 834 INEYEGGVIIVSHDERLIRETGCTLYVIEDQTI 866
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
369-570 |
5.25e-13 |
|
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: 69.39 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHI----ATRAFAIppnidvllceqeVVATDKTAINtILEADVRrtEMLkkadE 444
Cdd:COG4778 29 GVSFSVAAGECVALTGPSGAGKSTLLKCIygnyLPDSGSI------------LVRHDGGWVD-LAQASPR--EIL----A 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 445 LEK-------QFvagdltvqeeLN--------DTFAE-LKAIG--AYSAEARARRILAGLGFSKEMQDRPTNKFSGGWRM 506
Cdd:COG4778 90 LRRrtigyvsQF----------LRviprvsalDVVAEpLLERGvdREEARARARELLARLNLPERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 507 RVSLARALYLEPTLLMLDEPTNHLDL---NAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLD 570
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAanrAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
673-872 |
6.08e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.11 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRK---NHRLHV 739
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvlikgepikyDKKsllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHSGEHL---TAEESAAEYLQRLfNLPHEKARK----ALGSFGLVSHAHTIKmKDLSGGQKARVALAELCLSAPDV 812
Cdd:PRK13639 81 GIVFQNPDDQLfapTVEEDVAFGPLNL-GLSKEEVEKrvkeALKAVGMEGFENKPP-HHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 813 LILDEPTNNLD---IESIDALAEAINEyEGGVIIVS-HDERLIRETGCTLYVIEDqtiNEIVGE 872
Cdd:PRK13639 159 IVLDEPTSGLDpmgASQIMKLLYDLNK-EGITIIIStHDVDLVPVYADKVYVMSD---GKIIKE 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
369-557 |
8.05e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 70.90 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVAtdktaintiLEADVRRTEMlkkadelekq 448
Cdd:COG3842 23 DVSLSIEPGEFVALLGPSGCGKTTLLRMIA--GFETPDSGRILLDGRDVTG---------LPPEKRNVGM---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 fVAGD------LTVQEelNDTFAeLKAIGAYSAEARAR--RILA--GLGfskEMQDRPTNKFSGGWRMRVSLARALYLEP 518
Cdd:COG3842 82 -VFQDyalfphLTVAE--NVAFG-LRMRGVPKAEIRARvaELLElvGLE---GLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24641342 519 TLLMLDEPTNHLDLNA----VIWLDNYLQGWKKTLLIVSHDQS 557
Cdd:COG3842 155 RVLLLDEPLSALDAKLreemREELRRLQRELGITFIYVTHDQE 197
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
693-850 |
8.13e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 8.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------------QRKNHRLHVGRFDQHSGEHLTAEES 755
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvifngqpmsklssaakaELRNQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 AAEYLQRLFNLP---HEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAE 832
Cdd:PRK11629 108 VAMPLLIGKKKPaeiNSRALEMLAAVGLEHRANH-RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180
....*....|....*....|..
gi 24641342 833 ---AINEYEG-GVIIVSHDERL 850
Cdd:PRK11629 187 llgELNRLQGtAFLVVTHDLQL 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
678-892 |
8.21e-13 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 68.76 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDfGIDLT----SRVAIVGPNGVGKSTFLKLLLGeLE-PQEGE--------------QRKNHRLH 738
Cdd:cd03258 6 NVSKVFGDTGGKVTALK-DVSLSvpkgEIFGIIGRSGAGKSTLIRCING-LErPTSGSvlvdgtdltllsgkELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 739 VGRFDQHSgeHLTAEESAAE---YLQRLFNLP----HEKARKALGSFGLvSHAHTIKMKDLSGGQKARVALAELCLSAPD 811
Cdd:cd03258 84 IGMIFQHF--NLLSSRTVFEnvaLPLEIAGVPkaeiEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 812 VLILDEPTNNLDIE---SIDALAEAINEYEG-GVIIVSHDERLIRETGCTLYVIEDqtiNEIVGEFDdyrkevldsLGEV 887
Cdd:cd03258 161 VLLCDEATSALDPEttqSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEK---GEVVEEGT---------VEEV 228
|
....*
gi 24641342 888 VNNPS 892
Cdd:cd03258 229 FANPQ 233
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
693-880 |
8.93e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.95 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHR------LHVGrFDQhsgeHLTAEESAaeYLQ-RLFN 765
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsalleLGAG-FHP----ELTGRENI--YLNgRLLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 766 LPHEKARKALGS---F-GLVSHAHTiKMKDLSGGQKARVALAelcLSA---PDVLILDEptnNL---DIE----SIDALA 831
Cdd:COG1134 118 LSRKEIDEKFDEiveFaELGDFIDQ-PVKTYSSGMRARLAFA---VATavdPDILLVDE---VLavgDAAfqkkCLARIR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 832 EAINEyEGGVIIVSHDERLIRETgCT--LY-----VIEDQTINEIVgefDDYRKEV 880
Cdd:COG1134 191 ELRES-GRTVIFVSHSMGAVRRL-CDraIWlekgrLVMDGDPEEVI---AAYEALL 241
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
692-857 |
9.04e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.71 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 692 KVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHR------LHVGrFDqhsgEHLTAEESAAEYLqRLFN 765
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllgLGGG-FN----PELTGRENIYLNG-RLLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 766 LPHEKARKA---------LGSFGlvshahTIKMKDLSGGQKARVALAelcLSA---PDVLILDEPTNNLDIE----SIDA 829
Cdd:cd03220 114 LSRKEIDEKideiiefseLGDFI------DLPVKTYSSGMKARLAFA---IATalePDILLIDEVLAVGDAAfqekCQRR 184
|
170 180
....*....|....*....|....*...
gi 24641342 830 LAEAINEyEGGVIIVSHDERLIRETgCT 857
Cdd:cd03220 185 LRELLKQ-GKTVILVSHDPSSIKRL-CD 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
364-577 |
9.17e-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: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 364 NDLFVNanllIAHGRRYGLVGPNGHGKTTLLRHIATRafaIPPNIDVLLCEQEVVATDKTAI----------NTILEadv 433
Cdd:cd03263 19 DDLSLN----VYKGEIFGLLGHNGAGKTTTLKMLTGE---LRPTSGTAYINGYSIRTDRKAArqslgycpqfDALFD--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 434 rrtemlkkadelekqfvagDLTVQEELNdTFAELKAIGAYSAEARARRILAGLGFSKEmQDRPTNKFSGGWRMRVSLARA 513
Cdd:cd03263 89 -------------------ELTVREHLR-FYARLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 514 LYLEPTLLMLDEPTNHLDLNA--VIWldNYLQGWKK--TLLIVSHDQSFLDNVCNEIIHLDQKKLQYY 577
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASrrAIW--DLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDGKLRCI 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
693-847 |
9.30e-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: 68.90 E-value: 9.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG--------------EQR------KNHRLHvgrfdqhsgEHLTA 752
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGkillngkditnlppEKRdisyvpQNYALF---------PHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 753 EESAAEYLQRLFNLPHEKARKALGSFGLVSHAHTI--KMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIES---- 826
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLnrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkekl 168
|
170 180
....*....|....*....|.
gi 24641342 827 IDALAEAINEYEGGVIIVSHD 847
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHD 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
369-531 |
9.82e-13 |
|
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: 71.64 E-value: 9.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTL----LRHIATRAfaippniDVLLCEQEVVATDKTAINTileadvRRTEMlkkade 444
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLglalLRLIPSEG-------EIRFDGQDLDGLSRRALRP------LRRRM------ 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 445 lekQFVAGD--------LTVQEelndTFAE---LKAIGAYSAE--ARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLA 511
Cdd:COG4172 365 ---QVVFQDpfgslsprMTVGQ----IIAEglrVHGPGLSAAErrARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIA 437
|
170 180
....*....|....*....|
gi 24641342 512 RALYLEPTLLMLDEPTNHLD 531
Cdd:COG4172 438 RALILEPKLLVLDEPTSALD 457
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
676-868 |
9.85e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 9.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFiKVDFGIDLTSRVAIVGPNGVGKSTFLKLL-------LGELE-----------PQEGEQRKnHRL 737
Cdd:PRK11124 5 LNGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNiagnhfdfsktPSDKAIRE-LRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 HVGR-FDQ-HSGEHLTAEESAAEYLQRLFNL----PHEKARKALGSFGLVSHAHTIKMKdLSGGQKARVALAELCLSAPD 811
Cdd:PRK11124 83 NVGMvFQQyNLWPHLTVQQNLIEAPCRVLGLskdqALARAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 812 VLILDEPTNNLDIESIDALAEAINEY-EGGV--IIVSHDERLIRETGCTLYVIEDQTINE 868
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELaETGItqVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
369-571 |
1.05e-12 |
|
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: 68.91 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATRafaIPPNI-DVLLCEQEVvaTDKTAiNTILEADVRRTemlkkadelek 447
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGF---YRPTSgRILFDGRDI--TGLPP-HRIARLGIART----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 448 qF----VAGDLTVQEEL---------NDTFAELKAIGAYSAE-----ARARRILAGLGFSkEMQDRPTNKFSGGWRMRVS 509
Cdd:COG0411 85 -FqnprLFPELTVLENVlvaaharlgRGLLAALLRLPRARREerearERAEELLERVGLA-DRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 510 LARALYLEPTLLMLDEPT---NHLDLNAVI-WLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:COG0411 163 IARALATEPKLLLLDEPAaglNPEETEELAeLIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
676-863 |
1.07e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 66.68 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLfikvDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNhrlhvGRfdqhsgehlt 751
Cdd:cd03216 3 LRGITKRFGGVKAL----D-GVSLSVRrgevHALLGENGAGKSTLMKILSGLYKPDSGEILVD-----GK---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 752 aeesaaeylQRLFNLPHEkARKAlGsFGLVSHahtikmkdLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALA 831
Cdd:cd03216 63 ---------EVSFASPRD-ARRA-G-IAMVYQ--------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190
....*....|....*....|....*....|....*
gi 24641342 832 EAINEY--EG-GVIIVSHDERLIRETGCTLYVIED 863
Cdd:cd03216 123 KVIRRLraQGvAVIFISHRLDEVFEIADRVTVLRD 157
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
687-851 |
1.13e-12 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 66.61 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 687 KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLK---LLLGelepqeGEQRKNHRlhvgRFDQHSGehltaEESAAEYLQRL 763
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALG------GAQSATRR----RSGVKAG-----CIVAAVSAELI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 764 FNLPHekarkalgsfglvshahtikmkdLSGGQKARVALA---ELCLSAPDVL-ILDEPTNNLDIESIDALAEAINEYEG 839
Cdd:cd03227 73 FTRLQ-----------------------LSGGEKELSALAlilALASLKPRPLyILDEIDRGLDPRDGQALAEAILEHLV 129
|
170
....*....|....*
gi 24641342 840 G---VIIVSHDERLI 851
Cdd:cd03227 130 KgaqVIVITHLPELA 144
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
353-531 |
1.29e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 67.89 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 353 KIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNI----DVLLceqevvatDKTAINTi 428
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG---TLSPAFsasgEVLL--------NGRRLTA- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 429 LEADVRRTEMLKKADELekqF----VAGDLTvqeelndtFAELKAIGAYSAEARARRILAGLGFSKeMQDRPTNKFSGGW 504
Cdd:COG4136 71 LPAEQRRIGILFQDDLL---FphlsVGENLA--------FALPPTIGRAQRRARVEQALEEAGLAG-FADRDPATLSGGQ 138
|
170 180
....*....|....*....|....*..
gi 24641342 505 RMRVSLARALYLEPTLLMLDEPTNHLD 531
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
673-847 |
1.37e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.99 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG-----------EQRKNHRLHVGR 741
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrvkvmgrevnaENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQHSGEHL---TAEESAAEYLQRLFNLPHE---KARKALGSFGLVSHAHTIKMKdLSGGQKARVALAELCLSAPDVLIL 815
Cdd:PRK13647 84 VFQDPDDQVfssTVWDDVAFGPVNMGLDKDEverRVEEALKAVRMWDFRDKPPYH-LSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 24641342 816 DEPTNNLDIESIDALAEAINEY--EGGVIIVS-HD 847
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLhnQGKTVIVAtHD 197
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
352-573 |
1.38e-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: 67.69 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNIDVLLCEQEVVAtdktaintilEA 431
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG---IILPDSGEVLFDGKPLD----------IA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEMLKKADELEKqfvagDLTVQEELNdTFAELKAIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVSLA 511
Cdd:cd03269 68 ARNRIGYLPEERGLYP-----KMKVIDQLV-YLAQLKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 512 RALYLEPTLLMLDEPTNHLD-LNAVIWLD--NYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKK 573
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDpVNVELLKDviRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
337-574 |
1.41e-12 |
|
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: 71.29 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 337 QKSAGQKAALEQAVDIKIENFTISAKGNDLFV--NANLLIAHGRRYGLVGPNGHGKTTLLRHIaTRaFAIPPNIDVLLce 414
Cdd:TIGR02203 316 EKDTGTRAIERARGDVEFRNVTFRYPGRDRPAldSISLVIEPGETVALVGRSGSGKSTLVNLI-PR-FYEPDSGQILL-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 415 qevvatDKTAINTILEADVRRtemlkkadelEKQFVAGDLTVqeeLNDTFAELKAIGAYS--AEARARRILAG------- 485
Cdd:TIGR02203 392 ------DGHDLADYTLASLRR----------QVALVSQDVVL---FNDTIANNIAYGRTEqaDRAEIERALAAayaqdfv 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 486 ----LGFSKEMQDRPTNkFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD------LNAViwLDNYLQGwkKTLLIVSHD 555
Cdd:TIGR02203 453 dklpLGLDTPIGENGVL-LSGGQRQRLAIARALLKDAPILILDEATSALDneserlVQAA--LERLMQG--RTTLVIAHR 527
|
250
....*....|....*....
gi 24641342 556 QSFLDNVcNEIIHLDQKKL 574
Cdd:TIGR02203 528 LSTIEKA-DRIVVMDDGRI 545
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
690-836 |
1.47e-12 |
|
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: 67.78 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 690 FIKVDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEQR----------KNHRLHVGRFDQHSG--EHLTAE 753
Cdd:cd03265 13 FEAVR-GVSFRVRrgeiFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvaghdvvrepREVRRRIGIVFQDLSvdDELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 754 ESAaeYLQ-RLFNLPHEKARK----ALGSFGLVSHAHTIkMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESID 828
Cdd:cd03265 92 ENL--YIHaRLYGVPGAERRErideLLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
....*...
gi 24641342 829 ALAEAINE 836
Cdd:cd03265 169 HVWEYIEK 176
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
352-585 |
1.83e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.12 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLR-------------HIATRAFAIPPNIDvllceqevv 418
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRvlnlletpdsgqlNIAGHQFDFSQKPS--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 419 atdktaintilEADVRrtEMLKKADELEKQF-VAGDLTVQEELndTFAELKAIGAYSAEARAR--RILAGLGFSkEMQDR 495
Cdd:COG4161 74 -----------EKAIR--LLRQKVGMVFQQYnLWPHLTVMENL--IEAPCKVLGLSKEQAREKamKLLARLRLT-DKADR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 496 PTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD---LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQK 572
Cdd:COG4161 138 FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeiTAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKG 217
|
250
....*....|...
gi 24641342 573 KLQYYkGNYSMFK 585
Cdd:COG4161 218 RIIEQ-GDASHFT 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
676-846 |
2.13e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.54 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAF----PSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-------------QRKNHRLH 738
Cdd:PRK13637 5 IENLTHIYmegtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvditdkkvKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 739 VGRFDQHSgEHLTAEESAA---EYLQRLFNLP----HEKARKALGSFGLvsHAHTIKMK---DLSGGQKARVALAELCLS 808
Cdd:PRK13637 85 VGLVFQYP-EYQLFEETIEkdiAFGPINLGLSeeeiENRVKRAMNIVGL--DYEDYKDKspfELSGGQKRRVAIAGVVAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24641342 809 APDVLILDEPTNNLDIESIDALAEAI----NEYEGGVIIVSH 846
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIkelhKEYNMTIILVSH 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
339-555 |
2.16e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 70.47 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 339 SAGQKAALEQAVDIKIENFTISAKGNDLFVNA-NLLIAHGRRYGLVGPNGHGKTTLLrhiATRAFAIPPnidvllcEQEV 417
Cdd:TIGR02868 322 APAAGAVGLGKPTLELRDLSAGYPGAPPVLDGvSLDLPPGERVAILGPSGSGKSTLL---ATLAGLLDP-------LQGE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 418 VATDKTAINTILEADVRRTEMLkkadeLEKQFVAGDLTVQEEL-----NDTFAELkaigaYSAEARAR--RILAGL--GF 488
Cdd:TIGR02868 392 VTLDGVPVSSLDQDEVRRRVSV-----CAQDAHLFDTTVRENLrlarpDATDEEL-----WAALERVGlaDWLRALpdGL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 489 SKEMQDRPTnKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD----------LNAViwldnyLQGwkKTLLIVSHD 555
Cdd:TIGR02868 462 DTVLGEGGA-RLSGGERQRLALARALLADAPILLLDEPTEHLDaetadelledLLAA------LSG--RTVVLITHH 529
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
352-556 |
2.19e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 69.41 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIA---TrafaipPNidvllcEQEVVATDKTAiNTI 428
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAgleT------PD------SGRIVLNGRDL-FTN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 429 LEADVRRTemlkkadelekQFVAGD------LTVQEelNDTFAeLKAIGAYSAEARAR------RI-LAGLGfskemqDR 495
Cdd:COG1118 70 LPPRERRV-----------GFVFQHyalfphMTVAE--NIAFG-LRVRPPSKAEIRARveelleLVqLEGLA------DR 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 496 -PTNkFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDlNAV-----IWLDNYLQGWKKTLLIVSHDQ 556
Cdd:COG1118 130 yPSQ-LSGGQRQRVALARALAVEPEVLLLDEPFGALD-AKVrkelrRWLRRLHDELGGTTVFVTHDQ 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
703-847 |
2.22e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.04 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGeLEPQEGEQrknhrlhvgRFDQHSGEHLTAEESAAE--YL---QR-LFNLP--------- 767
Cdd:PRK03695 25 LHLVGPNGAGKSTLLARMAG-LLPGSGSI---------QFAGQPLEAWSAAELARHraYLsqqQTpPFAMPvfqyltlhq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 768 HEKARKALGSFGLVSHAHTIKMKD--------LSGGQKARVALAELCLS-APDV------LILDEPTNNLDIESIDALAE 832
Cdd:PRK03695 95 PDKTRTEAVASALNEVAEALGLDDklgrsvnqLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDVAQQAALDR 174
|
170
....*....|....*...
gi 24641342 833 AINEY--EGGVIIVS-HD 847
Cdd:PRK03695 175 LLSELcqQGIAVVMSsHD 192
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
705-849 |
2.40e-12 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 69.06 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 705 IVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNHRLHVGRFDQHSG--EHLTAEESAAeYLQRLFNLPHE---- 769
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSimldgedvtNVPPHLRHINMVFQSYAlfPHMTVEENVA-FGLKMRKVPRAeikp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 770 KARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALA---EAINEYEG-GVIIVS 845
Cdd:TIGR01187 80 RVLEALRLVQLEEFADR-KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlelKTIQEQLGiTFVFVT 158
|
....
gi 24641342 846 HDER 849
Cdd:TIGR01187 159 HDQE 162
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
363-587 |
2.60e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 70.66 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 363 GNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafaippnidvllceqEVVATDKTaintileadVRRTEMLKKA 442
Cdd:PLN03073 521 GPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG----------------ELQPSSGT---------VFRSAKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 443 dELEKQFVAG-DLTVQeelndtfAELKAIGAYSA--EARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPT 519
Cdd:PLN03073 576 -VFSQHHVDGlDLSSN-------PLLYMMRCFPGvpEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPH 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 520 LLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSMFKKM 587
Cdd:PLN03073 648 ILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKT 715
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
695-862 |
2.69e-12 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 67.07 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 695 FGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKN---------HRL------HV--GR--FDQHS----- 746
Cdd:cd03224 17 FGVSLTVPegeiVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglppHERaragigYVpeGRriFPELTveenl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 747 --GEHLTAEESAAEYLQRLFNL-P--HEKaRKALGSfglvshahtikmkDLSGGQKARVALAELCLSAPDVLILDEPTNN 821
Cdd:cd03224 97 llGAYARRRAKRKARLERVYELfPrlKER-RKQLAG-------------TLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24641342 822 LD---IESIDALAEAINEYEGGVIIVSHDERLIRETGCTLYVIE 862
Cdd:cd03224 163 LApkiVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLE 206
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
696-853 |
2.78e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.40 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLTSR----VAIVGPNGVGKSTFLKLLLG--ELEPQEGEQRknhrlhvgrFDqhsGE---HLTAEESA---------- 756
Cdd:COG0396 18 GVNLTIKpgevHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSIL---------LD---GEdilELSPDERAragiflafqy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 757 ---------AEYLQRLFNLPHEKARKALGSFGLVSHahtiKMKDL---------------SGGQKARVALAELCLSAPDV 812
Cdd:COG0396 86 pveipgvsvSNFLRTALNARRGEELSAREFLKLLKE----KMKELgldedfldryvnegfSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24641342 813 LILDEPTNNLDIESIDALAEAINEY---EGGVIIVSHDERLIRE 853
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLrspDRGILIITHYQRILDY 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
676-844 |
2.82e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.09 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE------------QRKNHRLHVGRFD 743
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKvlvsgidtgdfsKLQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 744 QHSGEHL---TAEESAAEYLQRLFnLPHEKARK----ALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILD 816
Cdd:PRK13644 84 QNPETQFvgrTVEEDLAFGPENLC-LPPIEIRKrvdrALAEIGLEKYRHR-SPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180
....*....|....*....|....*....
gi 24641342 817 EPTNNLDIESIDALAEAINE-YEGGVIIV 844
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKlHEKGKTIV 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
369-562 |
3.12e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.57 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDV-LLCEQEVVATDKTAINTILEADV---RRTEMLKKADE 444
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHL--NALLLPDTGTIeWIFKDEKNKKKTKEKEKVLEKLViqkTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 445 LEK------QFVAGDLTVQEELNDTFAELKAIGAYSAEA--RARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYL 516
Cdd:PRK13651 103 IRRrvgvvfQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAkkRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24641342 517 EPTLLMLDEPTNHLDLNAVI----WLDN-YLQGwkKTLLIVSHDqsfLDNV 562
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKeileIFDNlNKQG--KTIILVTHD---LDNV 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
381-605 |
3.16e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIATRafaippnidvllcEQ------EVVATDKTAIntileADVRRtemlkkaDELEkqfvaGDL 454
Cdd:PRK11819 354 GIIGPNGAGKSTLFKMITGQ-------------EQpdsgtiKIGETVKLAY-----VDQSR-------DALD-----PNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 455 TVQEELNDTFAELKaIGAYSAEARArrILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNA 534
Cdd:PRK11819 404 TVWEEISGGLDIIK-VGNREIPSRA--YVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 535 VIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHL-DQKKLQYYKGNYSmfkkmyvqkrremikEYEKQEKR 605
Cdd:PRK11819 481 LRALEEALLEFPGCAVVISHDRWFLDRIATHILAFeGDSQVEWFEGNFQ---------------EYEEDKKR 537
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
693-823 |
5.45e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 67.35 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRKNHRLHVGRfdQHSG------EHLTAEESA 756
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTvtigervitaGKKNKKLKPLR--KKVGivfqfpEHQLFEETV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 757 AE---YLQRLFNLPHEKA-RKALGSFGLVSHAHTIKMK---DLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:PRK13634 104 EKdicFGPMNFGVSEEDAkQKAREMIELVGLPEELLARspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
352-556 |
7.51e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 67.94 E-value: 7.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEV--VATDKTAINTIL 429
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLA--GFEQPTAGQIMLDGVDLshVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 EADVRRTEMlkkadelekqfvagdlTVqeELNDTFAeLKAIGAYSAEARAR-RILAGLGFSKEMQDRPTNKFSGGWRMRV 508
Cdd:PRK11607 98 QSYALFPHM----------------TV--EQNIAFG-LKQDKLPKAEIASRvNEMLGLVHMQEFAKRKPHQLSGGQRQRV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24641342 509 SLARALYLEPTLLMLDEPTNHLD--LNAVIWLD--NYLQGWKKTLLIVSHDQ 556
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
352-556 |
7.76e-12 |
|
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: 65.74 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVvatdktainTILEA 431
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIA--GLEEPTSGRIYIGGRDV---------TDLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEMLKKADELEKQfvagdLTVQEelNDTFA-ELKAIGAYSAEARARRILAGLGFSKEMQDRPTnKFSGGWRMRVSL 510
Cdd:cd03301 70 KDRDIAMVFQNYALYPH-----MTVYD--NIAFGlKLRKVPKDEIDERVREVAELLQIEHLLDRKPK-QLSGGQRQRVAL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24641342 511 ARALYLEPTLLMLDEPTNHLD----LNAVIWLDNYLQGWKKTLLIVSHDQ 556
Cdd:cd03301 142 GRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
659-868 |
8.14e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.70 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 659 VKFRFPEPSQLQPPILGVHNVTFAFPSQKPLFIKvdfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKN 734
Cdd:PRK11160 324 VTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLK---GLSLQikagEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 735 HRlhvgRFDQHSGEHLTAEESAAEylQR--LF------NL----PH---EKARKALGSFGLVSHAHTIKMKD-------- 791
Cdd:PRK11160 401 GQ----PIADYSEAALRQAISVVS--QRvhLFsatlrdNLllaaPNasdEALIEVLQQVGLEKLLEDDKGLNawlgeggr 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 792 -LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHdeRLireTGCT----LYVIEDQ 864
Cdd:PRK11160 475 qLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNktVLMITH--RL---TGLEqfdrICVMDNG 549
|
....
gi 24641342 865 TINE 868
Cdd:PRK11160 550 QIIE 553
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
674-846 |
8.97e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.76 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQKPLFikvDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNhrlhvgrfdqhsGEHLTAE 753
Cdd:PRK10771 2 LKLTDITWLYHHLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN------------GQDHTTT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 754 ESAAEYLQRLF---NL-PHEKARKALGsFGL-----VSHAHTIKMKD-----------------LSGGQKARVALAElCL 807
Cdd:PRK10771 67 PPSRRPVSMLFqenNLfSHLTVAQNIG-LGLnpglkLNAAQREKLHAiarqmgiedllarlpgqLSGGQRQRVALAR-CL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24641342 808 --SAPdVLILDEPTNNLD----IESIDALAEAINEYEGGVIIVSH 846
Cdd:PRK10771 145 vrEQP-ILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
352-557 |
1.02e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 65.82 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENftISAKGNDLFV-NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVvatdktainTILE 430
Cdd:cd03299 1 LKVEN--LSKDWKEFKLkNVSLEVERGDYFVILGPTGSGKSVLLETIA--GFIKPDSGKILLNGKDI---------TNLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 ADVRRtemlkkadeleKQFVAGD------LTVQEelNDTFA-ELKAIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGG 503
Cdd:cd03299 68 PEKRD-----------ISYVPQNyalfphMTVYK--NIAYGlKKRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 504 WRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK----TLLIVSHDQS 557
Cdd:cd03299 134 EQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefgvTVLHVTHDFE 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
355-535 |
1.05e-11 |
|
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: 64.82 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 355 ENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNIDVLLCEQEVVATDKTAINtileadvR 434
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAG---LSPPLAGRVLLNGGPLDFQRDSIA-------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 435 RTEMLKKADELEkqfvaGDLTVQEELndTFaeLKAIGAYSA--EARARRILAGLGfskemqDRPTNKFSGGWRMRVSLAR 512
Cdd:cd03231 74 GLLYLGHAPGIK-----TTLSVLENL--RF--WHADHSDEQveEALARVGLNGFE------DRPVAQLSAGQQRRVALAR 138
|
170 180
....*....|....*....|...
gi 24641342 513 ALYLEPTLLMLDEPTNHLDLNAV 535
Cdd:cd03231 139 LLLSGRPLWILDEPTTALDKAGV 161
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
673-847 |
1.09e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.41 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRK---NHRLHV 739
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRilfdgkpidySRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHSGEHLTaeeSAAEYLQRLF-----NLP----HEKARKALGSFGlVSHAHTIKMKDLSGGQKARVALAELCLSAP 810
Cdd:PRK13636 85 GMVFQDPDNQLF---SASVYQDVSFgavnlKLPedevRKRVDNALKRTG-IEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24641342 811 DVLILDEPTNNLDIESIDALAEAINEYEGG----VIIVSHD 847
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKElgltIIIATHD 201
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
372-576 |
1.25e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 64.82 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 372 LLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTAintileadvRRTEMLkkadelekqfva 451
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIA--GFETPQSGRVLINGVDVTAAPPAD---------RPVSML------------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 452 gdltVQEelNDTFAEL---KAIG-------AYSAEARAR--RILAGLGFSKEMQDRPtNKFSGGWRMRVSLARALYLEPT 519
Cdd:cd03298 76 ----FQE--NNLFAHLtveQNVGlglspglKLTAEDRQAieVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 520 LLMLDEPTNHLD---LNAVIWLDNYL-QGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQY 576
Cdd:cd03298 149 VLLLDEPFAALDpalRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
369-574 |
1.30e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 65.12 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATRAfaIPPNIDVLLCEQEVVATDKTAIntileADVRRTEMLKKADELekq 448
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEE--LPTSGTIRVNGQDVSDLRGRAI-----PYLRRKIGVVFQDFR--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 fVAGDLTVQEelNDTFAeLKAIGAYSAEARAR--RILAGLGFSKEMQDRPtNKFSGGWRMRVSLARALYLEPTLLMLDEP 526
Cdd:cd03292 89 -LLPDRNVYE--NVAFA-LEVTGVPPREIRKRvpAALELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24641342 527 TNHLDLNAVIWLDNYLQGWKK---TLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKagtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
676-853 |
1.43e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFikvdfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGeqrknhRLHVGRFDQHSGEHLT 751
Cdd:PRK11264 6 VKNLVKKFHGQTVLH-----GIDLEVKpgevVAIIGPSGSGKTTLLRCINLLEQPEAG------TIRVGDITIDTARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 752 AEESAAEYLQRL-------FNL-PH-----------------------EKARKALGSFGLvSHAHTIKMKDLSGGQKARV 800
Cdd:PRK11264 75 QQKGLIRQLRQHvgfvfqnFNLfPHrtvleniiegpvivkgepkeeatARARELLAKVGL-AGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 801 ALAELCLSAPDVLILDEPTNNLDIE-------SIDALAEAineyEGGVIIVSHDERLIRE 853
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPElvgevlnTIRQLAQE----KRTMVIVTHEMSFARD 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
678-847 |
1.50e-11 |
|
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: 65.40 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNH-----------RLHVGRFDQHS 746
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelRRKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 747 G--EHLTAEESAAEYLQRLFNLPHEKARKALGSFGLVsHAHTIKMKD-----LSGGQKARVALAELCLSAPDVLILDEPT 819
Cdd:cd03295 85 GlfPHMTVEENIALVPKLLKWPKEKIRERADELLALV-GLDPAEFADrypheLSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190
....*....|....*....|....*....|..
gi 24641342 820 NNLDIESIDALAEA---INEYEGGVII-VSHD 847
Cdd:cd03295 164 GALDPITRDQLQEEfkrLQQELGKTIVfVTHD 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
671-888 |
2.38e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.97 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILGVHNVTFAFPSQKPLFikvdfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEQR---KNHRLHVGRFD 743
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALD-----GVSLELRpgevHALLGENGAGKSTLMKILSGVYQPDSGEILldgEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 744 QHSG-----------EHLTAEESaaeylqrLF--NLP-----------HEKARKALGSFGLVSHAHTiKMKDLSGGQKAR 799
Cdd:COG1129 77 QAAGiaiihqelnlvPNLSVAEN-------IFlgREPrrgglidwramRRRARELLARLGLDIDPDT-PVGDLSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 800 VALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEY--EG-GVIIVSH--DE--------------RLIREtgctlYV 860
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISHrlDEvfeiadrvtvlrdgRLVGT-----GP 223
|
250 260 270
....*....|....*....|....*....|...
gi 24641342 861 IEDQTINEI----VG-EFDDYRKEVLDSLGEVV 888
Cdd:COG1129 224 VAELTEDELvrlmVGrELEDLFPKRAAAPGEVV 256
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
677-870 |
2.51e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.29 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 677 HNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKNHR--------- 736
Cdd:PRK13657 338 DDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRilidgtdirtvTRASLRrniavvfqd 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 737 -----------LHVGRFDQHSGEHLTAEESAA--EYLqrlfnlphekARKALGSFGLVSHahtiKMKDLSGGQKARVALA 803
Cdd:PRK13657 418 aglfnrsiednIRVGRPDATDEEMRAAAERAQahDFI----------ERKPDGYDTVVGE----RGRQLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 804 ELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHdeRL--IRETGCTLY-----VIEDQTINEIV 870
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMKGrtTFIIAH--RLstVRNADRILVfdngrVVESGSFDELV 557
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
369-575 |
2.83e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 64.67 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEvvATDKtaintileaDVRRTEMlkkadelekQ 448
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIA--GLERPDSGTILFGGED--ATDV---------PVQERNV---------G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGD------LTVQEelNDTFA-ELKAIGAYSAEA----RARRILAGLGFSKeMQDRPTNKFSGGWRMRVSLARALYLE 517
Cdd:cd03296 78 FVFQHyalfrhMTVFD--NVAFGlRVKPRSERPPEAeiraKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 518 PTLLMLDEPTNHLDlnAVI------WLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQ 575
Cdd:cd03296 155 PKVLLLDEPFGALD--AKVrkelrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
673-888 |
2.91e-11 |
|
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: 64.83 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPS--------QKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG--------------E 730
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgakqRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGtvsfrgqdlyqldrK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 731 QRKNHRLHVGRFDQHS----GEHLTAEESAAEYLQRLFNLpHEKARKA-----LGSFGLVSHAHTIKMKDLSGGQKARVA 801
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSpsavNPRMTVRQIIGEPLRHLTSL-DESEQKAriaelLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 802 LAELCLSAPDVLILDEPTNNLDI---ESIDALAEAINEyEGGV--IIVSHDERLIRETGCTLYVIED-QTINEI-VGEFD 874
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMvlqAVILELLRKLQQ-AFGTayLFITHDLRLVQSFCQRVAVMDKgQIVEECdVAQLL 239
|
250
....*....|....
gi 24641342 875 DYRKEVLDSLGEVV 888
Cdd:TIGR02769 240 SFKHPAGRNLQSAV 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
672-832 |
2.92e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.40 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSQkPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrLHVGRFDQHSGEHLT 751
Cdd:PRK09536 2 PMIDVSDLSVEFGDT-TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGT------VLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 752 AEESAAEYLQ--------------RLFNLPH---------------EKARKALGSFGLVSHAHTikmkDLSGGQKARVAL 802
Cdd:PRK09536 75 ASRRVASVPQdtslsfefdvrqvvEMGRTPHrsrfdtwtetdraavERAMERTGVAQFADRPVT----SLSGGERQRVLL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 24641342 803 AELCLSAPDVLILDEPTNNLDI-------ESIDALAE 832
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDInhqvrtlELVRRLVD 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
673-847 |
3.12e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.21 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFP-SQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRK--------------NHRL 737
Cdd:PRK13640 5 IVEFKHVSFTYPdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKitvdgitltaktvwDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 HVGRFDQHSGEHL---TAEESAAEYLQRLfNLPHEK----ARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAP 810
Cdd:PRK13640 85 KVGIVFQNPDNQFvgaTVGDDVAFGLENR-AVPRPEmikiVRDVLADVGMLDYIDS-EPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24641342 811 DVLILDEPTNNLDIES----IDALAEAINEYEGGVIIVSHD 847
Cdd:PRK13640 163 KIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHD 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
377-571 |
3.16e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.04 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 377 GRRYGLVGPNGHGKTT----LLRHIATRA---FAIPPnIDVLLCEQ--------EVVATD-KTAINTILEAdvrrtemlk 440
Cdd:PRK15134 312 GETLGLVGESGSGKSTtglaLLRLINSQGeiwFDGQP-LHNLNRRQllpvrhriQVVFQDpNSSLNPRLNV--------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 441 kadeleKQFVAGDLTVQEelndtfaelKAIGAYSAEARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTL 520
Cdd:PRK15134 382 ------LQIIEEGLRVHQ---------PTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 521 LMLDEPTNHLD--LNAVI--WLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:PRK15134 447 IILDEPTSSLDktVQAQIlaLLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
363-566 |
3.27e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.62 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 363 GNDLFVNA-NLLIAHGRRYGLVGPNGHGKTTLLRHIATRAFAIPPNIDVLlcEQEVVATDKTAintileadVRRTEMLKK 441
Cdd:PRK13536 52 GDKAVVNGlSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVL--GVPVPARARLA--------RARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 442 ADELEKQFvagdlTVQEELNdTFAELKAIGAYSAEARarrILAGLGFSK--EMQDRPTNKFSGGWRMRVSLARALYLEPT 519
Cdd:PRK13536 122 FDNLDLEF-----TVRENLL-VFGRYFGMSTREIEAV---IPSLLEFARleSKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24641342 520 LLMLDEPTNHLDLNA--VIW--LDNYL-QGwkKTLLIVSHDQSFLDNVCNEI 566
Cdd:PRK13536 193 LLILDEPTTGLDPHArhLIWerLRSLLaRG--KTILLTTHFMEEAERLCDRL 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
686-851 |
3.59e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 686 QKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRknHRLHVGRFDQhsgehltaEESAAEYLQRLFN 765
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC--VDVPDNQFGR--------EASLIDAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 766 LPheKARKALGSFGLVShAHTI--KMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALA----EAINEYEG 839
Cdd:COG2401 112 FK--DAVELLNAVGLSD-AVLWlrRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVArnlqKLARRAGI 188
|
170
....*....|..
gi 24641342 840 GVIIVSHDERLI 851
Cdd:COG2401 189 TLVVATHHYDVI 200
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
369-531 |
3.81e-11 |
|
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: 64.13 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATraFAIPPNIDVLLCEQEVVATDKTAINTILeadvRRTEMLkkadelEKQ 448
Cdd:cd03256 19 DVSLSINPGEFVALIGPSGAGKSTLLRCLNG--LVEPTSGSVLIDGTDINKLKGKALRQLR----RQIGMI------FQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 F-VAGDLTVQEELN----DTFAELKAI-GAYSAE--ARARRILAGLGFSkEMQDRPTNKFSGGWRMRVSLARALYLEPTL 520
Cdd:cd03256 87 FnLIERLSVLENVLsgrlGRRSTWRSLfGLFPKEekQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARALMQQPKL 165
|
170
....*....|.
gi 24641342 521 LMLDEPTNHLD 531
Cdd:cd03256 166 ILADEPVASLD 176
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
640-856 |
4.69e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.58 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 640 KQDEDEGPQELlARPKEYIvKFRfpepsqlqppilgvhNVTFAFP-SQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLK 718
Cdd:PRK11176 325 EQEKDEGKRVI-ERAKGDI-EFR---------------NVTFTYPgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIAN 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 719 LLLGELEPQEGE-----------QRKNHRLHVGRFDQH---------------SGEHLTAEESaaeylqrlfnlphEKAR 772
Cdd:PRK11176 388 LLTRFYDIDEGEilldghdlrdyTLASLRNQVALVSQNvhlfndtianniayaRTEQYSREQI-------------EEAA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 773 KALGSFGLVShahtiKMKD------------LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG 840
Cdd:PRK11176 455 RMAYAMDFIN-----KMDNgldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN 529
|
250 260
....*....|....*....|....*.
gi 24641342 841 --VIIVSH--------DERLIRETGC 856
Cdd:PRK11176 530 rtSLVIAHrlstiekaDEILVVEDGE 555
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
476-594 |
5.17e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 66.35 E-value: 5.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 476 EARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHD 555
Cdd:PRK10636 407 EQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHD 486
|
90 100 110
....*....|....*....|....*....|....*....
gi 24641342 556 QSFLDNVCNEIIHLDQKKLQYYKGNYSMFKKMYVQKRRE 594
Cdd:PRK10636 487 RHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQ 525
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
369-574 |
5.26e-11 |
|
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: 64.06 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTAINTileadVRRTEMLKKADELEKq 448
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLL--GLEKPAQGTVSFRGQDLYQLDRKQRRA-----FRRDVQLVFQDSPSA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 fVAGDLTVQEELNDTFAELKAIGAYSAEARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTN 528
Cdd:TIGR02769 101 -VNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24641342 529 HLD--LNAVI--WLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:TIGR02769 180 NLDmvLQAVIleLLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
692-823 |
5.58e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 63.41 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 692 KVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---QRKN------HRLHVGRFDQHSG--EHLTAEESAAEYL 760
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEillDGKDitnlppHKRPVNTVFQNYAlfPHLTVFENIAFGL 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 761 qRLFNLP----HEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:cd03300 98 -RLKKLPkaeiKERVAEALDLVQLEGYANR-KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
673-847 |
5.59e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPS--QKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG-----------EQRKNHRLHV 739
Cdd:PRK13650 4 IIEVKNLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGqiiidgdllteENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHSGEHL---TAEESAAEYLQRLfNLPHEKARK----ALGSFGLVShahtIKMKD---LSGGQKARVALAELCLSA 809
Cdd:PRK13650 84 GMVFQNPDNQFvgaTVEDDVAFGLENK-GIPHEEMKErvneALELVGMQD----FKEREparLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24641342 810 PDVLILDEPTNNLD----IESIDALAEAINEYEGGVIIVSHD 847
Cdd:PRK13650 159 PKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
355-535 |
5.71e-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: 62.76 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 355 ENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPnidvllcEQEVVATDKTAINTILEADVR 434
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAG---LLRP-------DSGEVRWNGTPLAEQRDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 435 RTEMLKKADELEkqfvaGDLTVQEELndTFaeLKAIGAYSA----EARARRILAGLgfskemQDRPTNKFSGGWRMRVSL 510
Cdd:TIGR01189 74 NILYLGHLPGLK-----PELSALENL--HF--WAAIHGGAQrtieDALAAVGLTGF------EDLPAAQLSAGQQRRLAL 138
|
170 180
....*....|....*....|....*
gi 24641342 511 ARALYLEPTLLMLDEPTNHLDLNAV 535
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGV 163
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
703-851 |
6.70e-11 |
|
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: 61.24 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKnhrlhvgrfdqhsgehLTAEESAAEYLQRLFNLPhekarkalgsfglvs 782
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIY----------------IDGEDILEEVLDQLLLII--------------- 53
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 783 haHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGGVIIVSHDERLI 851
Cdd:smart00382 54 --VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
365-555 |
7.15e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.30 E-value: 7.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 365 DLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTAintilEADVRRTEM--LKKA 442
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLG--GLDTPTSGDVIFNGQPMSKLSSAA-----KAELRNQKLgfIYQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 443 DELEKQFVAgdltvqeeLNDTFAELKAIGAYSAEA--RARRILAGLGFSKEMQDRPTnKFSGGWRMRVSLARALYLEPTL 520
Cdd:PRK11629 96 HHLLPDFTA--------LENVAMPLLIGKKKPAEInsRALEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24641342 521 LMLDEPTNHLDL-NAVIWLD-----NYLQGwkKTLLIVSHD 555
Cdd:PRK11629 167 VLADEPTGNLDArNADSIFQllgelNRLQG--TAFLVVTHD 205
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
678-823 |
7.73e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.00 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGEQR---------------KNHRLH 738
Cdd:PRK13649 7 NVSYTYQAGTPFEGRALFDVNLTiedgSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstsknkdiKQIRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 739 VGRFDQHSGEHLTAE---ESAAEYLQRlFNLPHEKARK-ALGSFGLVSHAHTIKMK---DLSGGQKARVALAELCLSAPD 811
Cdd:PRK13649 87 VGLVFQFPESQLFEEtvlKDVAFGPQN-FGVSQEEAEAlAREKLALVGISESLFEKnpfELSGGQMRRVAIAGILAMEPK 165
|
170
....*....|..
gi 24641342 812 VLILDEPTNNLD 823
Cdd:PRK13649 166 ILVLDEPTAGLD 177
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
684-846 |
8.64e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 8.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 684 PSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLG-------------EL-----------------EPQ--EGEQ 731
Cdd:PRK11174 360 PDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingiELreldpeswrkhlswvgqNPQlpHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 732 RKNHRLHVGRFDQHSGEHLTAEESAAEYLQRLFN-LPHEKARKALGsfglvshahtikmkdLSGGQKARVALAELCLSAP 810
Cdd:PRK11174 440 RDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQgLDTPIGDQAAG---------------LSVGQAQRLALARALLQPC 504
|
170 180 190
....*....|....*....|....*....|....*...
gi 24641342 811 DVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSH 846
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALNAASRRqtTLMVTH 542
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
687-823 |
8.80e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.47 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 687 KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRKNHRLHVG---RFDQHSGEhLTAE 753
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKitvlgvpvpaRARLARARIGvvpQFDNLDLE-FTVR 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 754 ESAAEYlQRLFNLPHEKARKALGS---FGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:PRK13536 133 ENLLVF-GRYFGMSTREIEAVIPSlleFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
366-571 |
9.63e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 366 LFvNANLLIAHGRRYGLVGPNGHGKTTLLR-------------HIATRAFAIPPNIDvllceqevvatdktaintilEAD 432
Cdd:PRK11124 18 LF-DITLDCPQGETLVLLGPSGAGKSSLLRvlnllemprsgtlNIAGNHFDFSKTPS--------------------DKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 433 VRrtEMLKKADELEKQF-VAGDLTVQEELNDtfAELKAIGAYSAEA--RARRILAGLGFSkEMQDRPTNKFSGGWRMRVS 509
Cdd:PRK11124 77 IR--ELRRNVGMVFQQYnLWPHLTVQQNLIE--APCRVLGLSKDQAlaRAEKLLERLRLK-PYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 510 LARALYLEPTLLMLDEPTNHLD---LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMEN 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
703-850 |
1.07e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.49 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEGEQRK-NHRLHvgRFDQHSGEHLTAEE--------------SAAEYLQrlfnLP 767
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLH--QMDEEARAKLRAKHvgfvfqsfmliptlNALENVE----LP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 768 -----------HEKARKALGSFGLVSHAHTIKMKdLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAI-- 834
Cdd:PRK10584 113 allrgessrqsRNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfs 191
|
170
....*....|....*...
gi 24641342 835 --NEYEGGVIIVSHDERL 850
Cdd:PRK10584 192 lnREHGTTLILVTHDLQL 209
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
671-860 |
1.21e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 62.83 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILGVHNVTFAFPSQKPLfIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNH---RLH 738
Cdd:COG4674 8 GPILYVEDLTVSFDGFKAL-NDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSvlfggtdltGLDEHeiaRLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 739 VGR-------FDQHS----------GEH-----LTAEESAAEylqrlfnlpHEKARKALGSFGLVSHAHTiKMKDLSGGQ 796
Cdd:COG4674 87 IGRkfqkptvFEELTvfenlelalkGDRgvfasLFARLTAEE---------RDRIEEVLETIGLTDKADR-LAGLLSHGQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 797 KARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHDERLIRETGCTLYV 860
Cdd:COG4674 157 KQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKhsVVVVEHDMEFVRQIARKVTV 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
672-851 |
1.22e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.13 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSQKPLfIKVDFGIDLT----SRVAIVGPNGVGKSTFLKLLlGELE-PQEGEQR-------------- 732
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQ-VEVLKGISLDiyagEMVAIVGASGSGKSTLMNIL-GCLDkPTSGTYRvagqdvatldadal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 733 -KNHRLHVGRFDQ--HSGEHLTAEE--------SAAEYLQRLfnlphEKARKALGSFGLVSHAHtIKMKDLSGGQKARVA 801
Cdd:PRK10535 81 aQLRREHFGFIFQryHLLSHLTAAQnvevpavyAGLERKQRL-----LRAQELLQRLGLEDRVE-YQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 802 LAELCLSAPDVLILDEPTNNLDIES---IDALAEAINEYEGGVIIVSHD-------ERLI 851
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHDpqvaaqaERVI 214
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
674-817 |
1.23e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 64.82 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQK--PLFIkvdFG-IDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKNH 735
Cdd:COG4615 328 LELRGVTYRYPGEDgdEGFT---LGpIDLTIRrgelVFIVGGNGSGKSTLAKLLTGLYRPESGEilldgqpvtadNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 736 RLHvgrF-----DQHSGEHL------TAEESAAEYLQRLfNLPHeKARKALGSFglvshaHTIkmkDLSGGQKARVALAE 804
Cdd:COG4615 405 RQL---FsavfsDFHLFDRLlgldgeADPARARELLERL-ELDH-KVSVEDGRF------STT---DLSQGQRKRLALLV 470
|
170
....*....|...
gi 24641342 805 LCLSAPDVLILDE 817
Cdd:COG4615 471 ALLEDRPILVFDE 483
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
667-866 |
1.36e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.86 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 667 SQLQPPILGVHNVTFAfPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNHRL 737
Cdd:PRK11831 1 EQSVANLVDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEilfdgenipAMSRSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 HVGRFDQ----HSG---EHLTAEESAAEYLQRLFNLPHEKARKA----LGSFGLVSHAHtIKMKDLSGGQKARVALAELC 806
Cdd:PRK11831 80 YTVRKRMsmlfQSGalfTDMNVFDNVAYPLREHTQLPAPLLHSTvmmkLEAVGLRGAAK-LMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 807 LSAPDVLILDEPTNNLDIESIDALAEAINEYEG--GV--IIVSHDERLIRETGCTLYVIEDQTI 866
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVtcVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
693-850 |
1.42e-10 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 63.97 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGeqrknhRLHV-GR--FDQHSGEHLTAEESAAEY-LQ--RLFnl 766
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSG------RIRLgGEvlQDSARGIFLPPHRRRIGYvFQeaRLF-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 767 PHEKARKALGsFGL---------VSHAHTIKM-----------KDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIES 826
Cdd:COG4148 90 PHLSVRGNLL-YGRkrapraerrISFDEVVELlgighlldrrpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190
....*....|....*....|....*....|....*
gi 24641342 827 -------IDALAEainEYEGGVIIVSHD----ERL 850
Cdd:COG4148 169 kaeilpyLERLRD---ELDIPILYVSHSldevARL 200
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
369-574 |
1.43e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.97 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVatdKTAINTileadvRRTEMLKKADELEKQ 448
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVA--GLEKPTEGQIFIDGEDVT---HRSIQQ------RDICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGDltvqeelNDTFAeLKAIGAYSAEaRARRI--------LAGlgfskeMQDRPTNKFSGGWRMRVSLARALYLEPTL 520
Cdd:PRK11432 93 MSLGE-------NVGYG-LKMLGVPKEE-RKQRVkealelvdLAG------FEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 521 LMLDEPTNHLDLNaviwLDNYL--------QGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:PRK11432 158 LLFDEPLSNLDAN----LRRSMrekirelqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
352-852 |
1.56e-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: 64.71 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNA----NLLIAHGRRYGLVGPNGHGKT-TllrhiatrAFAI----PPNI-----DVLLCEQEV 417
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAvkgvSFDIAAGETLALVGESGSGKSvT--------ALSIlrllPDPAahpsgSILFDGQDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 418 VATDktaintilEADVRRtemlkkadelekqfVAGD----------------LTVQEELNDTFAELKAIGAYSAEARARR 481
Cdd:COG4172 79 LGLS--------ERELRR--------------IRGNriamifqepmtslnplHTIGKQIAEVLRLHRGLSGAAARARALE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 482 ILAGLGFskemqDRPTNK-------FSGGWRMRVSLARALYLEPTLLMLDEPTNHLD--LNAVIwLDnYLQGWKKT---- 548
Cdd:COG4172 137 LLERVGI-----PDPERRldayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtVQAQI-LD-LLKDLQRElgma 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 549 LLIVSHD----QSFLDNVCneiihldqkklqyykgnysmfkkmyVqkrreMikeyekQEKRLRElkahgqskkaaekkqk 624
Cdd:COG4172 210 LLLITHDlgvvRRFADRVA-------------------------V-----M------RQGEIVE---------------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 625 esltrkqeknkskqqkqdedEGP-QELLARPK-EY-------IVKFRFPEPSQLQPPILGVHNVTFAFPSQKPLFIK--- 692
Cdd:COG4172 238 --------------------QGPtAELFAAPQhPYtrkllaaEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRRtvg 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 ----VDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGeLEPQEGE------------------QRK------------- 733
Cdd:COG4172 298 hvkaVD-GVSLTLRrgetLGLVGESGSGKSTLGLALLR-LIPSEGEirfdgqdldglsrralrpLRRrmqvvfqdpfgsl 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 734 NHRLHVGrfdQHSGEHLTA---EESAAEYLQRlfnlphekARKALGSFGLVSHA-----HtikmkDLSGGQKARVALAE- 804
Cdd:COG4172 376 SPRMTVG---QIIAEGLRVhgpGLSAAERRAR--------VAEALEEVGLDPAArhrypH-----EFSGGQRQRIAIARa 439
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 24641342 805 LCLSaPDVLILDEPTNNLDIeSIDA-----LAEAINEYEGGVIIVSHDERLIR 852
Cdd:COG4172 440 LILE-PKLLVLDEPTSALDV-SVQAqildlLRDLQREHGLAYLFISHDLAVVR 490
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
676-847 |
1.65e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.34 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKplfikvdfgidLTsrvAIVGPNGVGKSTFLKLLLGELEPQEGE------------QRKNHRlHVGRFD 743
Cdd:PRK11231 18 LNDLSLSLPTGK-----------IT---ALIGPNGCGKSTLLKCFARLLTPQSGTvflgdkpismlsSRQLAR-RLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 744 QHsgeHLTAEESAAE---------YLQ---RLFNLPHEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPD 811
Cdd:PRK11231 83 QH---HLTPEGITVRelvaygrspWLSlwgRLSAEDNARVNQAMEQTRINHLADR-RLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24641342 812 VLILDEPTNNLDI----ESIDALAEaINEYEGGVIIVSHD 847
Cdd:PRK11231 159 VVLLDEPTTYLDInhqvELMRLMRE-LNTQGKTVVTVLHD 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
670-887 |
1.75e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 670 QPPILGVHNVTFAFPSQKPLfIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHR----------LHV 739
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaaLAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHSGEHLTAEESAAEYLQrLFNLPH-----------EKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLS 808
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLY-LGQLPHkggivnrrllnYEAREQLEHLGVDIDPDT-PLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 809 APDVLILDEPTNNLDIESIDALAEAINEY--EGGVII-VSH----------------DERLIRETGCTLYVIEDQTINEI 869
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELraEGRVILyVSHrmeeifalcdaitvfkDGRYVATFDDMAQVDRDQLVQAM 237
|
250 260
....*....|....*....|..
gi 24641342 870 VG-EFDD---YRKEvldSLGEV 887
Cdd:PRK11288 238 VGrEIGDiygYRPR---PLGEV 256
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
676-847 |
1.81e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIKVDFGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGE-------QRKNH--------- 735
Cdd:PRK13651 5 VKNIVKIFNKKLPTELKALDNVSVEINqgefIAIIGQTGSGKTTFIEHLNALLLPDTGTiewifkdEKNKKktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 736 -------------------RLHVGRFDQHSGEHL---------------------TAEESAAEYLQrLFNLPHEKARKAl 775
Cdd:PRK13651 85 eklviqktrfkkikkikeiRRRVGVVFQFAEYQLfeqtiekdiifgpvsmgvskeEAKKRAAKYIE-LVGLDESYLQRS- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 776 gSFglvshahtikmkDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINE-YEGG--VIIVSHD 847
Cdd:PRK13651 163 -PF------------ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGktIILVTHD 224
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
369-567 |
2.31e-10 |
|
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: 61.64 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVaTDKTAINTILEADVRRTEMlkkadelekQ 448
Cdd:TIGR02324 26 NVSLTVNAGECVALSGPSGAGKSTLLKSLY--ANYLPDSGRILVRHEGAW-VDLAQASPREVLEVRRKTI---------G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGDLTVQEELN--DTFAE-LKAIGAYSAEA--RARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLML 523
Cdd:TIGR02324 94 YVSQFLRVIPRVSalEVVAEpLLERGVPREAAraRARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPILLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24641342 524 DEPTNHLDLN---AVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEII 567
Cdd:TIGR02324 174 DEPTASLDAAnrqVVVELIAEAKARGAALIGIFHDEEVRELVADRVM 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
352-569 |
2.57e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.00 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRAFAIPPNIDVLLCEQEVVatdktaintilea 431
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGEDIT------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 dvrrtemlkkadelekqfvagDLTVQEelndtfaelkaigaysaeaRARrilAGLGFSkeMQD-------------RPTN 498
Cdd:cd03217 68 ---------------------DLPPEE-------------------RAR---LGIFLA--FQYppeipgvknadflRYVN 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 499 K-FSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNA------VIwldNYLQGWKKTLLIVSHDQSFLDNVCNEIIHL 569
Cdd:cd03217 103 EgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAlrlvaeVI---NKLREEGKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
352-571 |
2.75e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNIDVLLCEQEV---VATDKTAINTI 428
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG---LVAPDEGVIKRNGKLrigYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 429 LEADVRRTEMLKKAdelekqfvagdltVQEElnDTFAELKaigaysaeararRILAGlgfskEMQDRPTNKFSGGWRMRV 508
Cdd:PRK09544 82 LPLTVNRFLRLRPG-------------TKKE--DILPALK------------RVQAG-----HLIDAPMQKLSGGETQRV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 509 SLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTL----LIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:PRK09544 130 LLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
361-535 |
2.90e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 361 AKGND-LFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNI-DVLLCEQEVVATDKTAINTILEadvrrtem 438
Cdd:PRK13539 11 VRGGRvLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG---LLPPAAgTIKLDGGDIDDPDVAEACHYLG-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 439 lkkadelEKQFVAGDLTVQEELndTF-AELKAIGAYSAEARARRI-LAGLGfskemqDRPTNKFSGGWRMRVSLARALYL 516
Cdd:PRK13539 80 -------HRNAMKPALTVAENL--EFwAAFLGGEELDIAAALEAVgLAPLA------HLPFGYLSAGQKRRVALARLLVS 144
|
170
....*....|....*....
gi 24641342 517 EPTLLMLDEPTNHLDLNAV 535
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAV 163
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
679-846 |
2.97e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 62.44 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 679 VTFAFPSQKPLFIKVDFGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGEQR---------------KNHRLHV 739
Cdd:PRK13643 7 VNYTYQPNSPFASRALFDIDLEvkkgSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTvgdivvsstskqkeiKPVRKKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHSGEHLTAEESAAE--YLQRLFNLPHEKARK----ALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVL 813
Cdd:PRK13643 87 GVVFQFPESQLFEETVLKDvaFGPQNFGIPKEKAEKiaaeKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 24641342 814 ILDEPTNNLDIES---IDALAEAINEYEGGVIIVSH 846
Cdd:PRK13643 167 VLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
707-823 |
3.36e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 707 GPNGVGKSTFLKLLLGELEPQEGEQR--------KNH--RLHVGRFDQhsGEHLTAEESAAEYLQ---RLFNLPHEKARK 773
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWlfgqpvdaGDIatRRRVGYMSQ--AFSLYGELTVRQNLElhaRLFHLPAAEIAA 376
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 24641342 774 ----ALGSFGLVSHAHTIKmKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:NF033858 377 rvaeMLERFDLADVADALP-DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
704-832 |
3.60e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.50 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 704 AIVGPNGVGKSTFLKLLLGELEPQEGEqRKNHRLHVGR--FDQHsgEHLTAEE------------------SAAEYLQRL 763
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLLSGE-RQSQFSHITRlsFEQL--QKLVSDEwqrnntdmlspgeddtgrTTAEIIQDE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 764 FNLPHEKARKAlGSFGlVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAE 832
Cdd:PRK10938 110 VKDPARCEQLA-QQFG-ITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAE 176
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
674-850 |
4.06e-10 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 63.58 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 674 LGVHNVTFAFPSQ-KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKNHRLHVGR 741
Cdd:TIGR02203 331 VEFRNVTFRYPGRdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQilldghdladyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQH----------------SGEHLTAE-ESAAE--YLQRLFNLPHEKARKALGSFGLVshahtikmkdLSGGQKARVAL 802
Cdd:TIGR02203 411 VSQDvvlfndtianniaygrTEQADRAEiERALAaaYAQDFVDKLPLGLDTPIGENGVL----------LSGGQRQRLAI 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24641342 803 AELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHdeRL 850
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGrtTLVIAH--RL 528
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
676-823 |
4.70e-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: 60.35 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLfIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGeqrknhRLHVGrfdqhsGEHLT---- 751
Cdd:cd03301 3 LENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG------RIYIG------GRDVTdlpp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 752 AEESAAEYLQRLFNLPHEKARKALgSFGLVSH--------------AHTIKM--------KDLSGGQKARVALAELCLSA 809
Cdd:cd03301 70 KDRDIAMVFQNYALYPHMTVYDNI-AFGLKLRkvpkdeidervrevAELLQIehlldrkpKQLSGGQRQRVALGRAIVRE 148
|
170
....*....|....
gi 24641342 810 PDVLILDEPTNNLD 823
Cdd:cd03301 149 PKVFLMDEPLSNLD 162
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
702-847 |
5.08e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.01 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 702 RVAIVGPNGVGKSTFLKLLLGeLEPQEGEQRknhrlhvgrFDQHSGEHLTAEESAA------------------EYLQrL 763
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAG-LLPGQGEIL---------LNGRPLSDWSAAELARhraylsqqqsppfampvfQYLA-L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 764 F---NLPHEKARKAL----GSFGL-------VSHahtikmkdLSGGQKARVALAELCLSA-PDV------LILDEPTNNL 822
Cdd:COG4138 93 HqpaGASSEAVEQLLaqlaEALGLedklsrpLTQ--------LSGGEWQRVRLAAVLLQVwPTInpegqlLLLDEPMNSL 164
|
170 180
....*....|....*....|....*...
gi 24641342 823 DIESIDALAEAINEY--EGGVIIVS-HD 847
Cdd:COG4138 165 DVAQQAALDRLLRELcqQGITVVMSsHD 192
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
673-848 |
5.24e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQkPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---QRKNHRLHVGRFDQH---- 745
Cdd:PRK13540 1 MLDVIELDFDYHDQ-PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEilfERQSIKKDLCTYQKQlcfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 746 ---SG--EHLTAEESAaeylqrLFNLphEKARKALGSFGLV---SHAHTIKMKD--LSGGQKARVALAELCLSAPDVLIL 815
Cdd:PRK13540 80 ghrSGinPYLTLRENC------LYDI--HFSPGAVGITELCrlfSLEHLIDYPCglLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 24641342 816 DEPTNNLDIESIDALAEAINEYE---GGVIIVSHDE 848
Cdd:PRK13540 152 DEPLVALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
676-886 |
5.61e-10 |
|
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: 62.90 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIkVDFGIDLTSRVAIVGPNGVGKSTFLKLLLG--ELEPQEGE-----------QRKNHRLHVGRF 742
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKN-ISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRiiyhvalcekcGYVERPSKVGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 743 DQHSGEHLTAEE----------------SAAEYLQRLFNL-------------------PHEKA-RKALGSFGLVSHAHT 786
Cdd:TIGR03269 82 CPVCGGTLEPEEvdfwnlsdklrrrirkRIAIMLQRTFALygddtvldnvlealeeigyEGKEAvGRAVDLIEMVQLSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 787 IK--MKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESI----DALAEAINEYEGGVIIVSH---------DERLI 851
Cdd:TIGR03269 162 IThiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHwpeviedlsDKAIW 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 24641342 852 RETGCtlyVIEDQTINEIVGEF----DDYRKEVLDSLGE 886
Cdd:TIGR03269 242 LENGE---IKEEGTPDEVVAVFmegvSEVEKECEVEVGE 277
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
703-865 |
5.61e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrLHVGrfDQHSGEHLTAEESAAEYLQRLFNLPHEKARKALgSFGL-- 780
Cdd:PRK11000 32 VVFVGPSGCGKSTLLRMIAGLEDITSGD------LFIG--EKRMNDVPPAERGVGMVFQSYALYPHLSVAENM-SFGLkl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 781 -----------VSHAHTI---------KMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIesidALAeaineyegg 840
Cdd:PRK11000 103 agakkeeinqrVNQVAEVlqlahlldrKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA----ALR--------- 169
|
170 180
....*....|....*....|....*.
gi 24641342 841 VIIVSHDERLIRETGCTL-YVIEDQT 865
Cdd:PRK11000 170 VQMRIEISRLHKRLGRTMiYVTHDQV 195
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
704-824 |
5.73e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.81 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 704 AIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLhvgRFDQHSGEHLTAEESAAEYL---QRLFnlPHEKARKAL----- 775
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV---LFDAEKGICLPPEKRRIGYVfqdARLF--PHYKVRGNLrygma 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 776 ----GSF----GLVSHAHTIKM--KDLSGGQKARVALAELCLSAPDVLILDEPTNNLDI 824
Cdd:PRK11144 103 ksmvAQFdkivALLGIEPLLDRypGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
694-887 |
6.40e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.02 E-value: 6.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 694 DFGIDLTS--RVAIVGPNGVGKSTFLKLLLGeLEPQEGEQRKNH-----RLH-----VGRFDQHSG--EHLTAEESAAEY 759
Cdd:PRK10851 20 DISLDIPSgqMVALLGPSGSGKTTLLRIIAG-LEHQTSGHIRFHgtdvsRLHardrkVGFVFQHYAlfRHMTVFDNIAFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 760 LQRL--FNLPHEKA--RKALGSFGLVSHAHTIKM--KDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEA 833
Cdd:PRK10851 99 LTVLprRERPNAAAikAKVTQLLEMVQLAHLADRypAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRW 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 834 I----NEYEGGVIIVSHDERLIRETGCTLyVIEDQTINEIVGEFDDYRKE-----VLDSLGEV 887
Cdd:PRK10851 179 LrqlhEELKFTSVFVTHDQEEAMEVADRV-VVMSQGNIEQAGTPDQVWREpatrfVLEFMGEV 240
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
676-861 |
7.30e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.43 E-value: 7.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRlhvgrfDQHSGEHLTAEES 755
Cdd:PRK10790 343 IDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR------PLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 AAEYLQ-------RLF-------NLPHEKARKALGSFGLVSHAHTikMKD------------LSGGQKARVALAELCLSA 809
Cdd:PRK10790 417 VAMVQQdpvvladTFLanvtlgrDISEEQVWQALETVQLAELARS--LPDglytplgeqgnnLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24641342 810 PDVLILDEPTNNLDIESIDALAEAIneyeggviivshdeRLIRETgCTLYVI 861
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQAL--------------AAVREH-TTLVVI 531
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
375-574 |
7.75e-10 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 61.67 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 375 AHGRRyGLVGPNGHGKTTLLRHIA--TRafaipPNIDVLLCEQEVVATDKTAIntILEADVRRTEMLKKADELEKQfvag 452
Cdd:TIGR02142 22 GQGVT-AIFGRSGSGKTTLIRLIAglTR-----PDEGEIVLNGRTLFDSRKGI--FLPPEKRRIGYVFQEARLFPH---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 453 dLTVQEELNdtFAELKAIGAYSaEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDL 532
Cdd:TIGR02142 90 -LSVRGNLR--YGMKRARPSER-RISFERVIELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24641342 533 ---NAVI-WLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:TIGR02142 165 prkYEILpYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
649-824 |
8.01e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 62.83 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 649 ELLARPKEYIVKFRFPEPSQLQPPILgVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQE 728
Cdd:TIGR01193 450 EVYLVDSEFINKKKRTELNNLNGDIV-INDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 729 GEQRKNHRLhVGRFDQH---------------------------SGEHLTAEE-----SAAEYLQRLFNLPhekarkaLG 776
Cdd:TIGR01193 529 GEILLNGFS-LKDIDRHtlrqfinylpqepyifsgsilenlllgAKENVSQDEiwaacEIAEIKDDIENMP-------LG 600
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24641342 777 -SFGLVSHAHTIkmkdlSGGQKARVALAELCLSAPDVLILDEPTNNLDI 824
Cdd:TIGR01193 601 yQTELSEEGSSI-----SGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
351-555 |
8.89e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.41 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 351 DIKIENFTIsAKGNDLFVNA-NLLIAHGRRYGLVGPNGHGKTTLLRHIATrafaippnidVLLCEQEVVATDKTAINTIl 429
Cdd:PRK11231 2 TLRTENLTV-GYGTKRILNDlSLSLPTGKITALIGPNGCGKSTLLKCFAR----------LLTPQSGTVFLGDKPISML- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 eadvrrtemlkKADELEKQ--FVAGDLTVQEELndTFAELKAIG-----------AYSAEARARRILAGLGFSkEMQDRP 496
Cdd:PRK11231 70 -----------SSRQLARRlaLLPQHHLTPEGI--TVRELVAYGrspwlslwgrlSAEDNARVNQAMEQTRIN-HLADRR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 497 TNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK---KTLLIVSHD 555
Cdd:PRK11231 136 LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtqgKTVVTVLHD 197
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
347-569 |
8.96e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.39 E-value: 8.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 347 EQAVDIKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATraFAIPPNIDVLLceqevvatDKTAIN 426
Cdd:PRK10253 3 ESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSR--LMTPAHGHVWL--------DGEHIQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 427 TILEADV-RRTEMLKkadelEKQFVAGDLTVQEelndtfaeLKAIGAY-----------SAEARARRILAGLGFSkEMQD 494
Cdd:PRK10253 73 HYASKEVaRRIGLLA-----QNATTPGDITVQE--------LVARGRYphqplftrwrkEDEEAVTKAMQATGIT-HLAD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 495 RPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYL------QGWkkTLLIVSHDqsfLDNVCNEIIH 568
Cdd:PRK10253 139 QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLselnreKGY--TLAAVLHD---LNQACRYASH 213
|
.
gi 24641342 569 L 569
Cdd:PRK10253 214 L 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-554 |
9.06e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRhIATRAFAIPPNI----DVLLCEQEVVATDKTAINt 427
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLR-VFNRLIELYPEArvsgEVYLDGQDIFKMDVIELR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 428 ileadvRRTEML-KKADELEKQFVAGDLTVQEELNDTFAELKAIgaysaEARARRILAGLGFSKEMQDR---PTNKFSGG 503
Cdd:PRK14247 82 ------RRVQMVfQIPNPIPNLSIFENVALGLKLNRLVKSKKEL-----QERVRWALEKAQLWDEVKDRldaPAGKLSGG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24641342 504 WRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK--TLLIVSH 554
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
489-852 |
1.02e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 489 SKEMQDRPtNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNA---VIWLDNYLQG-WKKTLLIVSHDQSFL----D 560
Cdd:PRK15134 147 AKRLTDYP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELQQeLNMGLLFITHNLSIVrklaD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 561 NVCneiihldqkklqyykgnySMFKKMYVQKRREmikeyekqeKRLRELKAHgqskkaaekkqkeSLTRkqeknkskqqk 640
Cdd:PRK15134 226 RVA------------------VMQNGRCVEQNRA---------ATLFSAPTH-------------PYTQ----------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 641 qdedegpQELLARPKEYIVkfrfPEPSQlQPPILGVHNVTFAFPSQKPLFIK-VDF-----GIDLTSR----VAIVGPNG 710
Cdd:PRK15134 255 -------KLLNSEPSGDPV----PLPEP-ASPLLDVEQLQVAFPIRKGILKRtVDHnvvvkNISFTLRpgetLGLVGESG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 711 VGKST----FLKLLLGELE------PQEGEQRKN-----HRLHVGRFDQHSG--EHLTAEESAAEYL---QRLFNLPHEK 770
Cdd:PRK15134 323 SGKSTtglaLLRLINSQGEiwfdgqPLHNLNRRQllpvrHRIQVVFQDPNSSlnPRLNVLQIIEEGLrvhQPTLSAAQRE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 771 AR--KALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD---IESIDALAEAINE-YEGGVIIV 844
Cdd:PRK15134 403 QQviAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLQQkHQLAYLFI 482
|
....*...
gi 24641342 845 SHDERLIR 852
Cdd:PRK15134 483 SHDLHVVR 490
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
673-845 |
1.09e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPLFiKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEpqeGEQRKNHRLHV-GRFDQHSGE--- 748
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALH-AVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSAGSHIELlGRTVQREGRlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 749 HLTAEESAAEYLQRLFNL-----------------------------PHEKAR--KALGSFGLVSHAHTiKMKDLSGGQK 797
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLvnrlsvlenvligalgstpfwrtcfswftREQKQRalQALTRVGMVHFAHQ-RVSTLSGGQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24641342 798 ARVALAELCLSAPDVLILDEPTNNLDIESIDALAEA---INEYEGGVIIVS 845
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTlrdINQNDGITVVVT 209
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
352-532 |
1.22e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 59.74 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTAIntileA 431
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT--GELTPSSGEVRLNGRPLAAWSPWEL-----A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 dvRRTEMLKKADELekQFvagDLTVQEelndtFAELKAIGAYSAEARARRI------LAGLGfskEMQDRPTNKFSGGWR 505
Cdd:COG4559 75 --RRRAVLPQHSSL--AF---PFTVEE-----VVALGRAPHGSSAAQDRQIvrealaLVGLA---HLAGRSYQTLSGGEQ 139
|
170 180 190
....*....|....*....|....*....|....
gi 24641342 506 MRVSLARAL-------YLEPTLLMLDEPTNHLDL 532
Cdd:COG4559 140 QRVQLARVLaqlwepvDGGPRWLFLDEPTSALDL 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
672-852 |
1.27e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.09 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSQ----KPLFIKVDFGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGE------------- 730
Cdd:PRK10419 2 TLLNVSGLSHHYAHGglsgKHQHQTVLNNVSLSLKsgetVALLGRSGCGKSTLARLLVGLESPSQGNvswrgeplaklnr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 731 -QRKNHRLHVGRFDQHS----GEHLTAEESAAEYLQRLFNL-PHEKARKALGSFGLVSHAHTIKMK---DLSGGQKARVA 801
Cdd:PRK10419 82 aQRKAFRRDIQMVFQDSisavNPRKTVREIIREPLRHLLSLdKAERLARASEMLRAVDLDDSVLDKrppQLSGGQLQRVC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 802 LAELCLSAPDVLILDEPTNNLDI----ESIDALAEAINEYEGGVIIVSHDERLIR 852
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVE 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
352-574 |
1.52e-09 |
|
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: 59.13 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNA----NLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVVATDKTAint 427
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTAlkdvSLSVPKGEIFGIIGRSGAGKSTLIRCI--NGLERPTSGSVLVDGTDLTLLSGKE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 428 iLEADVRRTEMLKKadelekQF-VAGDLTVQEelNDTFA-ELKAIGAYSAEARARRILAGLGFSKEMQDRPTNkFSGGWR 505
Cdd:cd03258 77 -LRKARRRIGMIFQ------HFnLLSSRTVFE--NVALPlEIAGVPKAEIEERVLELLELVGLEDKADAYPAQ-LSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 506 MRVSLARALYLEPTLLMLDEPTNHLDLNAViwlDNYLQGWKK-------TLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETT---QSILALLRDinrelglTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
693-851 |
1.69e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.73 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNH-----RLHVGR-FDQHsgeHLTAEES-- 755
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKiwfsghditRLKNRevpflRRQIGMiFQDH---HLLMDRTvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 756 ------------AAEYLQRlfnlpheKARKALGSFGLVSHAHTIKMKdLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:PRK10908 98 dnvaipliiagaSGDDIRR-------RVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190
....*....|....*....|....*....|.
gi 24641342 824 ---IESIDALAEAINEYEGGVIIVSHDERLI 851
Cdd:PRK10908 170 dalSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
371-571 |
1.71e-09 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 59.24 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 371 NLLIAHGRRYGLVGPNGHGKTTLLRHIAtraFAIPPN---IDVllcEQEVVATDKTAINTIleadvrRTEMlkkadelek 447
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLLRCIN---LLEEPDsgtITV---DGEDLTDSKKDINKL------RRKV--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 448 qfvaG----------DLTVQEelNDTFAELKA--IGAYSAEARARRILAGLGFSKEMQDRPtNKFSGGWRMRVSLARALY 515
Cdd:COG1126 80 ----GmvfqqfnlfpHLTVLE--NVTLAPIKVkkMSKAEAEERAMELLERVGLADKADAYP-AQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 516 LEPTLLMLDEPTNHLD-------LNAVIWLDNylQGWkkTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:COG1126 153 MEPKVMLFDEPTSALDpelvgevLDVMRDLAK--EGM--TMVVVTHEMGFAREVADRVVFMDG 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
703-864 |
1.74e-09 |
|
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: 57.97 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEGEQrknhrlhvgrfdqhsgehltaeesaaeylqrlfnlphekarkalgSFGLVS 782
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDND---------------------------------------------EWDGIT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 783 HAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAIN----EYEGGVIIVSHDERLIRETGCTL 858
Cdd:cd03222 63 PVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlseEGKKTALVVEHDLAVLDYLSDRI 142
|
....*.
gi 24641342 859 YVIEDQ 864
Cdd:cd03222 143 HVFEGE 148
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
695-819 |
1.83e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 58.84 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 695 FGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNHRL------HV--GR--FdqhsgEHLT 751
Cdd:COG0410 20 HGVSLEveegEIVALLGRNGAGKTTLLKAISGLLPPRSGSirfdgeditGLPPHRIarlgigYVpeGRriF-----PSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 752 AEE-------------SAAEYLQRLFNL-P--HEKaRKALGSfglvshahtikmkDLSGGQK-----ARvALaelcLSAP 810
Cdd:COG0410 95 VEEnlllgayarrdraEVRADLERVYELfPrlKER-RRQRAG-------------TLSGGEQqmlaiGR-AL----MSRP 155
|
....*....
gi 24641342 811 DVLILDEPT 819
Cdd:COG0410 156 KLLLLDEPS 164
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
672-847 |
1.93e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.28 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSQKpLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLL--LGELepqEGEQRKNHRLHVgrFDQHSGEH 749
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNEL---ESEVRVEGRVEF--FNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 750 LTAEESAAEYLQRLFNLPH-----------------------------EKARKALGSFGLVSHAHTIKMKDLSGGQKARV 800
Cdd:PRK14258 80 RVNLNRLRRQVSMVHPKPNlfpmsvydnvaygvkivgwrpkleiddivESALKDADLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24641342 801 ALAELCLSAPDVLILDEPTNNLD-IES--IDALAEAIN-EYEGGVIIVSHD 847
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDpIASmkVESLIQSLRlRSELTMVIVSHN 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
664-848 |
1.95e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.62 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 664 PEPSQLQPPILGVHNVTFAFPSQkPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----QRKNHRLH 738
Cdd:PRK11607 10 AKTRKALTPLLEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQimldgVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 739 VGR-----FDQHS-GEHLTAEESAAeylqrlFNLPHEKARKALGS------FGLVSHAHTIKMK--DLSGGQKARVALAE 804
Cdd:PRK11607 89 YQRpinmmFQSYAlFPHMTVEQNIA------FGLKQDKLPKAEIAsrvnemLGLVHMQEFAKRKphQLSGGQRQRVALAR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24641342 805 LCLSAPDVLILDEPTNNLD--------IESIDALAEAineyegGV--IIVSHDE 848
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV------GVtcVMVTHDQ 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
352-555 |
2.38e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.36 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAK-GNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafaippnidVLLCEQEVVATDKTAINTILE 430
Cdd:PRK13647 5 IEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG----------IYLPQRGRVKVMGREVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 ADVRRTEMLKKADELEKQFVAgdlTVQEELndTFAELK-AIGAYSAEARARRILAGLGFsKEMQDRPTNKFSGGWRMRVS 509
Cdd:PRK13647 75 KWVRSKVGLVFQDPDDQVFSS---TVWDDV--AFGPVNmGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24641342 510 LARALYLEPTLLMLDEPTNHLD------LNAVIW-LDNylQGwkKTLLIVSHD 555
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDprgqetLMEILDrLHN--QG--KTVIVATHD 197
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
374-567 |
2.41e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 59.75 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 374 IAHGRRYGLVGPNGHGKTTLLRHIaTRAfaIPPNI-DVLLCEQEVVATDKTAIntileADVRRtEMlkkadelekQFVAG 452
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLL-LRL--EEPTSgEILFDGQDITGLSGREL-----RPLRR-RM---------QMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 453 D--------LTVQeelnDTFAE-LKAIGAYSAEARARRILAGL---GFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTL 520
Cdd:COG4608 103 DpyaslnprMTVG----DIIAEpLRIHGLASKAERRERVAELLelvGLRPEHADRYPHEFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24641342 521 LMLDEPTNHLDLN--A-VIwldNYLQGWKK----TLLIVSHDQSFLDNVCNEII 567
Cdd:COG4608 179 IVCDEPVSALDVSiqAqVL---NLLEDLQDelglTYLFISHDLSVVRHISDRVA 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
703-847 |
2.47e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHvGRFDQHSGEHLTaeesaaEYLQRLFN--------------LPH 768
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWD-EILDEFRGSELQ------NYFTKLLEgdvkvivkpqyvdlIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 769 E---------KARKALGSFGLVSHAHTIK------MKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIE---SIDAL 830
Cdd:cd03236 102 AvkgkvgellKKKDERGKLDELVDQLELRhvldrnIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARL 181
|
170
....*....|....*..
gi 24641342 831 AEAINEYEGGVIIVSHD 847
Cdd:cd03236 182 IRELAEDDNYVLVVEHD 198
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
501-577 |
2.55e-09 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 60.92 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLD------LNAVIwldnylQGWKK---TLLIVSHDQSFLdNVCNEIIHLDQ 571
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaaLAAAI------RALKArgaTVVVITHRPSLL-AAVDKLLVLRD 541
|
....*.
gi 24641342 572 KKLQYY 577
Cdd:COG4618 542 GRVQAF 547
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
477-557 |
2.57e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.92 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 477 ARARRILAGLGFSKEMQDRPTnKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQG-WKK---TLLIV 552
Cdd:PRK11247 112 DAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlWQQhgfTVLLV 190
|
....*
gi 24641342 553 SHDQS 557
Cdd:PRK11247 191 THDVS 195
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
369-574 |
2.83e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.93 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTAIntileADVRRTEMLKKADELEKq 448
Cdd:PRK10419 30 NVSLSLKSGETVALLGRSGCGKSTLARLLV--GLESPSQGNVSWRGEPLAKLNRAQR-----KAFRRDIQMVFQDSISA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 fVAGDLTVQEELNDTFAELKAIGAYSAEARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTN 528
Cdd:PRK10419 102 -VNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24641342 529 HLDLN---AVIWLDNYLQGWKKT-LLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:PRK10419 181 NLDLVlqaGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
696-823 |
3.02e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 59.70 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----QRKNHrLHVGR------------FDqhsgeHLTAEE 754
Cdd:COG3839 21 DIDLDiedgEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEiliggRDVTD-LPPKDrniamvfqsyalYP-----HMTVYE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 755 SAAEYLqRLFNLP----HEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALA-----ElclsaPDVLILDEPTNNLD 823
Cdd:COG3839 95 NIAFPL-KLRKVPkaeiDRRVREAAELLGLEDLLDR-KPKQLSGGQRQRVALGralvrE-----PKVFLLDEPLSNLD 165
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
350-573 |
3.19e-09 |
|
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: 58.40 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 350 VDIKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRhiatrafAIPPNIDVllcEQEVVATDKTAINTIL 429
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVN-------LIPRFYDV---DSGRILIDGHDVRDYT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 EADVRRtemlkkadelEKQFVAGDLTVqeeLNDTFAELKAIGAYSAEA----RARRILAGLGFSKEMQD--------RPT 497
Cdd:cd03251 71 LASLRR----------QIGLVSQDVFL---FNDTVAENIAYGRPGATReeveEAARAANAHEFIMELPEgydtvigeRGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 498 nKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDL-------NAviwLDNYLQGwkKTLLIVSHDQSFLDNVcNEIIHLD 570
Cdd:cd03251 138 -KLSGGQRQRIAIARALLKDPPILILDEATSALDTeserlvqAA---LERLMKN--RTTFVIAHRLSTIENA-DRIVVLE 210
|
...
gi 24641342 571 QKK 573
Cdd:cd03251 211 DGK 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
696-853 |
3.58e-09 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 58.66 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLTSR----VAIVGPNGVGKSTFLKLLlGELE-PQEGEqrknhrLHVG----RFDQHSGEHLTAEESAAeyLQRL--- 763
Cdd:COG4598 26 GVSLTARkgdvISIIGSSGSGKSTFLRCI-NLLEtPDSGE------IRVGgeeiRLKPDRDGELVPADRRQ--LQRIrtr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 764 -------FNL-PH-----------------------EKARKALGSFGLVSHAHTIKmKDLSGGQKARVALAE-LCLSaPD 811
Cdd:COG4598 97 lgmvfqsFNLwSHmtvlenvieapvhvlgrpkaeaiERAEALLAKVGLADKRDAYP-AHLSGGQQQRAAIARaLAME-PE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24641342 812 VLILDEPTNNLDIE-------SIDALAEaineyEG-GVIIVSHDERLIRE 853
Cdd:COG4598 175 VMLFDEPTSALDPElvgevlkVMRDLAE-----EGrTMLVVTHEMGFARD 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
381-527 |
3.76e-09 |
|
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: 57.83 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIA--TRAFAIppniDVLLCEQEVvatDKTAINTILEADV------RRtemlkkadelekqfVAG 452
Cdd:cd03224 30 ALLGRNGAGKTTLLKTIMglLPPRSG----SIRFDGRDI---TGLPPHERARAGIgyvpegRR--------------IFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 453 DLTVQEELndtfaelkAIGAY-SAEARARRILAGLgFS-----KEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEP 526
Cdd:cd03224 89 ELTVEENL--------LLGAYaRRRAKRKARLERV-YElfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
.
gi 24641342 527 T 527
Cdd:cd03224 160 S 160
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
703-823 |
4.21e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.06 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPqeGEQRKNHRLHVGR------FDQHSG---------EHLTAEE----SAAEYLQRl 763
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMpidakeMRAISAyvqqddlfiPTLTVREhlmfQAHLRMPR- 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 764 fNLPHEKARKA----LGSFGLVSHAHTI-----KMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:TIGR00955 131 -RVTKKEKRERvdevLQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
343-556 |
4.29e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 59.58 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 343 KAALEQAVDIKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEV--VAT 420
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA--GFETPDSGRIMLDGQDIthVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 421 DKTAINTILEADVRRTEMlkkadelekqfvagdlTVQEelNDTFAeLKAIGAYSAEARaRRILAGLGFSK--EMQDRPTN 498
Cdd:PRK09452 84 ENRHVNTVFQSYALFPHM----------------TVFE--NVAFG-LRMQKTPAAEIT-PRVMEALRMVQleEFAQRKPH 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 499 KFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLI----VSHDQ 556
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGItfvfVTHDQ 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
673-854 |
4.32e-09 |
|
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: 58.91 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPLFIKVDfGIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQ---EGE--------------Q 731
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVD-GVSFDvrrgETLGLVGESGSGKSTLARAILGLLPPPgitSGEilfdgedllklsekE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 732 RKNHRlhvGR-----FdQHSGEHL----TAEESAAEYLQRLFNLP----HEKARKALGSFGLVSHAHTIKMK--DLSGGQ 796
Cdd:COG0444 80 LRKIR---GReiqmiF-QDPMTSLnpvmTVGDQIAEPLRIHGGLSkaeaRERAIELLERVGLPDPERRLDRYphELSGGM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 797 KARVALA-ELCLSaPDVLILDEPTNNLDIeSIDA-----LAEAINEYEGGVIIVSHDERLIRET 854
Cdd:COG0444 156 RQRVMIArALALE-PKLLIADEPTTALDV-TIQAqilnlLKDLQRELGLAILFITHDLGVVAEI 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
318-555 |
4.44e-09 |
|
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: 58.42 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 318 KKGGAGHSDLDNNFTMSQVQKSAGQKAALEQAvdikieNFTISAkgNDLFVnanlliahgrrygLVGPNGHGKTTLLRHI 397
Cdd:cd03294 12 KNPQKAFKLLAKGKSKEEILKKTGQTVGVNDV------SLDVRE--GEIFV-------------IMGLSGSGKSTLLRCI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 398 aTRAfaIPPNI-DVLLCEQEVVATDKTAINtileaDVRRTEMlkkADELEKQFVAGDLTVQEelNDTFA-ELKAIGAYSA 475
Cdd:cd03294 71 -NRL--IEPTSgKVLIDGQDIAAMSRKELR-----ELRRKKI---SMVFQSFALLPHRTVLE--NVAFGlEVQGVPRAER 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 476 EARARRILAGLGFsKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDlnAVIWLDNY-----LQG-WKKTL 549
Cdd:cd03294 138 EERAAEALELVGL-EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD--PLIRREMQdellrLQAeLQKTI 214
|
....*.
gi 24641342 550 LIVSHD 555
Cdd:cd03294 215 VFITHD 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
684-847 |
4.69e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 58.69 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 684 PSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---------------QRKNHRLHVGRFDQHSGE 748
Cdd:PRK13641 17 PMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTitiagyhitpetgnkNLKKLRKKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 749 HLTAEE--SAAEYLQRLFNLPHEKAR----KALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNL 822
Cdd:PRK13641 97 QLFENTvlKDVEFGPKNFGFSEDEAKekalKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180
....*....|....*....|....*...
gi 24641342 823 DIESIDALAEAINEYEGG---VIIVSHD 847
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAghtVILVTHN 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
369-554 |
4.87e-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: 57.67 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATRafaippnidvllceqevVATDKTAINTIL--EADVRRTEMLKKADELE 446
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGR-----------------VEGGGTTSGQILfnGQPRKPDQFQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 447 KQ-FVAGDLTVQEELndTFAELKAIGAYSAEARARRILAGLGFSKEMQDRPTNKF----SGGWRMRVSLARALYLEPTLL 521
Cdd:cd03234 88 QDdILLPGLTVRETL--TYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLvkgiSGGERRRVSIAVQLLWDPKVL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 24641342 522 MLDEPTNHLD----LNAVIWLDNYLQGwKKTLLIVSH 554
Cdd:cd03234 166 ILDEPTSGLDsftaLNLVSTLSQLARR-NRIVILTIH 201
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
672-847 |
5.03e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSQKPLFiKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRknhrlhvgrFDQHSGEHLT 751
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILN-NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLL---------FEGEDISTLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 752 AEEsaaeYLQR---------LF------NL----------PHEKA-RKALGSFGLVSHAHTIKMKDLSGGQKARVALAEL 805
Cdd:PRK10247 76 PEI----YRQQvsycaqtptLFgdtvydNLifpwqirnqqPDPAIfLDDLERFALPDTILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24641342 806 CLSAPDVLILDEPTNNLDIESIDALAEAINEY----EGGVIIVSHD 847
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHD 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
659-847 |
5.32e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.26 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 659 VKFRFPEPSQLQPpilgvhnVTFAFPSQKPlfikvdfgidltsrVAIVGPNGVGKSTFLKLLLGELEPQEGE-------- 730
Cdd:PRK10575 17 VSFRVPGRTLLHP-------LSLTFPAGKV--------------TGLIGHNGSGKSTLLKMLGRHQPPSEGEilldaqpl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 731 ---QRKNHRLHVGRFDQH--SGEHLTAEESAA--EY-----LQRLFNLPHEKARKALGSFGLVSHAHTIkMKDLSGGQKA 798
Cdd:PRK10575 76 eswSSKAFARKVAYLPQQlpAAEGMTVRELVAigRYpwhgaLGRFGAADREKVEEAISLVGLKPLAHRL-VDSLSGGERQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24641342 799 RVALAELCLSAPDVLILDEPTNNLDI-ESIDALA--EAINEYEG-GVIIVSHD 847
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIaHQVDVLAlvHRLSQERGlTVIAVLHD 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
377-567 |
5.63e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 377 GRRYGLVGPNGHGKTTLLRH---IATrafaiPPNIDVLLCEQEVVATDKTAintilEADVRRtemlkkadelEKQFV--- 450
Cdd:PRK11308 41 GKTLAVVGESGCGKSTLARLltmIET-----PTGGELYYQGQDLLKADPEA-----QKLLRQ----------KIQIVfqn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 451 -AGDLTVQEELNDTFAELKAIGA-YSAEARARRILAGL---GFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDE 525
Cdd:PRK11308 101 pYGSLNPRKKVGQILEEPLLINTsLSAAERREKALAMMakvGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24641342 526 PTNHLD-------LNAVIWLDnylQGWKKTLLIVSHDQSFLDNVCNEII 567
Cdd:PRK11308 181 PVSALDvsvqaqvLNLMMDLQ---QELGLSYVFISHDLSVVEHIADEVM 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
671-847 |
6.28e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 56.29 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILGVHNVTFAfpsqkplfIKVDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNhrlhvgrfdqhs 746
Cdd:cd03215 2 EPVLEVRGLSVK--------GAVR-DVSFEVRageiVGIAGLVGNGQTELAEALFGLRPPASGEITLD------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 747 GEHLTAEESAAEYLQRLFNLPHEkaRKALGSFGLVSHAHTIKMKD-LSGG--QKarVALA-ELcLSAPDVLILDEPTNNL 822
Cdd:cd03215 61 GKPVTRRSPRDAIRAGIAYVPED--RKREGLVLDLSVAENIALSSlLSGGnqQK--VVLArWL-ARDPRVLILDEPTRGV 135
|
170 180
....*....|....*....|....*...
gi 24641342 823 DIESIDALAEAINEY--EG-GVIIVSHD 847
Cdd:cd03215 136 DVGAKAEIYRLIRELadAGkAVLLISSE 163
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
369-577 |
6.52e-09 |
|
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: 57.16 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPN---IDVllceqevvatdKTAINTILEADVrrtemlkkadel 445
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAG---IYPPDsgtVTV-----------RGRVSSLLGLGG------------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 446 ekqFVAGDLTVQEelNDTF-AELKAIGAYSAEARARRIL--AGLGfskEMQDRPTNKFSGGWRMRVSLARALYLEPTLLM 522
Cdd:cd03220 94 ---GFNPELTGRE--NIYLnGRLLGLSRKEIDEKIDEIIefSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 523 LDEPTNHLDLN----AVIWLDNYLQGwKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYY 577
Cdd:cd03220 166 IDEVLAVGDAAfqekCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
352-569 |
6.54e-09 |
|
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: 57.66 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRAFAIPPNIDVLLCEQEVVAtdktaintiLEA 431
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSGTILFKGQDLLE---------LEP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEMLKKADE--LEKQFVAGDLTVQEELNdtfAELKAIG-------AYSAEARARriLAGLGFSKEMQDRPTNK-FS 501
Cdd:TIGR01978 72 DERARAGLFLAFQypEEIPGVSNLEFLRSALN---ARRSARGeepldllDFEKLLKEK--LALLDMDEEFLNRSVNEgFS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 502 GGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK---KTLLIVSHDQSFLDNVCNEIIHL 569
Cdd:TIGR01978 147 GGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLRepdRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
696-844 |
6.54e-09 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 57.15 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEQRknhrlhvgrFDqhsGEHLTAEEsaaeylqrlfnlPHEKA 771
Cdd:TIGR03410 18 GVSLEVPkgevTCVLGRNGVGKTTLLKTLMGLLPVKSGSIR---------LD---GEDITKLP------------PHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 772 RKALG-------SFGLVSHAHTIKM-------------------------------KDLSGGQKARVALAELCLSAPDVL 813
Cdd:TIGR03410 74 RAGIAyvpqgreIFPRLTVEENLLTglaalprrsrkipdeiyelfpvlkemlgrrgGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190
....*....|....*....|....*....|...
gi 24641342 814 ILDEPTNNLDIESIDALAEAINEY--EGGVIIV 844
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLraEGGMAIL 186
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
644-824 |
6.75e-09 |
|
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: 57.94 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 644 DEGPQELLARPKEYIVKFRFPEpsqlqppilGVHNVTFA-FPSQ-KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLL 721
Cdd:cd03291 14 DEGFGELLEKAKQENNDRKHSS---------DDNNLFFSnLCLVgAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 722 GELEPQEGEQRknhrlHVGRFDQHS----------GEHLTAEESAAEYL-----------QRLFNLPhEKARKALGSFGL 780
Cdd:cd03291 85 GELEPSEGKIK-----HSGRISFSSqfswimpgtiKENIIFGVSYDEYRyksvvkacqleEDITKFP-EKDNTVLGEGGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24641342 781 VshahtikmkdLSGGQKARVALAELCLSAPDVLILDEPTNNLDI 824
Cdd:cd03291 159 T----------LSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
672-823 |
8.58e-09 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 57.56 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPS---QKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVG----R--- 741
Cdd:COG4525 2 SMLTVRHVSVRYPGggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGpgadRgvv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 FDQHS-GEHLTAEESAAEYLqRLFNLP----HEKARKALGSFGLvSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILD 816
Cdd:COG4525 82 FQKDAlLPWLNVLDNVAFGL-RLRGVPkaerRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMD 159
|
....*..
gi 24641342 817 EPTNNLD 823
Cdd:COG4525 160 EPFGALD 166
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
676-823 |
8.86e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 56.96 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFiKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNHRLHVGRFDQHS 746
Cdd:cd03296 5 VRNVSKRFGDFVALD-DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTilfggedatDVPVQERNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 747 G--EHLTAEESAAEYL--QRLFNLPHE-----KARKALGSFGLVSHAHTIKmKDLSGGQKARVALAELCLSAPDVLILDE 817
Cdd:cd03296 84 AlfRHMTVFDNVAFGLrvKPRSERPPEaeiraKVHELLKLVQLDWLADRYP-AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
....*.
gi 24641342 818 PTNNLD 823
Cdd:cd03296 163 PFGALD 168
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
696-823 |
9.19e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.40 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGE---------QRKNHR--LHVGR-F-DQHSG--EHLTAEE-- 754
Cdd:COG1101 24 GLNLTIEegdfVTVIGSNGAGKSTLLNAIAGSLPPDSGSilidgkdvtKLPEYKraKYIGRvFqDPMMGtaPSMTIEEnl 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 755 SAAEYLQRLFNL-----PHEKA--RKALGSFGL-VSHAHTIKMKDLSGGQkaRVALAEL--CLSAPDVLILDEPTNNLD 823
Cdd:COG1101 104 ALAYRRGKRRGLrrgltKKRRElfRELLATLGLgLENRLDTKVGLLSGGQ--RQALSLLmaTLTKPKLLLLDEHTAALD 180
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
673-847 |
9.37e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPL--FIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG-----------EQRKNHRLHV 739
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvkidgelltaENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHSGEHL---TAEESAAEYLQRLfNLPHEKARKALGSFGLVSHAHTIKMKD---LSGGQKARVALAELCLSAPDVL 813
Cdd:PRK13642 84 GMVFQNPDNQFvgaTVEDDVAFGMENQ-GIPREEMIKRVDEALLAVNMLDFKTREparLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 24641342 814 ILDEPTNNLD----IESIDALAEAINEYEGGVIIVSHD 847
Cdd:PRK13642 163 ILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
371-597 |
9.51e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.55 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 371 NLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVVATDKTAINtileadVRRTEMLKKADELEKQFV 450
Cdd:PRK13636 26 NINIKKGEVTAILGGNGAGKSTLFQNL--NGILKPSSGRILFDGKPIDYSRKGLMK------LRESVGMVFQDPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 451 AgdlTVQEELNDTFAELKaIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHL 530
Cdd:PRK13636 98 A---SVYQDVSFGAVNLK-LPEDEVRKRVDNALKRTGIE-HLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 531 DLNAVI----WLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSMFKKmyvqkrREMIK 597
Cdd:PRK13636 173 DPMGVSeimkLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE------KEMLR 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
705-861 |
9.74e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.32 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 705 IVGPNGVGKSTFLKLLLGELEPQEGE---QRK----------NHRLHVGRFDQHSGEHL--TAEESAAEYLQRLFNLPHE 769
Cdd:PRK13638 32 LVGANGCGKSTLFMNLSGLLRPQKGAvlwQGKpldyskrgllALRQQVATVFQDPEQQIfyTDIDSDIAFSLRNLGVPEA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 770 K-ARKALGSFGLVSHAHTIK--MKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIE---SIDALAEAINEYEGGVII 843
Cdd:PRK13638 112 EiTRRVDEALTLVDAQHFRHqpIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAgrtQMIAIIRRIVAQGNHVII 191
|
170
....*....|....*...
gi 24641342 844 VSHDERLIRETGCTLYVI 861
Cdd:PRK13638 192 SSHDIDLIYEISDAVYVL 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
678-846 |
9.84e-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: 56.73 E-value: 9.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGeqrknhRLHVGRFDQHSgehltaeeSA 756
Cdd:cd03252 5 HVRFRYKPDGPVILDnISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENG------RVLVDGHDLAL--------AD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 757 AEYLQR----------LFN-------------LPHEKARKALGSFGlvSHAHTIKMKD------------LSGGQKARVA 801
Cdd:cd03252 71 PAWLRRqvgvvlqenvLFNrsirdnialadpgMSMERVIEAAKLAG--AHDFISELPEgydtivgeqgagLSGGQRQRIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24641342 802 LAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSH 846
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAH 195
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
369-531 |
1.23e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.79 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKtaintileadvrrtemlkkadelEKQ 448
Cdd:COG4525 25 DVSLTIESGEFVVALGASGCGKTTLLNLIA--GFLAPSSGEITLDGVPVTGPGA-----------------------DRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGD------LTVQEelNDTFA-ELKAIGAYSAEARARRILAGLGFsKEMQDRPTNKFSGGWRMRVSLARALYLEPTLL 521
Cdd:COG4525 80 VVFQKdallpwLNVLD--NVAFGlRLRGVPKAERRARAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170
....*....|
gi 24641342 522 MLDEPTNHLD 531
Cdd:COG4525 157 LMDEPFGALD 166
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
381-577 |
1.24e-08 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 55.63 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIATRAFAIPPNIDVLLCEQEVvatDKTAINTILeADVRRTEMLkkadelekqfvAGDLTVQEEL 460
Cdd:cd03213 39 AIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGRPL---DKRSFRKII-GYVPQDDIL-----------HPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 461 ndtfaelkaigAYSAEARarrilaGLgfskemqdrptnkfSGGWRMRVSLARALYLEPTLLMLDEPTNHLD----LNAVI 536
Cdd:cd03213 104 -----------MFAAKLR------GL--------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDsssaLQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24641342 537 WLDNYLQGwKKTLLIVSHD-QSFLDNVCNEIIHLDQKKLQYY 577
Cdd:cd03213 153 LLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRVIYF 193
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
366-538 |
1.26e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 366 LFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDktaintileaDVRRTEMLkkadel 445
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILA--GLARPDAGEVLWQGEPIRRQR----------DEYHQDLL------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 446 ekqF------VAGDLTVQEELNdtFAElkAIGAYSAEARARRILAGLGFSKEMqDRPTNKFSGGWRMRVSLARaLYL-EP 518
Cdd:PRK13538 78 ---YlghqpgIKTELTALENLR--FYQ--RLHGPGDDEALWEALAQVGLAGFE-DVPVRQLSAGQQRRVALAR-LWLtRA 148
|
170 180
....*....|....*....|
gi 24641342 519 TLLMLDEPTNHLDLNAVIWL 538
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARL 168
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
352-555 |
1.26e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 56.30 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAkgNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVvatdktainTILEA 431
Cdd:COG3840 2 LRLDDLTYRY--GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIA--GFLPPDSGRILWNGQDL---------TALPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEMLkkadelekqFvagdltvQEelNDTFAELK-----AIG-----AYSAEARAR--RILAGLGFSkEMQDRPTNK 499
Cdd:COG3840 69 AERPVSML---------F-------QE--NNLFPHLTvaqniGLGlrpglKLTAEQRAQveQALERVGLA-GLLDRLPGQ 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 500 FSGGWRMRVSLARALYLEPTLLMLDEPTNHLD--LNA--VIWLDNYLQGWKKTLLIVSHD 555
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDpaLRQemLDLVDELCRERGLTVLMVTHD 189
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
352-531 |
1.27e-08 |
|
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: 56.54 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFV-NANLLIAHGRRYGLVGPNGHGKTTLLRHIaTRAFAiPPNIDVLLCEQEVVATDKTAIntile 430
Cdd:cd03295 1 IEFENVTKRYGGGKKAVnNLNLEIAKGEFLVLIGPSGSGKTTTMKMI-NRLIE-PTSGEIFIDGEDIREQDPVEL----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 advRRtemlKKADELEKQFVAGDLTVQEELNdTFAELKAIGAYSAEARARRILAGLGF-SKEMQDRPTNKFSGGWRMRVS 509
Cdd:cd03295 74 ---RR----KIGYVIQQIGLFPHMTVEENIA-LVPKLLKWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVG 145
|
170 180
....*....|....*....|..
gi 24641342 510 LARALYLEPTLLMLDEPTNHLD 531
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALD 167
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
352-564 |
1.27e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFV-----NANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVVATDKTain 426
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsralfDIDLEVKKGSYTALIGHTGSGKSTLLQHL--NGLLQPTEGKVTVGDIVVSSTSKQ--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 427 tileadvRRTEMLKKADELEKQFVAGDLTVQEELNDTFAELKAIGAYSAEAR--ARRILAGLGFSKEMQDRPTNKFSGGW 504
Cdd:PRK13643 77 -------KEIKPVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEkiAAEKLEMVGLADEFWEKSPFELSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 505 RMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK---KTLLIVSHdqsFLDNVCN 564
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHqsgQTVVLVTH---LMDDVAD 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
705-847 |
1.30e-08 |
|
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: 56.88 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 705 IVGPNGVGKSTFLKLLLGELEPQEG---------------EQRKNHRLHVGRFDQHSG--EHLTAEESAAEYLQrLFNLP 767
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGkvlidgqdiaamsrkELRELRRKKISMVFQSFAllPHRTVLENVAFGLE-VQGVP 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 768 ----HEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD----IESIDALAEAINEYEG 839
Cdd:cd03294 134 raerEERAAEALELVGLEGWEHK-YPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQK 212
|
....*...
gi 24641342 840 GVIIVSHD 847
Cdd:cd03294 213 TIVFITHD 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
678-850 |
1.41e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 58.29 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGeqrknhRLHVGRFD-----QHSgehlta 752
Cdd:COG5265 362 NVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSG------RILIDGQDirdvtQAS------ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 753 eesaaeyLQR----------LFN----------LP-------HEKARKA-LGSF---------------GLvshahtiKm 789
Cdd:COG5265 430 -------LRAaigivpqdtvLFNdtiayniaygRPdaseeevEAAARAAqIHDFieslpdgydtrvgerGL-------K- 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 790 kdLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHdeRL 850
Cdd:COG5265 495 --LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGrtTLVIAH--RL 553
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
352-571 |
1.66e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.40 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafaippnidvllCEQEVVA------TDKTAi 425
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAG-------------LEHQTSGhirfhgTDVSR- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 426 ntiLEADVRRTEMLKKADELEKQF-----VAGDLTV---QEELNdtfaelkaigAYSAEARARRILAGLGFSkEMQDRPT 497
Cdd:PRK10851 69 ---LHARDRKVGFVFQHYALFRHMtvfdnIAFGLTVlprRERPN----------AAAIKAKVTQLLEMVQLA-HLADRYP 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 498 NKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVI----WLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQ 571
Cdd:PRK10851 135 AQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKelrrWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQ 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
371-556 |
1.75e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.39 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 371 NLLIAHGRRYGLVGPNGHGKTTLLRHIA-----TRAfaippniDVLLCEQEVvaTDktaintiLEADVRRTEMLKkadel 445
Cdd:COG3839 23 DLDIEDGEFLVLLGPSGCGKSTLLRMIAgledpTSG-------EILIGGRDV--TD-------LPPKDRNIAMVF----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 446 ekQFVAgdL----TVQEelNDTFAeLKAIGAYSAE--ARARRILAGLGFSKEMQDRPTNkFSGGWRMRVSLARALYLEPT 519
Cdd:COG3839 82 --QSYA--LyphmTVYE--NIAFP-LKLRKVPKAEidRRVREAAELLGLEDLLDRKPKQ-LSGGQRQRVALGRALVREPK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24641342 520 LLMLDEPTNHLD----LNAVIWLDNYLQGWKKTLLIVSHDQ 556
Cdd:COG3839 154 VFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQ 194
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
697-847 |
1.90e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 55.40 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 697 IDLTSRV-AIVGPNGVGKSTFLK----LLLGELEPQEGEQR------------------KNHRLHVGRFDQHSGEHLTAE 753
Cdd:COG0419 19 IDFDDGLnLIVGPNGAGKSTILEairyALYGKARSRSKLRSdlinvgseeasvelefehGGKRYRIERRQGEFAEFLEAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 754 ESA-AEYLQRLFNLPH-EKARKALGS--------FGLVSHAHTIK------------MKDLSGGQKARVALAELcLSapd 811
Cdd:COG0419 99 PSErKEALKRLLGLEIyEELKERLKEleealesaLEELAELQKLKqeilaqlsgldpIETLSGGERLRLALADL-LS--- 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 24641342 812 vLILDepTNNLDIESIDALAEAINEyeggVIIVSHD 847
Cdd:COG0419 175 -LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
676-823 |
1.98e-08 |
|
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: 58.42 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFP-SQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------------QRKNHRLH 738
Cdd:TIGR00957 639 VHNATFTWArDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHvhmkgsvayvpqqawiQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 739 VGRFDQHSGEHLTAEESAAEYLQRLFNLPhEKARKALGSFGLvshahtikmkDLSGGQKARVALAELCLSAPDVLILDEP 818
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEACALLPDLEILP-SGDRTEIGEKGV----------NLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
....*
gi 24641342 819 TNNLD 823
Cdd:TIGR00957 788 LSAVD 792
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
352-590 |
2.03e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRAfaippniDVLLCEQEVVATDKTAINtiLEA 431
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE-------DYEVTGGTVEFKGKDLLE--LSP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTEMLKKADE--LEKQFVAGDLTVQEELNDT--FAELKAIGAYSAEARARRILAGLGFSKEMQDRPTN-KFSGGWRM 506
Cdd:PRK09580 73 EDRAGEGIFMAFQypVEIPGVSNQFFLQTALNAVrsYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNvGFSGGEKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 507 RVSLARALYLEPTLLMLDEPTNHLDLNAVIWLD---NYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSM 583
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTL 232
|
....*..
gi 24641342 584 FKKMYVQ 590
Cdd:PRK09580 233 VKQLEEQ 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
688-824 |
2.14e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.38 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 688 PLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHV---------GRFDQHSGEHLTAEE---- 754
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFspqtswimpGTIKDNIIFGLSYDEyryt 519
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 755 ---SAAEYLQRLFNLPhEKARKALGSFGLVshahtikmkdLSGGQKARVALAELCLSAPDVLILDEPTNNLDI 824
Cdd:TIGR01271 520 sviKACQLEEDIALFP-EKDKTVLGEGGIT----------LSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
352-531 |
2.17e-08 |
|
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: 56.99 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNA----NLLIAHGRRYGLVGPNGHGKTTLlrhiatrAFAI-----PPNI---DVLLCEQEVVA 419
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAvdgvSFDVRRGETLGLVGESGSGKSTL-------ARAIlgllpPPGItsgEILFDGEDLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 420 TDKTAINTIleadvRRTEMlkkadelekQFVAGD--------LTVQEELNDTFAELKAIGAYSAEARARRILA--GLGFS 489
Cdd:COG0444 75 LSEKELRKI-----RGREI---------QMIFQDpmtslnpvMTVGDQIAEPLRIHGGLSKAEARERAIELLErvGLPDP 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24641342 490 KEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD 531
Cdd:COG0444 141 ERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
693-865 |
2.43e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.04 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----QRKNHRLHVGR-----FDQHS-GEHLTAEESAAeYLQ 761
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQifidgEDVTHRSIQQRdicmvFQSYAlFPHMSLGENVG-YGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 762 RLFNLPHEKARKAlgsfglVSHAhtIKMKDL-----------SGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDAL 830
Cdd:PRK11432 104 KMLGVPKEERKQR------VKEA--LELVDLagfedryvdqiSGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190
....*....|....*....|....*....|....*
gi 24641342 831 AEAINEYEGGVIIVShderliretgctLYVIEDQT 865
Cdd:PRK11432 176 REKIRELQQQFNITS------------LYVTHDQS 198
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
696-847 |
2.89e-08 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 55.55 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQ------EGEQRKN---HRLHVgrFDQHS-GEHLTAEESAAEYLQ 761
Cdd:TIGR01184 3 GVNLTIQqgefISLIGHSGCGKSTLLNLISGLAQPTsggvilEGKQITEpgpDRMVV--FQNYSlLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 762 R-LFNLPHEKARKA----LGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDI----ESIDALAE 832
Cdd:TIGR01184 81 RvLPDLSKSERRAIveehIALVGLTEAADK-RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNLQEELMQ 159
|
170
....*....|....*
gi 24641342 833 AINEYEGGVIIVSHD 847
Cdd:TIGR01184 160 IWEEHRVTVLMVTHD 174
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
671-846 |
2.98e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.34 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILGVHNVTFAFPSqkplFIKVDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKN------------ 734
Cdd:COG3845 3 PPALELRGITKRFGG----VVAND-DVSLTVRpgeiHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirsprda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 735 HRLHVGRFDQHSG--EHLTAEES---AAEYLQRLFnLPHEKARKAL----GSFGL-VS-HAhtiKMKDLSGGQKARVala 803
Cdd:COG3845 78 IALGIGMVHQHFMlvPNLTVAENivlGLEPTKGGR-LDRKAARARIrelsERYGLdVDpDA---KVEDLSVGEQQRV--- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24641342 804 EL--CLSA-PDVLILDEPTNNLDIESIDALAEAINEY--EG-GVIIVSH 846
Cdd:COG3845 151 EIlkALYRgARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITH 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
703-852 |
3.22e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.75 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEG------------------------EQRKNHRLHVGRFDQHSG--EHLTAEESA 756
Cdd:PRK10619 34 ISIIGSSGSGKSTFLRCINFLEKPSEGsivvngqtinlvrdkdgqlkvadkNQLRLLRTRLTMVFQHFNlwSHMTVLENV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 757 AEYLQRLFNLPHEKAR----KALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDA--- 829
Cdd:PRK10619 114 MEAPIQVLGLSKQEAReravKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEvlr 193
|
170 180
....*....|....*....|...
gi 24641342 830 LAEAINEYEGGVIIVSHDERLIR 852
Cdd:PRK10619 194 IMQQLAEEGKTMVVVTHEMGFAR 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
369-577 |
3.23e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.47 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNidvllcEQEVVATDKTA----INTILEAD------------ 432
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAG---ILEPT------SGRVEVNGRVSalleLGAGFHPEltgreniylngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 433 ---VRRTEMLKKADElekqfvagdltVQEelndtFAElkaIGAYsaeararrIlaglgfskemqDRPTNKFSGGWRMRVS 509
Cdd:COG1134 115 llgLSRKEIDEKFDE-----------IVE-----FAE---LGDF--------I-----------DQPVKTYSSGMRARLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 510 LARALYLEPTLLMLDEptnhldlnaviWL---DNYLQgwKK-------------TLLIVSHDQSFLDNVCNEIIHLDQKK 573
Cdd:COG1134 157 FAVATAVDPDILLVDE-----------VLavgDAAFQ--KKclarirelresgrTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
....
gi 24641342 574 LQYY 577
Cdd:COG1134 224 LVMD 227
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
567-611 |
3.59e-08 |
|
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: 51.42 E-value: 3.59e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 24641342 567 IHLDQKKLQYYKGNYSMFKKMYVQKRREMIKEYEKQEKRLRELKA 611
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEE 45
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
351-574 |
3.59e-08 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 54.92 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 351 DIKIENFTIS-AKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIaTRaFAIPPNIDVLLceqevvatDKTAINTIL 429
Cdd:cd03254 2 EIEFENVNFSyDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLL-MR-FYDPQKGQILI--------DGIDIRDIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 EADVRRtemlKKADELEKQFVAGDlTVQE--ELNDTFAELKAIGAYSAEARARRILAGL--GFSKEMQDRPTNkFSGGWR 505
Cdd:cd03254 72 RKSLRS----MIGVVLQDTFLFSG-TIMEniRLGRPNATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGN-LSQGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 506 MRVSLARALYLEPTLLMLDEPTNHLDL-------NAviwLDNYLQGwkKTLLIVSHDQSFLDNVcNEIIHLDQKKL 574
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTetekliqEA---LEKLMKG--RTSIIIAHRLSTIKNA-DKILVLDDGKI 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
352-532 |
3.67e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 55.55 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRhiatrafaippnidvLLCeQEVVATDKTAinTILEA 431
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLR---------------ALS-GELSPDSGEV--RLNGR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 DVRRTemlkKADELEK------QF--VAGDLTVQEelndtfaeLKAIGAY---SAEARARRI---------LAGLGfske 491
Cdd:PRK13548 65 PLADW----SPAELARrravlpQHssLSFPFTVEE--------VVAMGRAphgLSRAEDDALvaaalaqvdLAHLA---- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24641342 492 mqDRPTNKFSGGWRMRVSLARAL------YLEPTLLMLDEPTNHLDL 532
Cdd:PRK13548 129 --GRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDL 173
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
363-531 |
4.11e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.52 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 363 GNDLFvNANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVVATDKTAintileaDVRRtemLKKA 442
Cdd:PRK13649 20 GRALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLL--NGLHVPTQGSVRVDDTLITSTSKNK-------DIKQ---IRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 443 DELEKQFVAGDLTVQEELNDTFAELKAIGAY--SAEARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTL 520
Cdd:PRK13649 87 VGLVFQFPESQLFEETVLKDVAFGPQNFGVSqeEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKI 166
|
170
....*....|.
gi 24641342 521 LMLDEPTNHLD 531
Cdd:PRK13649 167 LVLDEPTAGLD 177
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
696-851 |
4.12e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLTSRV----AIVGPNGVGKSTFLKLLLG-------------------ELEPQEgeqrknhRLHVGRF--DQHSGEhl 750
Cdd:CHL00131 25 GLNLSINKgeihAIMGPNGSGKSTLSKVIAGhpaykilegdilfkgesilDLEPEE-------RAHLGIFlaFQYPIE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 751 TAEESAAEYLQRLFNLPHEKARK----ALGSFGLVSHA-HTIKMKD----------LSGGQKARVALAELCLSAPDVLIL 815
Cdd:CHL00131 96 IPGVSNADFLRLAYNSKRKFQGLpeldPLEFLEIINEKlKLVGMDPsflsrnvnegFSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 24641342 816 DEPTNNLDIESIDALAEAINEY---EGGVIIVSHDERLI 851
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLL 214
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
353-560 |
4.23e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 55.07 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 353 KIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATR-------------------------------- 400
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkyevtsgsilldgedilelspderaragifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 401 AF----AIP--PNIDVLlceqevvatdKTAINTILEADVRRTEMLKKADELEKQfvagdltvqeelndtfaelkaigays 474
Cdd:COG0396 82 AFqypvEIPgvSVSNFL----------RTALNARRGEELSAREFLKLLKEKMKE-------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 475 aeararrilagLGFSKEMQDRPTN-KFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD---LNAVIWLDNYLQGWKKTLL 550
Cdd:COG0396 126 -----------LGLDEDFLDRYVNeGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDidaLRIVAEGVNKLRSPDRGIL 194
|
250
....*....|
gi 24641342 551 IVSHDQSFLD 560
Cdd:COG0396 195 IITHYQRILD 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
371-531 |
4.27e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 371 NLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVVATDKtaintilEADVRRtemLKKADELEKQFV 450
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHL--NGLLQPTSGTVTIGERVITAGKK-------NKKLKP---LRKKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 451 AGDL---TVQEELndTFAELK-AIGAYSAEARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEP 526
Cdd:PRK13634 95 EHQLfeeTVEKDI--CFGPMNfGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
....*
gi 24641342 527 TNHLD 531
Cdd:PRK13634 173 TAGLD 177
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
373-538 |
4.56e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 373 LIAHGRRYGLVGPNGHGKTTLLRHIATRafaippnIDVLLCEQEVVATDKTAINTILeadvRRTEMLKKADELEKQfvag 452
Cdd:PLN03211 90 MASPGEILAVLGPSGSGKSTLLNALAGR-------IQGNNFTGTILANNRKPTKQIL----KRTGFVTQDDILYPH---- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 453 dLTVQEELndTFAEL----KAIGAYSAEARARRILAGLGFSKEMQDRPTNKF----SGGWRMRVSLARALYLEPTLLMLD 524
Cdd:PLN03211 155 -LTVRETL--VFCSLlrlpKSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILD 231
|
170
....*....|....
gi 24641342 525 EPTNHLDLNAVIWL 538
Cdd:PLN03211 232 EPTSGLDATAAYRL 245
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
670-823 |
4.64e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.11 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 670 QPPILGVHNVTFAFPSQKPLFikvdfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGE-----QRKNH----R 736
Cdd:PRK09452 11 LSPLVELRGISKSFDGKEVIS-----NLDLTINngefLTLLGPSGCGKTTVLRLIAGFETPDSGRimldgQDITHvpaeN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 737 LHVGRFDQHSG--EHLTAEESAAEYLqRLFNLPHEKARK----ALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAP 810
Cdd:PRK09452 86 RHVNTVFQSYAlfPHMTVFENVAFGL-RMQKTPAAEITPrvmeALRMVQLEEFAQR-KPHQLSGGQQQRVAIARAVVNKP 163
|
170
....*....|...
gi 24641342 811 DVLILDEPTNNLD 823
Cdd:PRK09452 164 KVLLLDESLSALD 176
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
381-527 |
4.76e-08 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 54.60 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIA--TRAFAIppniDVLLCEQEVvatDKTAINTILEADV------RRtemlkkadelekqfVAG 452
Cdd:COG0410 33 ALLGRNGAGKTTLLKAISglLPPRSG----SIRFDGEDI---TGLPPHRIARLGIgyvpegRR--------------IFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 453 DLTVQEELndtfaelkAIGAYSAEARARR------------ILaglgfsKEMQDRPTNKFSGGWRMRVSLARALYLEPTL 520
Cdd:COG0410 92 SLTVEENL--------LLGAYARRDRAEVradlervyelfpRL------KERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
....*..
gi 24641342 521 LMLDEPT 527
Cdd:COG0410 158 LLLDEPS 164
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
455-847 |
4.99e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 455 TVQEELNDTFAELKAIGAYSAEARARRILAGLGF--SKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDL 532
Cdd:PRK10261 122 TVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 533 N---AVIWLDNYLQG-WKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSMFKKMYVQKRREMIKEYekqeKRLRE 608
Cdd:PRK10261 202 TiqaQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAV----PQLGA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 609 LKAHgqskkaaekkqkeSLTRKQEKNKSKQQKQDEDEGPQELLArPKEyivkfrfpepsqlqpPILGVHNVTFAFPSQKP 688
Cdd:PRK10261 278 MKGL-------------DYPRRFPLISLEHPAKQEPPIEQDTVV-DGE---------------PILQVRNLVTRFPLRSG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 689 LFIKVDFGIDLTSRV----------AIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRlhvgRFDQHSGEHL-------- 750
Cdd:PRK10261 329 LLNRVTREVHAVEKVsfdlwpgetlSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ----RIDTLSPGKLqalrrdiq 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 751 --------------TAEESAAEYLQRLFNLPHEKARKA----LGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDV 812
Cdd:PRK10261 405 fifqdpyasldprqTVGDSIMEPLRVHGLLPGKAAAARvawlLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKV 484
|
410 420 430
....*....|....*....|....*....|....*....
gi 24641342 813 LILDEPTNNLDI----ESIDALAEAINEYEGGVIIVSHD 847
Cdd:PRK10261 485 IIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHD 523
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
350-526 |
5.33e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.16 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 350 VDIKIENFTisaKGN-DLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRafaIPPNI-DVLLCEQEVVATDKTAint 427
Cdd:PRK11831 8 VDMRGVSFT---RGNrCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQ---IAPDHgEILFDGENIPAMSRSR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 428 iLEADVRRTEMLKKADELekqFVagDLTVQEELNDTFAELKAIGAYSAEARARRILAGLGFSKEMQDRPtNKFSGGWRMR 507
Cdd:PRK11831 79 -LYTVRKRMSMLFQSGAL---FT--DMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMP-SELSGGMARR 151
|
170
....*....|....*....
gi 24641342 508 VSLARALYLEPTLLMLDEP 526
Cdd:PRK11831 152 AALARAIALEPDLIMFDEP 170
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
664-823 |
5.96e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 664 PEPSqLQP--PILGVHNVTFAFPS--QKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQegeqrknhrlhv 739
Cdd:PLN03130 604 PNPP-LEPglPAISIKNGYFSWDSkaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPR------------ 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 grfdqhSGEHLTAEESAAEYLQR------------LFNLPHEKAR--KALGSFGLVSHAHTIKMKDL----------SGG 795
Cdd:PLN03130 671 ------SDASVVIRGTVAYVPQVswifnatvrdniLFGSPFDPERyeRAIDVTALQHDLDLLPGGDLteigergvniSGG 744
|
170 180
....*....|....*....|....*...
gi 24641342 796 QKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:PLN03130 745 QKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
331-560 |
6.41e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 331 FTMSQVQKSAGQKAALEQAVDIKIENFTISAKGN--DLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRAFAIPP-- 406
Cdd:COG2401 8 FVLMRVTKVYSSVLDLSERVAIVLEAFGVELRVVerYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVag 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 407 --NIDVLLCEQEVvatdktainTILEADVRRTEMLKKADELEkqfVAGdltvqeeLNDTFAELkaigaysaeararrila 484
Cdd:COG2401 88 cvDVPDNQFGREA---------SLIDAIGRKGDFKDAVELLN---AVG-------LSDAVLWL----------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 485 glgfskemqdRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-LNAVIWLDNYLQGWKK---TLLIVSHDQSFLD 560
Cdd:COG2401 132 ----------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrQTAKRVARNLQKLARRagiTLVVATHHYDVID 201
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
374-593 |
7.04e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.09 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 374 IAHGRRYGLVGPNGHGKTTLLRhiatrafaippnidvLLCeqevvatdktainTIL-----EADV-------RRTEMLKK 441
Cdd:COG4586 45 IEPGEIVGFIGPNGAGKSTTIK---------------MLT-------------GILvptsgEVRVlgyvpfkRRKEFARR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 442 ADelekqFVAG-------DLTVQeelnDTFAELKAIgaYS-AEARARRILA------GLGfskEMQDRPTNKFSGGWRMR 507
Cdd:COG4586 97 IG-----VVFGqrsqlwwDLPAI----DSFRLLKAI--YRiPDAEYKKRLDelvellDLG---ELLDTPVRQLSLGQRMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 508 VSLARALYLEPTLLMLDEPTNHLDLNA--VIW--LDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQyYKGNYSM 583
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSkeAIRefLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII-YDGSLEE 241
|
250
....*....|
gi 24641342 584 FKKMYVQKRR 593
Cdd:COG4586 242 LKERFGPYKT 251
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
352-584 |
7.75e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.63 E-value: 7.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATRAFA-IPPNIDVLLCEQEVVATDKtaintiLE 430
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGdKSAGSHIELLGRTVQREGR------LA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 ADVRRTEmlKKADELEKQF-VAGDLTVQEELndtfaelkAIGAYSA---------------EARARRILAGLGFSKEMQD 494
Cdd:PRK09984 79 RDIRKSR--ANTGYIFQQFnLVNRLSVLENV--------LIGALGStpfwrtcfswftreqKQRALQALTRVGMVHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 495 RpTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-LNAVIWLDNYL---QGWKKTLLIVSHDQSFLDNVCNEIIHLD 570
Cdd:PRK09984 149 R-VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDpESARIVMDTLRdinQNDGITVVVTLHQVDYALRYCERIVALR 227
|
250
....*....|....
gi 24641342 571 QKKLqYYKGNYSMF 584
Cdd:PRK09984 228 QGHV-FYDGSSQQF 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-555 |
9.15e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.28 E-value: 9.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIATRAFAIPPNIDVllcEQEVVATDKtaintileaDVRRTEMLKKADELEKQ 448
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKV---DGKVLYFGK---------DIFQIDAIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGDLTVQEELNDTFA-ELKAIGAYSAEARARRI---LAGLGFSKEMQDR---PTNKFSGGWRMRVSLARALYLEPTLL 521
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIAyPLKSHGIKEKREIKKIVeecLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 24641342 522 MLDEPTNHLDLNAVIWLDNYLQGWKK--TLLIVSHD 555
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
369-556 |
9.37e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.04 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIA-----TRAfaippniDVLLCEQEVvatdktaiNTILEADvRRTEMLKKAD 443
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAglediTSG-------DLFIGEKRM--------NDVPPAE-RGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 444 ELEKQfvagdLTVQEelNDTFAeLKAIGAYSAEARAR-----RILAgLGfskEMQDRPTNKFSGGWRMRVSLARALYLEP 518
Cdd:PRK11000 85 ALYPH-----LSVAE--NMSFG-LKLAGAKKEEINQRvnqvaEVLQ-LA---HLLDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24641342 519 TLLMLDEPTNHLD----LNAVIWLDNYLQGWKKTLLIVSHDQ 556
Cdd:PRK11000 153 SVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHDQ 194
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
696-819 |
1.04e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLT----SRVAIVGPNGVGKSTFLKLLLGELEPQEGE--------QRKNHRLHVGR----FDQHSGEHLTAEESAAEY 759
Cdd:NF033858 19 DVSLDipagCMVGLIGPDGVGKSSLLSLIAGARKIQQGRvevlggdmADARHRRAVCPriayMPQGLGKNLYPTLSVFEN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 760 LQ---RLFNL-PHEKARKA---LGSFGLVSHAHTIKMKdLSGGQKARVAlaeLClSA----PDVLILDEPT 819
Cdd:NF033858 99 LDffgRLFGQdAAERRRRIdelLRATGLAPFADRPAGK-LSGGMKQKLG---LC-CAlihdPDLLILDEPT 164
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
380-584 |
1.04e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.86 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 380 YGLVGPNGHGKTTLLRH-----------IATRAFAIPPNIDVllceqevvatdKTAINTILEADVRRTEMLKKADELEKQ 448
Cdd:PRK13631 55 YFIIGNSGSGKSTLVTHfnglikskygtIQVGDIYIGDKKNN-----------HELITNPYSKKIKNFKELRRRVSMVFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGDL---TVQEELndTFAELkAIGAYSAEAR--ARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLML 523
Cdd:PRK13631 124 FPEYQLfkdTIEKDI--MFGPV-ALGVKKSEAKklAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 524 DEPTNHLDLNAV-----IWLDNYLQGwkKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSMF 584
Cdd:PRK13631 201 DEPTAGLDPKGEhemmqLILDAKANN--KTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
360-570 |
1.06e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.56 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 360 SAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafAIPPNIDVLLCEQEVVATDKTaintilEADVRRTEML 439
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVAS---LISPTSGTLLFEGEDISTLKP------EIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 440 KKADELEKQFVAGDLTVQEELNDTFAELKAIgaysaearaRRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPT 519
Cdd:PRK10247 87 AQTPTLFGDTVYDNLIFPWQIRNQQPDPAIF---------LDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 520 LLMLDEPTNHLD------LNAVIwlDNYLQGWKKTLLIVSHDQsfldnvcNEIIHLD 570
Cdd:PRK10247 158 VLLLDEITSALDesnkhnVNEII--HRYVREQNIAVLWVTHDK-------DEINHAD 205
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
337-574 |
1.10e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 55.62 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 337 QKSAGQKAALEQAVDIKIENFTI-SAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLrhiatrafaippniDVLL--- 412
Cdd:PRK11174 335 PQQGEKELASNDPVTIEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL--------------NALLgfl 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 413 -CEQEVvatdktAINTILEADVRRTEMLKKADEL--EKQFVAGdlTVQEE--LNDTFAELKAIGAYSAEARARRILAGL- 486
Cdd:PRK11174 401 pYQGSL------KINGIELRELDPESWRKHLSWVgqNPQLPHG--TLRDNvlLGNPDASDEQLQQALENAWVSEFLPLLp 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 487 -GFSKEMQDRpTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDL---NAVIW-LDNYLQGwkKTLLIVSHDQSFLDN 561
Cdd:PRK11174 473 qGLDTPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhseQLVMQaLNAASRR--QTTLMVTHQLEDLAQ 549
|
250
....*....|...
gi 24641342 562 vCNEIIHLDQKKL 574
Cdd:PRK11174 550 -WDQIWVMQDGQI 561
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
672-863 |
1.27e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.78 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSQKPlFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG--------------------EQ 731
Cdd:PRK11701 5 PLLSVRGLTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGevhyrmrdgqlrdlyalseaER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 732 RKNHRLHVGRFDQHS--------------GEHLTA---------EESAAEYLQRLfNLPHEKARKALGSFglvshahtik 788
Cdd:PRK11701 84 RRLLRTEWGFVHQHPrdglrmqvsaggniGERLMAvgarhygdiRATAGDWLERV-EIDAARIDDLPTTF---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 789 mkdlSGGQKARVALAELCLSAPDVLILDEPTNNLDIeSI-----DALAEAINEYEGGVIIVSHD---ERL---------- 850
Cdd:PRK11701 153 ----SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVqarllDLLRGLVRELGLAVVIVTHDlavARLlahrllvmkq 227
|
250
....*....|....*
gi 24641342 851 --IRETGCTLYVIED 863
Cdd:PRK11701 228 grVVESGLTDQVLDD 242
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
678-846 |
1.45e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.94 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPS-----QKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG------------EQRKNHRLHVG 740
Cdd:PRK13633 9 NVSYKYESneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkvyvdgldtsdeENLWDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 741 RFDQHSGEHLTA---EESAAEYLQRLFNLPHE------KARKALGSFGLVSHAHTIkmkdLSGGQKARVALAELCLSAPD 811
Cdd:PRK13633 89 MVFQNPDNQIVAtivEEDVAFGPENLGIPPEEirervdESLKKVGMYEYRRHAPHL----LSGGQKQRVAIAGILAMRPE 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 24641342 812 VLILDEPTNNLD----IESIDALAEAINEYEGGVIIVSH 846
Cdd:PRK13633 165 CIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
354-532 |
1.51e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.64 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 354 IENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLL----RHIAtrafaiPPNIDVLLCEQEVVATDKTAintil 429
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLkmlgRHQP------PSEGEILLDAQPLESWSSKA----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 eadvrrteMLKKADELEKQFVAGD-LTVQEelndtfaeLKAIGAY---------SAEARARR----ILAGLgfsKEMQDR 495
Cdd:PRK10575 83 --------FARKVAYLPQQLPAAEgMTVRE--------LVAIGRYpwhgalgrfGAADREKVeeaiSLVGL---KPLAHR 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 24641342 496 PTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDL 532
Cdd:PRK10575 144 LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
369-555 |
1.71e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVvatdktaintileadvrrtemlkKADELEKQ 448
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIA--GFVPYQHGSITLDGKPV-----------------------EGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGD------LTVQEelNDTFA-ELKAIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVSLARALYLEPTLL 521
Cdd:PRK11248 74 VVFQNegllpwRNVQD--NVAFGlQLAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24641342 522 MLDEPTNHLD---------LNAVIWldnylQGWKKTLLIVSHD 555
Cdd:PRK11248 151 LLDEPFGALDaftreqmqtLLLKLW-----QETGKQVLLITHD 188
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
703-823 |
1.75e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQ--EGEQRKNHRLHVGRFDQHSG---------EHLTAEESAAeyLQRLFNLP---- 767
Cdd:PLN03211 97 LAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKRTGfvtqddilyPHLTVRETLV--FCSLLRLPkslt 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 768 -HEKARKA---LGSFGLVSHAHTIK----MKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:PLN03211 175 kQEKILVAesvISELGLTKCENTIIgnsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
357-574 |
1.76e-07 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 53.26 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 357 FTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVVATDKTAINtileadvRRT 436
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI--QRFYVPENGRVLVDGHDLALADPAWLR-------RQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 437 EMLKKADELEKQFVAGDLTvqeeLNDTFAELKAIGAYSAEARARRILAGL--GFSKEMQDRPTNkFSGGWRMRVSLARAL 514
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIA----LADPGMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAG-LSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 515 YLEPTLLMLDEPTNHLDLNA--VIW--LDNYLQGwkKTLLIVSHDQSFLDNVcNEIIHLDQKKL 574
Cdd:cd03252 154 IHNPRILIFDEATSALDYESehAIMrnMHDICAG--RTVIIIAHRLSTVKNA-DRIIVMEKGRI 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
672-862 |
2.09e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.07 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSqkplFIKVDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEQR------------KNH 735
Cdd:PRK11300 4 PLLSVSGLMMRFGG----LLAVN-NVNLEVReqeiVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhieglpghQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 736 RLHVGRFDQHSG--EHLTAEE---------SAAEYLQRLFNLPH---------EKARKALGSFGLVSHAHTiKMKDLSGG 795
Cdd:PRK11300 79 RMGVVRTFQHVRlfREMTVIEnllvaqhqqLKTGLFSGLLKTPAfrraesealDRAATWLERVGLLEHANR-QAGNLAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 796 QKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAI----NEYEGGVIIVSHDERLIRETGCTLYVIE 862
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
669-823 |
2.93e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 669 LQP--PILGVHNVTFAFPSQ--KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQE---------------- 728
Cdd:PLN03232 608 LQPgaPAISIKNGYFSWDSKtsKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvirgsvayvpqv 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 729 -----GEQRKNhrLHVGRfDQHSGEHLTAEESAAeyLQRLFNLPHEKARKALGSFGLvshahtikmkDLSGGQKARVALA 803
Cdd:PLN03232 688 swifnATVREN--ILFGS-DFESERYWRAIDVTA--LQHDLDLLPGRDLTEIGERGV----------NISGGQKQRVSMA 752
|
170 180
....*....|....*....|
gi 24641342 804 ELCLSAPDVLILDEPTNNLD 823
Cdd:PLN03232 753 RAVYSNSDIYIFDDPLSALD 772
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
668-823 |
3.47e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 668 QLQPPILgVHNVTFAFPSQKplfikvdfgidLTsrvAIVGPNGVGKSTFLKLLLGELEPQEGE----------------Q 731
Cdd:PTZ00243 669 ELEPKVL-LRDVSVSVPRGK-----------LT---VVLGATGSGKSTLLQSLLSQFEISEGRvwaersiayvpqqawiM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 732 RKNHRLHVGRFDqhsgehltaEESAAEyLQRLFNLPHEKARKALGSFGLVSHahtIKMK--DLSGGQKARVALAELCLSA 809
Cdd:PTZ00243 734 NATVRGNILFFD---------EEDAAR-LADAVRVSQLEADLAQLGGGLETE---IGEKgvNLSGGQKARVSLARAVYAN 800
|
170
....*....|....
gi 24641342 810 PDVLILDEPTNNLD 823
Cdd:PTZ00243 801 RDVYLLDDPLSALD 814
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
671-850 |
3.59e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 51.64 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILgvHNVTFafpsqkplfiKVDFGidltSRVAIVGPNGVGKSTFLKLLLGELEPQEGeqrknhRLHVGRFDQhSGEHL 750
Cdd:cd03369 21 PPVL--KNVSF----------KVKAG----EKIGIVGRTGAGKSTLILALFRFLEAEEG------KIEIDGIDI-STIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 751 TAEESaaeylqRLFNLPHEKA------RKALGSFGLVSHAH---TIKMK----DLSGGQKARVALAELCLSAPDVLILDE 817
Cdd:cd03369 78 EDLRS------SLTIIPQDPTlfsgtiRSNLDPFDEYSDEEiygALRVSegglNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190
....*....|....*....|....*....|...
gi 24641342 818 PTNNLDIESIDALAEAINEYEGGVIIVSHDERL 850
Cdd:cd03369 152 ATASIDYATDALIQKTIREEFTNSTILTIAHRL 184
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
499-554 |
3.76e-07 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 54.02 E-value: 3.76e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 499 KFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-------LNAviwLDNYLQGwkKTLLIVSH 554
Cdd:COG1132 476 NLSGGQRQRIAIARALLKDPPILILDEATSALDtetealiQEA---LERLMKG--RTTIVIAH 533
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
673-846 |
4.03e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 52.93 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPLFIKVDFGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGEqrknhrLHVGrfDQHSGE 748
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEknkiYFIIGNSGSGKSTLVTHFNGLIKSKYGT------IQVG--DIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 749 HLTAEESAAEYLQR--------------LFNLP---------------------------HEKARKALGSFGLVSHAHTI 787
Cdd:PRK13631 93 KKNNHELITNPYSKkiknfkelrrrvsmVFQFPeyqlfkdtiekdimfgpvalgvkkseaKKLAKFYLNKMGLDDSYLER 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 788 KMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG---VIIVSH 846
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnktVFVITH 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
672-846 |
5.10e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.86 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAF-PSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE----------QRKNHRLHVG 740
Cdd:TIGR01257 927 PGVCVKNLVKIFePSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTvlvggkdietNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 741 RFDQHS--GEHLTAEESAAEYLQ---RLFNLPHEKARKALGSFGLvSHAHTIKMKDLSGGQKARVALAELCLSAPDVLIL 815
Cdd:TIGR01257 1007 MCPQHNilFHHLTVAEHILFYAQlkgRSWEEAQLEMEAMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVL 1085
|
170 180 190
....*....|....*....|....*....|...
gi 24641342 816 DEPTNNLDIESIDALAEAINEYEGG--VIIVSH 846
Cdd:TIGR01257 1086 DEPTSGVDPYSRRSIWDLLLKYRSGrtIIMSTH 1118
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
369-555 |
5.38e-07 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 51.70 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVAT--DKTAI--------------NTILEAD 432
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLIS--GLAQPTSGGVILEGKQITEPgpDRMVVfqnysllpwltvreNIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 433 vrrtEMLKKADELEKQFVagdltVQEELNdtfaelkaigaysaeararriLAGLGfskEMQDRPTNKFSGGWRMRVSLAR 512
Cdd:TIGR01184 81 ----RVLPDLSKSERRAI-----VEEHIA---------------------LVGLT---EAADKRPGQLSGGMKQRVAIAR 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24641342 513 ALYLEPTLLMLDEPTNHLD-LNAVIWLDNYLQGWKK---TLLIVSHD 555
Cdd:TIGR01184 128 ALSIRPKVLLLDEPFGALDaLTRGNLQEELMQIWEEhrvTVLMVTHD 174
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
371-575 |
5.59e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 53.57 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 371 NLLIAHGRRYGLVGPNGHGKTT---LLRHiatraFAIPPNIDVLLCEQEVVATDKTAINTileaDVRrtemlkkADELEK 447
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTvaaLLQN-----LYQPTGGQVLLDGVPLVQYDHHYLHR----QVA-------LVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 448 QFVAGDLTVQEELNDTFAELKAIGAYSAEARARRILAGL--GFSKEMqDRPTNKFSGGWRMRVSLARALYLEPTLLMLDE 525
Cdd:TIGR00958 565 VLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEV-GEKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24641342 526 PTNHLDLNAviwlDNYLQGWKK----TLLIVSHDQSFLDNvCNEIIHLDQKKLQ 575
Cdd:TIGR00958 644 ATSALDAEC----EQLLQESRSrasrTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
703-854 |
5.67e-07 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 51.39 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNH------------RLHVGRFDQHSG--EHLTAEE---SAAEYLQRLFN 765
Cdd:cd03218 29 VGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkraRLGIGYLPQEASifRKLTVEEnilAVLEIRGLSKK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 766 LPHEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD---IESIDALAEAINEYEGGVI 842
Cdd:cd03218 109 EREEKLEELLEEFHITHLRKS-KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKILKDRGIGVL 187
|
170
....*....|..
gi 24641342 843 IVSHDerlIRET 854
Cdd:cd03218 188 ITDHN---VRET 196
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
363-574 |
6.38e-07 |
|
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: 53.20 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 363 GNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLceqevvatdktaiNTILEADVRRTEMLKKA 442
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLV--GFFQARSGEILL-------------NGFSLKDIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 443 DELEKQFVAGDLTVQEEL----NDTFAELKAIGAYS-AEARARRILAGLGFSKEMQDRPTNkFSGGWRMRVSLARALYLE 517
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLllgaKENVSQDEIWAACEiAEIKDDIENMPLGYQTELSEEGSS-ISGGQKQRIALARALLTD 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 518 PTLLMLDEPTNHLD-LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVcNEIIHLDQKKL 574
Cdd:TIGR01193 630 SKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKI 686
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
357-570 |
6.63e-07 |
|
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: 51.64 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 357 FTISAKGNDlfvnanllIAHGRRYGLVGPNGHGKTTLLRHIATRafaIPPnidvllceqevvatdktainTILEADVRRT 436
Cdd:cd03237 13 FTLEVEGGS--------ISESEVIGILGPNGIGKTTFIKMLAGV---LKP--------------------DEGDIEIELD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 437 EMLKKADELEKQFvagDLTVQEELNDTFAELKAIGAYSAEararrILAGLGFSKEMqDRPTNKFSGGWRMRVSLARALYL 516
Cdd:cd03237 62 TVSYKPQYIKADY---EGTVRDLLSSITKDFYTHPYFKTE-----IAKPLQIEQIL-DREVPELSGGELQRVAIAACLSK 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 517 EPTLLMLDEPTNHLD----LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLD 570
Cdd:cd03237 133 DADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
470-556 |
7.56e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 470 IGAYSAEARARRILAG-----LGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-LNAVI---WLDN 540
Cdd:PRK10938 367 IGIYQAVSDRQQKLAQqwldiLGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDpLNRQLvrrFVDV 446
|
90
....*....|....*.
gi 24641342 541 YLQGWKKTLLIVSHDQ 556
Cdd:PRK10938 447 LISEGETQLLFVSHHA 462
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
352-570 |
9.04e-07 |
|
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: 50.55 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTIS-----AKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIA------TRAFAIPPNIdvLLCEQE---V 417
Cdd:cd03250 1 ISVEDASFTwdsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgeleklSGSVSVPGSI--AYVSQEpwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 418 VATDKtaiNTIL---EADVRRTEMLKKADELE---KQFVAGDLTVqeelndtfaelkaIGaysaeararrilaglgfske 491
Cdd:cd03250 79 NGTIR---ENILfgkPFDEERYEKVIKACALEpdlEILPDGDLTE-------------IG-------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 492 mqDRPTNkFSGGWRMRVSLARALYLEPTLLMLDEPtnhldLNAV-------IWlDNYLQG-WK--KTLLIVSHDQSFLDN 561
Cdd:cd03250 123 --EKGIN-LSGGQKQRISLARAVYSDADIYLLDDP-----LSAVdahvgrhIF-ENCILGlLLnnKTRILVTHQLQLLPH 193
|
....*....
gi 24641342 562 vCNEIIHLD 570
Cdd:cd03250 194 -ADQIVVLD 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
381-567 |
9.34e-07 |
|
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: 52.48 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIATRafaIPPNidvllcEQEVVATDKTA-----INTILEADVRrtEMLKKAdelekqfvagdlt 455
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGV---LKPD------EGEVDEDLKISykpqyISPDYDGTVE--EFLRSA------------- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 456 VQEELNDTFaelkaigaYSAEararrILAGLGFSKEMqDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD---- 531
Cdd:COG1245 426 NTDDFGSSY--------YKTE-----IIKPLGLEKLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqr 491
|
170 180 190
....*....|....*....|....*....|....*.
gi 24641342 532 LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEII 567
Cdd:COG1245 492 LAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
487-574 |
1.02e-06 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 50.55 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 487 GFSKEMQDRPT-------NKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGW--KKTLLIVSHDQS 557
Cdd:cd03248 131 SFISELASGYDtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLS 210
|
90
....*....|....*..
gi 24641342 558 FLDNVcNEIIHLDQKKL 574
Cdd:cd03248 211 TVERA-DQILVLDGGRI 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
355-574 |
1.22e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 50.66 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 355 ENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIATrafaippnidvllceqeVVATDKTAInTILEADVR 434
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG-----------------IVPRDAGNI-IIDDEDIS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 435 RTEMLKKADE-----LEKQFVAGDLTVQEELNDTFAELKAIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVS 509
Cdd:PRK10895 69 LLPLHARARRgigylPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 510 LARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKT---LLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:PRK10895 148 IARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSglgVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
705-892 |
1.24e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.96 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 705 IVGPNGVGKSTFLKLLLGELEPQEG---------------EQRKNHRLHVGRFDQHSG--EHLTAEESAAeYLQRLFNLP 767
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPTRGqvlidgvdiakisdaELREVRRKKIAMVFQSFAlmPHMTVLDNTA-FGMELAGIN 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 768 ----HEKARKALGSFGLVSHAHTIKmKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD----IESIDALAEAINEYEG 839
Cdd:PRK10070 138 aeerREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQR 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24641342 840 GVIIVSHDERLIRETGCTLYVIEDQTINEiVGEFDdyrkevldslgEVVNNPS 892
Cdd:PRK10070 217 TIVFISHDLDEAMRIGDRIAIMQNGEVVQ-VGTPD-----------EILNNPA 257
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
381-555 |
1.32e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.69 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIATRafaIPPNI-DVLLCEQEVVATDktaINTILEADVR---RTEM----LKKADELEKQFVAG 452
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSAR---LAPDAgEVHYRMRDGQLRD---LYALSEAERRrllRTEWgfvhQHPRDGLRMQVSAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 453 DlTVQEELNDT----FAELKAIGAY---SAEARARRIlaglgfskemQDRPTNkFSGGWRMRVSLARALYLEPTLLMLDE 525
Cdd:PRK11701 110 G-NIGERLMAVgarhYGDIRATAGDwleRVEIDAARI----------DDLPTT-FSGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180 190
....*....|....*....|....*....|....
gi 24641342 526 PTNHLDLNAVIWLDNYLQGWKKTL----LIVSHD 555
Cdd:PRK11701 178 PTGGLDVSVQARLLDLLRGLVRELglavVIVTHD 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
476-555 |
1.41e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.03 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 476 EARARRILAGLGFSKEMQDRPtNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNA---VIWLDNYLQGWKKTLLIV 552
Cdd:PRK10535 122 LLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIV 200
|
...
gi 24641342 553 SHD 555
Cdd:PRK10535 201 THD 203
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
673-824 |
1.47e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.56 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPLFIK--------VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQR-KNHRLHVGRFD 743
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRRqtveavkpLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 744 QHSGEHLTAEESAAEYL---QR---LFNLP-----------HEKA-RKALGSFGLVSHAHTIKMKDLSGGQKARVALAEL 805
Cdd:PRK15112 84 YRSQRIRMIFQDPSTSLnprQRisqILDFPlrlntdlepeqREKQiIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARA 163
|
170
....*....|....*....
gi 24641342 806 CLSAPDVLILDEPTNNLDI 824
Cdd:PRK15112 164 LILRPKVIIADEALASLDM 182
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
369-574 |
1.69e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.55 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVvaTDKTAINTILEadVRRT--------EMLK 440
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNI--NALLKPTTGTVTVDDITI--THKTKDKYIRP--VRKRigmvfqfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 441 KADELEKQFVAGDLTVQEELNDtfaelkaigaysAEARARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTL 520
Cdd:PRK13646 99 FEDTVEREIIFGPKNFKMNLDE------------VKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 521 LMLDEPTNHLDLNA---VIWLDNYLQ-GWKKTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:PRK13646 167 IVLDEPTAGLDPQSkrqVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
665-846 |
1.69e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.42 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 665 EPSQLQPPILGVHNVTFAFPSQKPLFikvdfGIDLT---SRV-AIVGPNGVGKSTFLKLL--LGELEPQ---EGE----- 730
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALK-----DINLDipeNKVtALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEilldg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 731 ---------------------QRKN-------------HRLHvGRFDQHSGEHLtAEESaaeyLQRLfNLPHE-KARkaL 775
Cdd:COG1117 78 ediydpdvdvvelrrrvgmvfQKPNpfpksiydnvaygLRLH-GIKSKSELDEI-VEES----LRKA-ALWDEvKDR--L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 776 GSFGLvshahtikmkDLSGGQKARvalaeLCLsA------PDVLILDEPTNNLD------IES-IDALAEainEYegGVI 842
Cdd:COG1117 149 KKSAL----------GLSGGQQQR-----LCI-AralavePEVLLMDEPTSALDpistakIEElILELKK---DY--TIV 207
|
....
gi 24641342 843 IVSH 846
Cdd:COG1117 208 IVTH 211
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
692-853 |
1.70e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.24 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 692 KVDFGIDLTSRVAIVGPNGVGKSTFLKLLL---GELEPQEGEQRKNHRLHVgRFDQhsgehltaeesaaeyLQRLFNLph 768
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGLyasGKARLISFLPKFSRNKLI-FIDQ---------------LQFLIDV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 769 ekarkALGSFGLVShahtiKMKDLSGGQKARVALA-ELCLSAPDVL-ILDEPTNNLDIESIDALAEAINEY--EGG-VII 843
Cdd:cd03238 75 -----GLGYLTLGQ-----KLSTLSGGELQRVKLAsELFSEPPGTLfILDEPSTGLHQQDINQLLEVIKGLidLGNtVIL 144
|
170
....*....|
gi 24641342 844 VSHDERLIRE 853
Cdd:cd03238 145 IEHNLDVLSS 154
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
352-604 |
1.74e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFT-ISAKGNDL----FVNANLLIAHGRRYGLVGPNGHGKTTLLRHI-----ATRAFAIPPNIDVllceqevvaTD 421
Cdd:PRK13637 3 IKIENLThIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLngllkPTSGKIIIDGVDI---------TD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 422 KtaintileaDVRRTEMLKKA-------------DELEKQFVAGDLTV---QEELNDtfaelkaigaysaeaRARRILAG 485
Cdd:PRK13637 74 K---------KVKLSDIRKKVglvfqypeyqlfeETIEKDIAFGPINLglsEEEIEN---------------RVKRAMNI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 486 LGFSKE-MQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-------LNAVIWL-DNYlqgwKKTLLIVSHDQ 556
Cdd:PRK13637 130 VGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKELhKEY----NMTIILVSHSM 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 24641342 557 SFLDNVCNEIIHLDQKKLQyykgnysmfkkmYVQKRREMIKEYEKQEK 604
Cdd:PRK13637 206 EDVAKLADRIIVMNKGKCE------------LQGTPREVFKEVETLES 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
352-531 |
1.83e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 50.57 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGN-DLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVVatdKTAINtile 430
Cdd:PRK13652 4 IETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHF--NGILKPTSGSVLIRGEPIT---KENIR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 431 aDVRRTEMLKKADELEKQFVAgdlTVQEELndTFAELK-AIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVS 509
Cdd:PRK13652 75 -EVRKFVGLVFQNPDDQIFSP---TVEQDI--AFGPINlGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVA 147
|
170 180
....*....|....*....|..
gi 24641342 510 LARALYLEPTLLMLDEPTNHLD 531
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLD 169
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
675-847 |
1.93e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 675 GVHNVTFAFPSQKPLfikvdfgidltsrvAIVGPNGVGKSTFLKLLLGEL-----------------EPQEG-------- 729
Cdd:PRK10762 267 GVNDVSFTLRKGEIL--------------GVSGLMGAGRTELMKVLYGALprtsgyvtldghevvtrSPQDGlangivyi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 730 -EQRKNHRLHVGrfdqhsgehLTAEE----SAAEYLQRL-FNLPHEKARKALGSFGLVSHAHTIKM----KDLSGGQKAR 799
Cdd:PRK10762 333 sEDRKRDGLVLG---------MSVKEnmslTALRYFSRAgGSLKHADEQQAVSDFIRLFNIKTPSMeqaiGLLSGGNQQK 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24641342 800 VALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEY--EG-GVIIVSHD 847
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkaEGlSIILVSSE 454
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
678-864 |
1.98e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLTS--RVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNH------------RLHVGRFD 743
Cdd:PTZ00265 387 NVRFHYDTRKDVEIYKDLNFTLTEgkTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdinlkwwRSKIGVVS 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 744 Q--------------HSGEHLTAEESAAEYL-------QRLFNLPHEKARKALGSFGLVSHA-------------HTIKM 789
Cdd:PTZ00265 467 QdpllfsnsiknnikYSLYSLKDLEALSNYYnedgndsQENKNKRNSCRAKCAGDLNDMSNTtdsneliemrknyQTIKD 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 790 KD-------------------------------LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYE 838
Cdd:PTZ00265 547 SEvvdvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
|
250 260 270
....*....|....*....|....*....|
gi 24641342 839 GG----VIIVSHDERLIRETGcTLYVIEDQ 864
Cdd:PTZ00265 627 GNenriTIIIAHRLSTIRYAN-TIFVLSNR 655
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
340-574 |
2.07e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 51.36 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 340 AGQKAALEQAVDIKIEN--FTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIaTRAFAippnidvllCEQEV 417
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNvsFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL-TRAWD---------PQQGE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 418 VATDKTAINTILEADVRRTemlkkadelekqfvagdLTVQEE----LNDTFAELKAIGAYSA-EARARRILAGLGFSKEM 492
Cdd:PRK11160 397 ILLNGQPIADYSEAALRQA-----------------ISVVSQrvhlFSATLRDNLLLAAPNAsDEALIEVLQQVGLEKLL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 493 QD------------RPtnkFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-------LNAviwLDNYLQGwkKTLLIVS 553
Cdd:PRK11160 460 EDdkglnawlgeggRQ---LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDaeterqiLEL---LAEHAQN--KTVLMIT 531
|
250 260
....*....|....*....|.
gi 24641342 554 HDQSFLDNVcNEIIHLDQKKL 574
Cdd:PRK11160 532 HRLTGLEQF-DRICVMDNGQI 551
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
381-526 |
2.41e-06 |
|
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: 49.46 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIATrafaippnidvllceqeVVATDKTAInTILEADVRRTEMLKKAdEL------EKQFVAGDL 454
Cdd:cd03218 30 GLLGPNGAGKTTTFYMIVG-----------------LVKPDSGKI-LLDGQDITKLPMHKRA-RLgigylpQEASIFRKL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 455 TVQEELndtFAELKAIGAYSAEARARR--ILAGLGFSKeMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEP 526
Cdd:cd03218 91 TVEENI---LAVLEIRGLSKKEREEKLeeLLEEFHITH-LRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
678-817 |
2.79e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEG-----------EQRKNHRLH-------V 739
Cdd:PRK10522 327 NVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGeilldgkpvtaEQPEDYRKLfsavftdF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHSGEHLTAEESAA--EYLQRLfNLPHEkarkalgsfglVSHA-HTIKMKDLSGGQKARVALAELCLSAPDVLILD 816
Cdd:PRK10522 407 HLFDQLLGPEGKPANPALveKWLERL-KMAHK-----------LELEdGRISNLKLSKGQKKRLALLLALAEERDILLLD 474
|
.
gi 24641342 817 E 817
Cdd:PRK10522 475 E 475
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
465-575 |
3.47e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.01 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 465 AELKAIGAYSAEARARRILAGLGFSKEMQDRPTnKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYL-- 542
Cdd:PRK10584 113 ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfs 191
|
90 100 110
....*....|....*....|....*....|....*
gi 24641342 543 --QGWKKTLLIVSHDQSfLDNVCNEIIHLDQKKLQ 575
Cdd:PRK10584 192 lnREHGTTLILVTHDLQ-LAARCDRRLRLVNGQLQ 225
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
678-852 |
3.64e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.90 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLlGELEPQEGEQRKNHR------------LHVGRF-DQ 744
Cdd:TIGR00954 456 NIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRLTKPAkgklfyvpqrpyMTLGTLrDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 745 -----HSGEHLTAEESAAEYLQRLFNLPHEKARKALGSFGLVSHAhtikMKDLSGGQKARVALAELCLSAPDVLILDEPT 819
Cdd:TIGR00954 535 iiypdSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDW----MDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|...
gi 24641342 820 NNLDIESIDALAEAINEYEGGVIIVSHDERLIR 852
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCREFGITLFSVSHRKSLWK 643
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
693-846 |
3.70e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.46 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLK-----LLLGELEPQEGEQR---KN----------HRLHVGRFDQHSGE--HLTA 752
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRlfgRNiyspdvdpieVRREVGMVFQYPNPfpHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 753 EESAAEYLqRLFNLPH------EKARKALGSFGLVSHAHTiKMKD----LSGGQKARVALAELCLSAPDVLILDEPTNNL 822
Cdd:PRK14267 103 YDNVAIGV-KLNGLVKskkeldERVEWALKKAALWDEVKD-RLNDypsnLSGGQRQRLVIARALAMKPKILLMDEPTANI 180
|
170 180
....*....|....*....|....*.
gi 24641342 823 DIESIDALAEAINEY--EGGVIIVSH 846
Cdd:PRK14267 181 DPVGTAKIEELLFELkkEYTIVLVTH 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
672-865 |
3.91e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSQKPLfIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE--------QRKNHRLH----V 739
Cdd:PRK09700 4 PYISMAGIGKSFGPVHAL-KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTitinninyNKLDHKLAaqlgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHSG--EHLTAEESAaeYLQRL------------FNLPHEKARKALGSFGLVSHAHTiKMKDLSGGQKARVALAEL 805
Cdd:PRK09700 83 GIIYQELSviDELTVLENL--YIGRHltkkvcgvniidWREMRVRAAMMLLRVGLKVDLDE-KVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 806 CLSAPDVLILDEPTNNLDIESIDALAEAINEYEG---GVIIVSHDERLIRETGCTLYVIEDQT 865
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKDGS 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
377-560 |
4.11e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.29 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 377 GRRYGLVGPNGHGKTTLLRHIATR------AFAIPPNIDVLLCE------QEVVATdktaintILEADVRRTEMLKKADE 444
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKlkpnlgKFDDPPDWDEILDEfrgselQNYFTK-------LLEGDVKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 445 LEKQF--VAGDLTVQEELNDTFAELkaigaysaeararriLAGLGFSKEMqDRPTNKFSGGWRMRVSLARALYLEPTLLM 522
Cdd:cd03236 99 IPKAVkgKVGELLKKKDERGKLDEL---------------VDQLELRHVL-DRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24641342 523 LDEPTNHLD----LNAVIWLDNYLQGwKKTLLIVSHDQSFLD 560
Cdd:cd03236 163 FDEPSSYLDikqrLNAARLIRELAED-DNYVLVVEHDLAVLD 203
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
672-847 |
4.26e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 49.32 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGRFDQHSGEHLT 751
Cdd:PRK14271 20 PAMAAVNLTLGF-AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 752 AEESAAEYLQRLFNLPHEKARKALG-----------SFGLVSHAHTIKM------KD--------LSGGQKARVALAELC 806
Cdd:PRK14271 99 FRRRVGMLFQRPNPFPMSIMDNVLAgvrahklvprkEFRGVAQARLTEVglwdavKDrlsdspfrLSGGQQQLLCLARTL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24641342 807 LSAPDVLILDEPTNNLDIESIDALAEAINEYEG--GVIIVSHD 847
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
369-555 |
4.32e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 50.03 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLceqevvatDKTAINTILEADVRRTEMLKKADELEKQ 448
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLI--------DGVDIAKISDAELREVRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGDLTVQEelNDTFA-ELKAIGAYSAEARARRILAGLGFSKEMQDRPtNKFSGGWRMRVSLARALYLEPTLLMLDEPT 527
Cdd:PRK10070 116 ALMPHMTVLD--NTAFGmELAGINAEERREKALDALRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190
....*....|....*....|....*....|..
gi 24641342 528 NHLDLNAVIWLDNYL----QGWKKTLLIVSHD 555
Cdd:PRK10070 193 SALDPLIRTEMQDELvklqAKHQRTIVFISHD 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
478-580 |
4.38e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.70 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 478 RARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK----TLLIVS 553
Cdd:PRK15079 140 RVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemglSLIFIA 219
|
90 100
....*....|....*....|....*..
gi 24641342 554 HDQSFLDnvcneiiHLDQKKLQYYKGN 580
Cdd:PRK15079 220 HDLAVVK-------HISDRVLVMYLGH 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
377-566 |
4.68e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 50.78 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 377 GRRYGLVGPNGHGKTTLLRHIATrafaippniDVLLCEQEVVATDKTAINTIleADVRRT----EMLKKADELekqfvag 452
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTG---------DTTVTSGDATVAGKSILTNI--SDVHQNmgycPQFDAIDDL------- 2026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 453 dLTVQEELNdTFAELKAIGAYSAEARARRILAGLGFSKeMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDL 532
Cdd:TIGR01257 2027 -LTGREHLY-LYARLRGVPAEEIEKVANWSIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190
....*....|....*....|....*....|....*..
gi 24641342 533 NAVIWLDNYLQGW---KKTLLIVSHDQSFLDNVCNEI 566
Cdd:TIGR01257 2104 QARRMLWNTIVSIireGRAVVLTSHSMEECEALCTRL 2140
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
371-554 |
4.76e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.81 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 371 NLLIAHGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTAintileadvRRTEMLkkadelekqfv 450
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIA--GFLTPASGSLTLNGQDHTTTPPSR---------RPVSML----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 451 agdltVQEelNDTFAEL---KAIG-------AYSAEARA--RRILAGLGFSkEMQDRPTNKFSGGWRMRVSLARALYLEP 518
Cdd:PRK10771 77 -----FQE--NNLFSHLtvaQNIGlglnpglKLNAAQREklHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24641342 519 TLLMLDEPTNHLD--LNAVI--WLDNYLQGWKKTLLIVSH 554
Cdd:PRK10771 149 PILLLDEPFSALDpaLRQEMltLVSQVCQERQLTLLMVSH 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
374-567 |
5.14e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 374 IAHGRRYGLVGPNGHGKTTLLRHIATRafaIPPNidvllcEQEVVATDKTAIntileadvrrtemlkKADELEKQFvagD 453
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGV---LKPD------EGEVDPELKISY---------------KPQYIKPDY---D 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 454 LTVQEELNdtfaelKAIGAYSAEARARRILAGLGFSKEMqDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-- 531
Cdd:PRK13409 415 GTVEDLLR------SITDDLGSSYYKSEIIKPLQLERLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDve 487
|
170 180 190
....*....|....*....|....*....|....*...
gi 24641342 532 --LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEII 567
Cdd:PRK13409 488 qrLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
382-531 |
5.33e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.05 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 382 LVGPNGHGKTTLLRHIATRafaIPPNIDVllceQEVVATDKTAIN----TILEADVRRTEMLkkadelekqfvAGDLTVQ 457
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFR---SPKGVKG----SGSVLLNGMPIDakemRAISAYVQQDDLF-----------IPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 458 EELNDTfAELKAIGAYSAEARARR---ILAGLGFSKEMQDR---PTNK--FSGGWRMRVSLARALYLEPTLLMLDEPTNH 529
Cdd:TIGR00955 118 EHLMFQ-AHLRMPRRVTKKEKRERvdeVLQALGLRKCANTRigvPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
..
gi 24641342 530 LD 531
Cdd:TIGR00955 197 LD 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
669-876 |
5.46e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.11 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 669 LQPPILGVHNVTFAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE-----------QRKNHRL 737
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKisilgqptrqaLQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 HV--------------------GRFDqHSGehltaeesaaeYLQRLFNLPHEKARKALGSFGLVSHAHTiKMKDLSGGQK 797
Cdd:PRK15056 82 YVpqseevdwsfpvlvedvvmmGRYG-HMG-----------WLRRAKKRDRQIVTAALARVDMVEFRHR-QIGELSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 798 ARVALAELCLSAPDVLILDEPTNNLDIESidalaeaineyEGGVIIVShdeRLIRETGCTLYViedQTIN-EIVGEFDDY 876
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKT-----------EARIISLL---RELRDEGKTMLV---STHNlGSVTEFCDY 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
671-847 |
5.61e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 671 PPILGVHNVTFAfpSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPqeGEQRKNHRLHVGRFDQHS---- 746
Cdd:PRK10418 2 PQQIELRNIALQ--AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVAPcalr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 747 GEHL---------------TAEESAAEYLQRLFNLPHEKA-RKALGSFGLVSHAHTIKMK--DLSGG--QKARVALAELC 806
Cdd:PRK10418 78 GRKIatimqnprsafnplhTMHTHARETCLALGKPADDATlTAALEAVGLENAARVLKLYpfEMSGGmlQRMMIALALLC 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24641342 807 lSAPdVLILDEPTNNLDIES----IDALAEAINEYEGGVIIVSHD 847
Cdd:PRK10418 158 -EAP-FIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHD 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-554 |
5.62e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIaTRAFAIPPNIDVllcEQEVVATDKTAINTILEA 431
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF-NRLLELNEEARV---EGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 432 -DVRRT--EMLKKADELEKQFVAGDLTVQEELNDTFAELKAIgaysaEARARRILAGLGFSKEMQDR----PTNkFSGGW 504
Cdd:PRK14267 81 iEVRREvgMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKEL-----DERVEWALKKAALWDEVKDRlndyPSN-LSGGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24641342 505 RMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK--TLLIVSH 554
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
333-570 |
5.85e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.81 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 333 MSQVQKSAGQKAALEQAVD--IKIENFTI-SAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIA------TRAFA 403
Cdd:COG4178 342 LEAADALPEAASRIETSEDgaLALEDLTLrTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygSGRIA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 404 IPPNIDVLLCEQ----------EVVA-------TDKTAINTILEAdVRRTEMLKKADElekqfvagdltvqeelndtfae 466
Cdd:COG4178 422 RPAGARVLFLPQrpylplgtlrEALLypataeaFSDAELREALEA-VGLGHLAERLDE---------------------- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 467 lkaigaysaEARARRILaglgfskemqdrptnkfSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQG-- 544
Cdd:COG4178 479 ---------EADWDQVL-----------------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREel 532
|
250 260
....*....|....*....|....*.
gi 24641342 545 WKKTLLIVSHdQSFLDNVCNEIIHLD 570
Cdd:COG4178 533 PGTTVISVGH-RSTLAAFHDRVLELT 557
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
358-574 |
6.35e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.06 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 358 TISAKGNDlfvNANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVVAtdktaintilEADVRRTE 437
Cdd:PRK13641 17 PMEKKGLD---NISFELEEGSFVALVGHTGSGKSTLMQHF--NALLKPSSGTITIAGYHITP----------ETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 438 MLKKADELEKQFVAGDLTVQEELNDTFAELKAIGAYSAEAR--ARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALY 515
Cdd:PRK13641 82 KLRKKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKekALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 516 LEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK---TLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
704-847 |
6.53e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.01 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 704 AIVGPNGVGKSTFLKLLLGELEPQEGEQRKNH---------------RLHVGRFDQHSGEHLTAE--ESAAEYLQRLFNL 766
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvRKRIGMVFQFPESQLFEDtvEREIIFGPKNFKM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 767 PHEKAR----KALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYE---- 838
Cdd:PRK13646 117 NLDEVKnyahRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtden 196
|
....*....
gi 24641342 839 GGVIIVSHD 847
Cdd:PRK13646 197 KTIILVSHD 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
349-645 |
6.57e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 349 AVDIKIENFTISAK-GNDLFVNANLLIAHGRRYGLVGPNGHGKTTLlrhIATRAFAIPPNIDVLLCEQEVVATdKTAINT 427
Cdd:PLN03232 614 AISIKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKTSL---ISAMLGELSHAETSSVVIRGSVAY-VPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 428 ILEADVRRTEMLKKADELEKQFVAGDLT-VQEELNdtfaelkaigaysaeararrILAGLGFSkEMQDRPTNkFSGGWRM 506
Cdd:PLN03232 690 IFNATVRENILFGSDFESERYWRAIDVTaLQHDLD--------------------LLPGRDLT-EIGERGVN-ISGGQKQ 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 507 RVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNY-----LQGwkKTLLIVSHDQSFLDNVcNEIIHLDQKKLQyYKGNY 581
Cdd:PLN03232 748 RVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScmkdeLKG--KTRVLVTNQLHFLPLM-DRIILVSEGMIK-EEGTF 823
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 582 -------SMFKKMY--VQKRREMIKEYEKQEKRLRElkahGQSKKAAEKKQKESLTRKQEKNKSKQQKQDEDE 645
Cdd:PLN03232 824 aelsksgSLFKKLMenAGKMDATQEVNTNDENILKL----GPTVTIDVSERNLGSTKQGKRGRSVLVKQEERE 892
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
693-850 |
6.77e-06 |
|
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: 48.03 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDF-GIDLTSRVAIVGPNGVGKSTFLKLLLGELEpqeGEQRKNHRLHVGRFDQHSGEH-----LTAEESAAEY-LQRLFN 765
Cdd:cd03279 20 IDFtGLDNNGLFLICGPTGAGKSTILDAITYALY---GKTPRYGRQENLRSVFAPGEDtaevsFTFQLGGKKYrVERSRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 766 LPHEKARKAL----GSFG--LVSHAHTikmkdLSGGQKARVALAeLCLSAPDV-----------LILDEPTNNLDIESID 828
Cdd:cd03279 97 LDYDQFTRIVllpqGEFDrfLARPVST-----LSGGETFLASLS-LALALSEVlqnrggarleaLFIDEGFGTLDPEALE 170
|
170 180
....*....|....*....|....*
gi 24641342 829 ALAEAINEYEGG---VIIVSHDERL 850
Cdd:cd03279 171 AVATALELIRTEnrmVGVISHVEEL 195
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
676-853 |
7.29e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 48.92 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIKVDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGeLE-PQEGeqrknhRLHVGrfdqhsGEHL 750
Cdd:COG1135 4 LENLSKTFPTKGGPVTALD-DVSLTIEkgeiFGIIGYSGAGKSTLIRCINL-LErPTSG------SVLVD------GVDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 751 TAEESAAeyLQRL----------FNLPHEK------------------ARKA-----LGSFGLVSHAHTiKMKDLSGGQK 797
Cdd:COG1135 70 TALSERE--LRAArrkigmifqhFNLLSSRtvaenvalpleiagvpkaEIRKrvaelLELVGLSDKADA-YPSQLSGGQK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 798 ARV----ALAelclSAPDVLILDEPTNNLDIE---SIDALAEAINEyEGG--VIIVSHDERLIRE 853
Cdd:COG1135 147 QRVgiarALA----NNPKVLLCDEATSALDPEttrSILDLLKDINR-ELGltIVLITHEMDVVRR 206
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
703-866 |
7.64e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEpqeGEQRKNHRLHVGRFDQhSGEHLTAEEsaAEYLQRLFNLPHEKARKA-------- 774
Cdd:PRK13547 30 TALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTGDVTL-NGEPLAAID--APRLARLRAVLPQAAQPAfafsarei 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 775 --LGSF------GLVSH--------------AHTIKMKD---LSGGQKARV----ALAEL-----CLSAPDVLILDEPTN 820
Cdd:PRK13547 104 vlLGRYpharraGALTHrdgeiawqalalagATALVGRDvttLSGGELARVqfarVLAQLwpphdAAQPPRYLLLDEPTA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24641342 821 NLDIESIDALAEAI----NEYEGGVIIVSHDERLIRETGCTLYVIEDQTI 866
Cdd:PRK13547 184 ALDLAHQHRLLDTVrrlaRDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
768-845 |
7.88e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.63 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 768 HEKARKALGSFGLVSHAHTIKMKDLSGG--QKarVALAELCLSAPDVLILDEPTNNLDIES-------IDALAEaineyE 838
Cdd:COG1129 371 RALAEEYIKRLRIKTPSPEQPVGNLSGGnqQK--VVLAKWLATDPKVLILDEPTRGIDVGAkaeiyrlIRELAA-----E 443
|
....*...
gi 24641342 839 G-GVIIVS 845
Cdd:COG1129 444 GkAVIVIS 451
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
696-851 |
8.26e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 696 GIDLTSRV----AIVGPNGVGKSTFLKLLLG--ELEPQEGEQRknhrlhvgrFDQHSGEHLTAEESAAEYLQRLFNLPHE 769
Cdd:PRK09580 19 GLNLEVRPgevhAIMGPNGSGKSTLSATLAGreDYEVTGGTVE---------FKGKDLLELSPEDRAGEGIFMAFQYPVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 770 --------------------KARKALGSFG----LVSHAHTIKMKD----------LSGGQKARVALAELCLSAPDVLIL 815
Cdd:PRK09580 90 ipgvsnqfflqtalnavrsyRGQEPLDRFDfqdlMEEKIALLKMPEdlltrsvnvgFSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 24641342 816 DEPTNNLDIESIDALAEAINEYEGG---VIIVSHDERLI 851
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSLRDGkrsFIIVTHYQRIL 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
687-823 |
8.28e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.16 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 687 KPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHRLHVGR-------FdQHSG--EHLTAEESAA 757
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaergvvF-QNEGllPWRNVQDNVA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 758 EYLQrLFNLPHE----KARKALGSFGLvSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD 823
Cdd:PRK11248 93 FGLQ-LAGVEKMqrleIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
369-555 |
8.78e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.54 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDVLLCEQEVVATDKTAINtileadVRRTEMLKKADELEKQ 448
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHF--NGILKPTSGEVLIKGEPIKYDKKSLLE------VRKTVGIVFQNPDDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAgdlTVQEELndTFAELK-AIGAYSAEARARRILAGLGFSKeMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPT 527
Cdd:PRK13639 92 FAP---TVEEDV--AFGPLNlGLSKEEVEKRVKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190
....*....|....*....|....*....|.
gi 24641342 528 NHLDLNAVIWLDNYLQGWKK---TLLIVSHD 555
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
678-847 |
8.87e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.47 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 678 NVTFAFPSQKPLFIKVDFGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGE----------------QRKNHRL 737
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNNTSLTFKknkvTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanlkkikEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 HVG---RFDQHSGEHLTAEESAAEYLQRLFNLPHEKARKALGSFGLVSHAHTIKMK---DLSGGQKARVALAELCLSAPD 811
Cdd:PRK13645 91 EIGlvfQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRspfELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24641342 812 VLILDEPTNNLDI---ESIDALAEAIN-EYEGGVIIVSHD 847
Cdd:PRK13645 171 TLVLDEPTGGLDPkgeEDFINLFERLNkEYKKRIIMVTHN 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
500-570 |
9.02e-06 |
|
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: 46.76 E-value: 9.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 500 FSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTLLIVSHDQSfLDNVCNEIIHLD 570
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPS-LWKFHDRVLDLD 161
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
382-573 |
9.34e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 382 LVGPNGHGKTTLLRHIAtrAFAIPPNIDVLLCEQEVVATDKTAINtilEADVRRT----EMLKKADELEKQFVAGDLTVQ 457
Cdd:PRK11300 36 LIGPNGAGKTTVFNCLT--GFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTfqhvRLFREMTVIENLLVAQHQQLK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 458 EELndtFAELKAIGAY---SAEA--RARRILAGLGFsKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHL-- 530
Cdd:PRK11300 111 TGL---FSGLLKTPAFrraESEAldRAATWLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLnp 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24641342 531 ----DLNAVIwlDNYLQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKK 573
Cdd:PRK11300 187 ketkELDELI--AELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
377-531 |
1.03e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 48.18 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 377 GRRYGLVGPNGHGKTTLLRhiatrafaippnidvllceqevvatdktAINTILEAD--------------VRRT-----E 437
Cdd:COG4152 27 GEIFGLLGPNGAGKTTTIR----------------------------IILGILAPDsgevlwdgepldpeDRRRigylpE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 438 ---MLKKadelekqfvagdLTVQEELNDtFAELKAIGAYSAEARARRILAGLGFsKEMQDRPTNKFSGGWRMRVSLARAL 514
Cdd:COG4152 79 ergLYPK------------MKVGEQLVY-LARLKGLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAAL 144
|
170
....*....|....*..
gi 24641342 515 YLEPTLLMLDEPTNHLD 531
Cdd:COG4152 145 LHDPELLILDEPFSGLD 161
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
381-555 |
1.04e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.08 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIATrafAIPPNIDVLLCEQEVVATDKTAINTIleadvrRTEMLKKADELEKQFVAGDLTvqeel 460
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSG---LLRPQKGAVLWQGKPLDYSKRGLLAL------RQQVATVFQDPEQQIFYTDID----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 461 NDTFAELKAIGAYSAEArARRILAGLGF--SKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD---LNAV 535
Cdd:PRK13638 97 SDIAFSLRNLGVPEAEI-TRRVDEALTLvdAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagRTQM 175
|
170 180
....*....|....*....|
gi 24641342 536 IWLDNYLQGWKKTLLIVSHD 555
Cdd:PRK13638 176 IAIIRRIVAQGNHVIISSHD 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
673-846 |
1.15e-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: 49.63 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFP-SQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQR---KNHRLHVGRFDQHSG- 747
Cdd:TIGR01257 1937 ILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATvagKSILTNISDVHQNMGy 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 748 --------EHLTAEESAAEYlQRLFNLPHEKARK----ALGSFGLVSHAHTIKmKDLSGGQKARVALAELCLSAPDVLIL 815
Cdd:TIGR01257 2017 cpqfdaidDLLTGREHLYLY-ARLRGVPAEEIEKvanwSIQSLGLSLYADRLA-GTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190
....*....|....*....|....*....|....
gi 24641342 816 DEPTNNLDIESIDALAE---AINEYEGGVIIVSH 846
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNtivSIIREGRAVVLTSH 2128
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-555 |
1.18e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.72 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIaTRAFAIppnidvllcEQEVVATDKTAI--NTIL 429
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNEL---------ESEVRVEGRVEFfnQNIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 EadvRRTEMLKKADELEKQFVAGDLTVQEELNDTFAELKAIGaYSAEARARRILAGLGFSKEMQDRPTNK-------FSG 502
Cdd:PRK14258 78 E---RRVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVG-WRPKLEIDDIVESALKDADLWDEIKHKihksaldLSG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 503 GWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK----KTLLIVSHD 555
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHN 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
494-569 |
1.42e-05 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 48.17 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 494 DRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPtnhldLNAviwLDN--------YLQGWKKTL----LIVSHDqsfLDn 561
Cdd:COG4148 128 DRRPATLSGGERQRVAIGRALLSSPRLLLMDEP-----LAA---LDLarkaeilpYLERLRDELdipiLYVSHS---LD- 195
|
....*...
gi 24641342 562 vcnEIIHL 569
Cdd:COG4148 196 ---EVARL 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
499-574 |
1.48e-05 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 46.54 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 499 KFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-------LNAVIwldNYLQGwkKTLLIVSHDQSFLDNVcNEIIHLDQ 571
Cdd:cd03247 98 RFSGGERQRLALARILLQDAPIVLLDEPTVGLDpiterqlLSLIF---EVLKD--KTLIWITHHLTGIEHM-DKILFLEN 171
|
...
gi 24641342 572 KKL 574
Cdd:cd03247 172 GKI 174
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
381-526 |
1.51e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 47.33 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 381 GLVGPNGHGKTTLLRHIATRafaIPPNI-DVLLCEQEVvaTD----KTAINTI--L--EADVRRtemlkkadelekqfva 451
Cdd:COG1137 33 GLLGPNGAGKTTTFYMIVGL---VKPDSgRIFLDGEDI--THlpmhKRARLGIgyLpqEASIFR---------------- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 452 gDLTVQEELnDTFAELKAIGAYSAEARARRILAGLGFSKeMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEP 526
Cdd:COG1137 92 -KLTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITH-LRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
490-567 |
1.55e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.18 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 490 KEMQDRPtNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNA---VIWLDNYLQGWKKTLLI-VSHDQSFLDNVCNE 565
Cdd:PRK09473 153 KRMKMYP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELKREFNTAIImITHDLGVVAGICDK 231
|
..
gi 24641342 566 II 567
Cdd:PRK09473 232 VL 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
681-847 |
1.62e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.35 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 681 FAFPSQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHR-LHVGRfDQHSGEHLTAEESAAEY 759
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvLYFGK-DIFQIDAIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 760 LQRLFNLPH--------------------------EKARKALGSFGLVSHAHTIKMKDLSGGQKARVALAELCLSAPDVL 813
Cdd:PRK14246 96 FQQPNPFPHlsiydniayplkshgikekreikkivEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 24641342 814 ILDEPTNNLDIESIDALAEAINEY--EGGVIIVSHD 847
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHN 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
377-566 |
1.83e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 377 GRRYGLVGPNGHGKTT----LLRHIATRAFAIPPN---IDVLLCEQevvatdktaintiLEAdVRRtemlkkadelEKQF 449
Cdd:PRK10261 350 GETLSLVGESGSGKSTtgraLLRLVESQGGEIIFNgqrIDTLSPGK-------------LQA-LRR----------DIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 450 VAGD----LTVQEELNDTFAE-LKAIGAYSAEARARRI---LAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLL 521
Cdd:PRK10261 406 IFQDpyasLDPRQTVGDSIMEpLRVHGLLPGKAAAARVawlLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24641342 522 MLDEPTNHLDLNAVIWLDNYLQGWKKTL----LIVSHDQSFLDNVCNEI 566
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISHDMAVVERISHRV 534
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
676-850 |
1.86e-05 |
|
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: 46.72 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 676 VHNVTFAFPSQKPLFIK-VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE------------------------ 730
Cdd:cd03244 5 FKNVSLRYRPNLPPVLKnISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSilidgvdiskiglhdlrsrisiip 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 731 Q---------RKNhrlhVGRFDQHSGEHLtaeesaAEYLQRLfnlpHEKARKALGSFGLvshAHTIKM--KDLSGGQKAR 799
Cdd:cd03244 85 QdpvlfsgtiRSN----LDPFGEYSDEEL------WQALERV----GLKEFVESLPGGL---DTVVEEggENLSVGQRQL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24641342 800 VALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEYEGG--VIIVSHdeRL 850
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDctVLTIAH--RL 198
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
487-559 |
2.30e-05 |
|
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: 46.56 E-value: 2.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 487 GFSKEMQDRPTNkFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDN-----YLQGWKKTLLIVSHDQSFL 559
Cdd:cd03290 129 GDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegilkFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
673-847 |
2.71e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 673 ILGVHNVTFAFPSQKPLFIKV---DFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGE--------QRKNHR-LHVG 740
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVrnlSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkmllRRRSRQvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 741 RFDQHSGEHL--------------------TAEESAAEYLQRLFNLPHEKA-RKALGSFGLVS--HAHTIKMK---DLSG 794
Cdd:PRK10261 92 EQSAAQMRHVrgadmamifqepmtslnpvfTVGEQIAESIRLHQGASREEAmVEAKRMLDQVRipEAQTILSRyphQLSG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 795 GQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAIN----EYEGGVIIVSHD 847
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHD 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
672-823 |
2.73e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 46.69 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 672 PILGVHNVTFAFPSQKPL-FIKVDFgiDLTSRVAIVGPNGVGKSTFLKLL--LGELEPQ---EGEQRKN-HRLHVGR--- 741
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALnSVSLDF--YPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNgHNIYSPRtdt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 742 ----------FDQHSGEHLTAEESAAeYLQRLfNLPHEKAR--KALGSfGLVSHAHTIKMKD--------LSGGQKARVA 801
Cdd:PRK14239 82 vdlrkeigmvFQQPNPFPMSIYENVV-YGLRL-KGIKDKQVldEAVEK-SLKGASIWDEVKDrlhdsalgLSGGQQQRVC 158
|
170 180
....*....|....*....|..
gi 24641342 802 LAELCLSAPDVLILDEPTNNLD 823
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALD 180
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
670-847 |
3.05e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.88 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 670 QPPILGVHNVTFAFPSQKPLFIK---------VDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNhrlhvg 740
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKPerlvkaldgVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQ------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 741 rfdqhsGEHLTAEESAAEYLQR-----LFNLPH-----------------------------EKARKALGSFGLVS-HA- 784
Cdd:PRK11308 76 ------GQDLLKADPEAQKLLRqkiqiVFQNPYgslnprkkvgqileepllintslsaaerrEKALAMMAKVGLRPeHYd 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 785 ---HtikMkdLSGGQKARVALAELCLSAPDVLILDEPTNNLDIeSIDA-----LAEAINEYEGGVIIVSHD 847
Cdd:PRK11308 150 rypH---M--FSGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQAqvlnlMMDLQQELGLSYVFISHD 214
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
352-555 |
4.75e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 352 IKIENFTISAKGNDLFVNANLLIahgrrygLVGPNGHGKTTLLRHIAT----RAFAIPPNIDVLL------CEQEVVATD 421
Cdd:COG0419 5 LRLENFRSYRDTETIDFDDGLNL-------IVGPNGAGKSTILEAIRYalygKARSRSKLRSDLInvgseeASVELEFEH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 422 KTAINTILEADVRRTEMLKKADELEKQFVAG--DLTVQEELNDTFAELKA-IGAYSAEARARRILAGLGFSKEMQDRPTN 498
Cdd:COG0419 78 GGKRYRIERRQGEFAEFLEAKPSERKEALKRllGLEIYEELKERLKELEEaLESALEELAELQKLKQEILAQLSGLDPIE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 499 KFSGGWRMRVSLARALYleptlLMLDepTNHLD---LNAVIwldNYLqgwkKTLLIVSHD 555
Cdd:COG0419 158 TLSGGERLRLALADLLS-----LILD--FGSLDeerLERLL---DAL----EELAIITHV 203
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
703-875 |
5.39e-05 |
|
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: 45.33 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLGELEPQEGEQRKNHrlhvgrFDQHSGEhltaeeSAAEYLQR--LFNLPHEkarkalgsfgl 780
Cdd:cd03233 36 VLVLGRPGSGCSTLLKALANRTEGNVSVEGDIH------YNGIPYK------EFAEKYPGeiIYVSEED----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 781 vSHAHTIKMKD----------------LSGGQKARVALAELCLSAPDVLILDEPTNNLDieSIDALaeainEYEGGVIIV 844
Cdd:cd03233 93 -VHFPTLTVREtldfalrckgnefvrgISGGERKRVSIAEALVSRASVLCWDNSTRGLD--SSTAL-----EILKCIRTM 164
|
170 180 190
....*....|....*....|....*....|.
gi 24641342 845 SHderlirETGCTLYVIEDQTINEIVGEFDD 875
Cdd:cd03233 165 AD------VLKTTTFVSLYQASDEIYDLFDK 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
792-853 |
6.08e-05 |
|
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: 46.60 E-value: 6.08e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 792 LSGGQKARVALAELCLSAPDVLILDEPTNNLDI----ESIDALAEAINEYEGGVIIVSHDERLIRE 853
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqaQILDLLKDLQRELGMALLLITHDLGVVRR 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
693-846 |
6.21e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 45.67 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 693 VDFGIDLTSRVAIVGPNGVGKSTFLKLL--LGELEPQ---EGEQRKNHR-------LHVGRFDQHSGE------HLTAEE 754
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGQdifkmdvIELRRRVQMVFQipnpipNLSIFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 755 SAA--EYLQRLFNLPHE---KARKALGSFGL---VSHAHTIKMKDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIES 826
Cdd:PRK14247 102 NVAlgLKLNRLVKSKKElqeRVRWALEKAQLwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEN 181
|
170 180
....*....|....*....|..
gi 24641342 827 IDALAEAINEY--EGGVIIVSH 846
Cdd:PRK14247 182 TAKIESLFLELkkDMTIVLVTH 203
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
501-554 |
8.36e-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: 43.96 E-value: 8.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYL-----QGwkKTLLIVSH 554
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIrrlraQG--VAVIFISH 140
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
790-846 |
8.44e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 8.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24641342 790 KDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAI----NEYEGGVIIVSH 846
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKADKTIITIAH 1417
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
495-555 |
8.87e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.92 E-value: 8.87e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 495 RPTNKFSGGWRMRVSLA-------RALYLEPTLLMLDEPTNHLDLNAVIWLDNYL-----QGwkKTLLIVSHD 555
Cdd:PRK03695 122 RSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLselcqQG--IAVVMSSHD 192
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
382-554 |
9.42e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.15 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 382 LVGPNGHGKTTLLRHIATRAFAIPpnidvllceqEVVATDKTAIN--TILEADVRRTEMLKKADELEKQFVAGDLTVQEe 459
Cdd:PRK14239 36 LIGPSGSGKSTLLRSINRMNDLNP----------EVTITGSIVYNghNIYSPRTDTVDLRKEIGMVFQQPNPFPMSIYE- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 460 lNDTFA-ELKAIGAYSA-EARARRILAGLGFSKEMQDRPTNK---FSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNA 534
Cdd:PRK14239 105 -NVVYGlRLKGIKDKQVlDEAVEKSLKGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPIS 183
|
170 180
....*....|....*....|..
gi 24641342 535 VIWLDNYLQGWKK--TLLIVSH 554
Cdd:PRK14239 184 AGKIEETLLGLKDdyTMLLVTR 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
363-571 |
1.06e-04 |
|
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: 44.53 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 363 GNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRhIATRAFAIPP------NIDVLLCEQE-------VVATDKTAINTIL 429
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILR-LLFRFYDVSSgsilidGQDIREVTLDslrraigVVPQDTVLFNDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 430 EADVRRtemlkkadelekqfvaGDLTVQEElnDTFAELKAigaysaeARARRILAGL--GFSKEMQDRPTnKFSGGWRMR 507
Cdd:cd03253 92 GYNIRY----------------GRPDATDE--EVIEAAKA-------AQIHDKIMRFpdGYDTIVGERGL-KLSGGEKQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 508 VSLARALYLEPTLLMLDEPTNHLD----------LNAViwldnyLQGwkKTLLIVSHDQSFLDNvCNEIIHLDQ 571
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDthtereiqaaLRDV------SKG--RTTIVIAHRLSTIVN-ADKIIVLKD 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
703-854 |
1.07e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 703 VAIVGPNGVGKSTFLKLLLG----------------ELEPQEGEQRKN-----------HRLHVgrFDQHSG-----EHL 750
Cdd:PRK10895 32 VGLLGPNGAGKTTTFYMVVGivprdagniiiddediSLLPLHARARRGigylpqeasifRRLSV--YDNLMAvlqirDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 751 TAEESA--AEYLQRLFNLPHekARKALGsfglvshahtikmKDLSGGQKARVALAELCLSAPDVLILDEPTNNLD-IESI 827
Cdd:PRK10895 110 SAEQREdrANELMEEFHIEH--LRDSMG-------------QSLSGGERRRVEIARALAANPKFILLDEPFAGVDpISVI 174
|
170 180
....*....|....*....|....*....
gi 24641342 828 D--ALAEAINEYEGGVIIVSHDerlIRET 854
Cdd:PRK10895 175 DikRIIEHLRDSGLGVLITDHN---VRET 200
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
665-847 |
1.13e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.79 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 665 EPSQLQPPILGVHNVTFAFPSQKPlfiKVDfGIDLTSR----VAIVGPNGVGKSTFLKLLLGELEPQEGE---------- 730
Cdd:COG3845 249 APAEPGEVVLEVENLSVRDDRGVP---ALK-DVSLEVRageiLGIAGVAGNGQSELAEALAGLRPPASGSirldgeditg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 731 ----QRKNH--------RLHVGrfdqhsgehLTAEESAAE--YLQRLFNLP------------HEKARKALGSFGLVSHA 784
Cdd:COG3845 325 lsprERRRLgvayipedRLGRG---------LVPDMSVAEnlILGRYRRPPfsrggfldrkaiRAFAEELIEEFDVRTPG 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 785 HTIKMKDLSGG--QKARVALaELcLSAPDVLILDEPTNNLDIESIDALAEAINEY--EG-GVIIVSHD 847
Cdd:COG3845 396 PDTPARSLSGGnqQKVILAR-EL-SRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrdAGaAVLLISED 461
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
501-569 |
1.13e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKKTL----LIVSHDqsfLDnvcnEIIHL 569
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREInipiLYVSHS---LD----EILRL 195
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
792-844 |
1.16e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.18 E-value: 1.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 792 LSGGQKARVALAELCLSAPDVLILDEPTNNLDIE---SIDALAEAINEyEGGVIIV 844
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPAttrSILELLKDINR-ELGLTIV 195
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
382-555 |
1.25e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 44.70 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 382 LVGPNGHGKTTLLR---HIATRAFAIPPNIDVLLCEQEVVAtdktaINTILEADVRRTEMLKKADELEKQFvagdltvqe 458
Cdd:PRK14271 52 LMGPTGSGKTTFLRtlnRMNDKVSGYRYSGDVLLGGRSIFN-----YRDVLEFRRRVGMLFQRPNPFPMSI--------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 459 eLNDTFAELKA-----IGAYSAEARARriLAGLGFSKEMQDRPTN---KFSGGWRMRVSLARALYLEPTLLMLDEPTNHL 530
Cdd:PRK14271 118 -MDNVLAGVRAhklvpRKEFRGVAQAR--LTEVGLWDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180
....*....|....*....|....*..
gi 24641342 531 DLNAVIWLDNYLQGW--KKTLLIVSHD 555
Cdd:PRK14271 195 DPTTTEKIEEFIRSLadRLTVIIVTHN 221
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
499-567 |
1.29e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.71 E-value: 1.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24641342 499 KFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD----LNAVIWLDNYLQGWKKTLLIVSHDQSFLDNVCNEII 567
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDieqrLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
792-845 |
1.33e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 1.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 792 LSGGQKARVALAELCLSAPDVLILDEPTNNLDIES-------IDALAEaineyEG-GVIIVS 845
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAkyeiytiINELAA-----EGkGVIVIS 461
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
500-554 |
2.14e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 2.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 500 FSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWK----KTLLIVSH 554
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkadKTIITIAH 1417
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
369-848 |
2.26e-04 |
|
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: 44.82 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRHIAtrafAIPP----NIDVLLCEQEVVA-----TDKTAINTILEadvrRTEML 439
Cdd:TIGR02633 19 GIDLEVRPGECVGLCGENGAGKSTLMKILS----GVYPhgtwDGEIYWSGSPLKAsnirdTERAGIVIIHQ----ELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 440 KKADELEKQFVAGDLTVQEELNDTFAELKaigaysaeaRARRILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPT 519
Cdd:TIGR02633 91 PELSVAENIFLGNEITLPGGRMAYNAMYL---------RAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 520 LLMLDEPTNHLDLNAVIWLDNYLQGWKK---TLLIVSHDQSFLDNVCNEII------HLDQKKLQyykgNYSMFKKMYVQ 590
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICvirdgqHVATKDMS----TMSEDDIITMM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 591 KRREMIKEYEKQEK-------RLRELKAHgqskkaaekkQKESLTRKQEKNKSKQQKQDEDEGPQELLARPKEYIVKFRF 663
Cdd:TIGR02633 238 VGREITSLYPHEPHeigdvilEARNLTCW----------DVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 664 PE-PSQLQPPIlgvhnvtfaFPSQKPLFIK-----VDFGIDLT----SRVAIVGPNGVGKSTFLKLLlgelepqegeqrk 733
Cdd:TIGR02633 308 GAyPGKFEGNV---------FINGKPVDIRnpaqaIRAGIAMVpedrKRHGIVPILGVGKNITLSVL------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 734 NHRLHVGRFDQhsgehlTAEESA-AEYLQRLfnlphekARKALGSFglvshahtIKMKDLSGGQKARVALAELCLSAPDV 812
Cdd:TIGR02633 366 KSFCFKMRIDA------AAELQIiGSAIQRL-------KVKTASPF--------LPIGRLSGGNQQKAVLAKMLLTNPRV 424
|
490 500 510
....*....|....*....|....*....|....*...
gi 24641342 813 LILDEPTNNLDIESIDALAEAINEY--EGGVIIVSHDE 848
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLaqEGVAIIVVSSE 462
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
470-574 |
2.55e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 43.32 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 470 IGAYSAEARARRILAGL---GFSKEMQDRPTnKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD---LNAVIWLDNYLQ 543
Cdd:PRK10908 106 IAGASGDDIRRRVSAALdkvGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFN 184
|
90 100 110
....*....|....*....|....*....|.
gi 24641342 544 GWKKTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:PRK10908 185 RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
382-554 |
3.10e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.57 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 382 LVGPNGHGKTTL--LRHiatRAFAipPnidvllcEQEVVATDKTAINTILEADVRRTemlkkadelekqfVAgdlTVQEE 459
Cdd:PRK13657 366 IVGPTGAGKSTLinLLQ---RVFD--P-------QSGRILIDGTDIRTVTRASLRRN-------------IA---VVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 460 ---LNDTFAELKAIG---AYSAEAR-ARRILAGLGFskeMQDRPT----------NKFSGGWRMRVSLARALYLEPTLLM 522
Cdd:PRK13657 418 aglFNRSIEDNIRVGrpdATDEEMRaAAERAQAHDF---IERKPDgydtvvgergRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 24641342 523 LDEPTNHLD------LNAViwLDNYLQGwkKTLLIVSH 554
Cdd:PRK13657 495 LDEATSALDveteakVKAA--LDELMKG--RTTFIIAH 528
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
475-531 |
3.64e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 3.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 475 AEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD 531
Cdd:NF000106 121 ARARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
792-845 |
4.43e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 4.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 792 LSGGQKARVALAELCLSAPDVLILDEPTNNLDIES-------IDALAEaineyEG-GVIIVS 845
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAkyeiyklINQLVQ-----QGvAIIVIS 462
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
382-573 |
4.61e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.45 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 382 LVGPNGHGKTTLLR-------HIATRAFAI---PPNIDVLLCEQEVVATDKTAINTILEADVRRT---EMLKKADELEKQ 448
Cdd:COG3593 28 LVGENNSGKSSILEalrlllgPSSSRKFDEedfYLGDDPDLPEIEIELTFGSLLSRLLRLLLKEEdkeELEEALEELNEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGDLTVQEELNDTFAELKA---IGAYSAEARARRILAGLGFS-KEMQDRPTNKFSGGWRMRVSLARALYL-------E 517
Cdd:COG3593 108 LKEALKALNELLSEYLKELLDgldLELELSLDELEDLLKSLSLRiEDGKELPLDRLGSGFQRLILLALLSALaelkrapA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 518 PTLLMLDEPTNHLDLNAVIWLDNYLQ---GWKKTLLIVSHDQSFLDNVC-NEIIHLDQKK 573
Cdd:COG3593 188 NPILLIEEPEAHLHPQAQRRLLKLLKelsEKPNQVIITTHSPHLLSEVPlENIRRLRRDS 247
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
664-847 |
4.68e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.17 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 664 PEPSQLQPPILGVHNVTFAFPSQKPLFIKVD---FGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQ---EGEQRKNHRl 737
Cdd:PRK09473 3 PLAQQQADALLDVKDLRVTFSTPDGDVTAVNdlnFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 738 HVGRFDQHSGEHLTAEESAAEYLQRLFNL-PHEKARKALGSFgLVSHAH---------TIKMKD---------------- 791
Cdd:PRK09473 82 EILNLPEKELNKLRAEQISMIFQDPMTSLnPYMRVGEQLMEV-LMLHKGmskaeafeeSVRMLDavkmpearkrmkmyph 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 792 -LSGGQKARVALAELCLSAPDVLILDEPTNNLDIeSIDA-----LAEAINEYEGGVIIVSHD 847
Cdd:PRK09473 161 eFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHD 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
500-532 |
5.04e-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: 44.13 E-value: 5.04e-04
10 20 30
....*....|....*....|....*....|...
gi 24641342 500 FSGGWRMRVSLARALYLEPTLLMLDEPTNHLDL 532
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
473-562 |
5.06e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.17 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 473 YSAEARARRILAGL-----GFSKEMQDRPTNkFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD-------LNAVIWLDN 540
Cdd:TIGR00957 730 YQQVLEACALLPDLeilpsGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEG 808
|
90 100
....*....|....*....|..
gi 24641342 541 YLQGwkKTLLIVSHDQSFLDNV 562
Cdd:TIGR00957 809 VLKN--KTRILVTHGISYLPQV 828
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
349-645 |
5.23e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 349 AVDIKIENFTISAKGND-LFVNANLLIAHGRRYGLVGPNGHGKTTLlrhIATRAFAIPPNIDVllceqEVVATDKTA--- 424
Cdd:PLN03130 614 AISIKNGYFSWDSKAERpTLSNINLDVPVGSLVAIVGSTGEGKTSL---ISAMLGELPPRSDA-----SVVIRGTVAyvp 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 425 -INTILEADVRRTEMLKKADELEKQFVAGDLT-VQEELNdtfaelkaigaysaeararrILAGlGFSKEMQDRPTNkFSG 502
Cdd:PLN03130 686 qVSWIFNATVRDNILFGSPFDPERYERAIDVTaLQHDLD--------------------LLPG-GDLTEIGERGVN-ISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 503 GWRMRVSLARALYLEPTLLMLDEPTNHLDLN-AVIWLDNYLQG--WKKTLLIVSHDQSFLDNVcNEIIHLDQKKLQyYKG 579
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDelRGKTRVLVTNQLHFLSQV-DRIILVHEGMIK-EEG 821
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 580 NYS-------MFKKMyVQKRREMiKEYEKQEKRLRELKAHGQ---SKKAAEKKQKESLTRKQEKNKSKQQKQDEDE 645
Cdd:PLN03130 822 TYEelsnngpLFQKL-MENAGKM-EEYVEENGEEEDDQTSSKpvaNGNANNLKKDSSSKKKSKEGKSVLIKQEERE 895
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
705-836 |
5.83e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 705 IVGPNGVGKSTFLKLLLGELE---------------PQEgEQRKNHRLHV---GRFDQHSGeHLTAEESA--AEYLQ--- 761
Cdd:TIGR00956 92 VLGRPGSGCSTLLKTIASNTDgfhigvegvitydgiTPE-EIKKHYRGDVvynAETDVHFP-HLTVGETLdfAARCKtpq 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 762 -RLFNLPHEKARK-----ALGSFGLvSHAHTIKMKD-----LSGGQKARVALAELCLSAPDVLILDEPTNNLD----IES 826
Cdd:TIGR00956 170 nRPDGVSREEYAKhiadvYMATYGL-SHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDsataLEF 248
|
170
....*....|
gi 24641342 827 IDALAEAINE 836
Cdd:TIGR00956 249 IRALKTSANI 258
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
365-531 |
6.03e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 365 DLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIA--TRAFAIPpnidvllceqevvATDKTAINTILEADVR---RTEML 439
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsnTDGFHIG-------------VEGVITYDGITPEEIKkhyRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 440 KKAdELEKQFvaGDLTVQEELnDTFAELKAIG----AYSAEARARRI----LAGLGFSKEMQDRPTNKF----SGGWRMR 507
Cdd:TIGR00956 142 YNA-ETDVHF--PHLTVGETL-DFAARCKTPQnrpdGVSREEYAKHIadvyMATYGLSHTRNTKVGNDFvrgvSGGERKR 217
|
170 180
....*....|....*....|....
gi 24641342 508 VSLARALYLEPTLLMLDEPTNHLD 531
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
348-564 |
6.58e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.56 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 348 QAVDIKIENFTISAK-GNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRhiATRAFaippnidVLLCEQEVvatdktain 426
Cdd:PRK15056 3 QQAGIVVNDVTVTWRnGHTALRDASFTVPGGSIAALVGVNGSGKSTLFK--ALMGF-------VRLASGKI--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 427 TILEADVRRTemlkkadeLEKQFVAGdLTVQEELNDTFAELKA----IGAYS-------AEARARRILAGLGFSKEMQD- 494
Cdd:PRK15056 65 SILGQPTRQA--------LQKNLVAY-VPQSEEVDWSFPVLVEdvvmMGRYGhmgwlrrAKKRDRQIVTAALARVDMVEf 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 495 --RPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNA---VIWLDNYLQGWKKTLLIVSHDQSFLDNVCN 564
Cdd:PRK15056 136 rhRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
382-560 |
7.32e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 382 LVGPNGHGKTTLLRHIAtraFAI----PPNIDVLLCEQEVVATDKTaintILEADVRRTEMLKKADELEKQFVAGDLTV- 456
Cdd:cd03240 27 IVGQNGAGKTTIIEALK---YALtgelPPNSKGGAHDPKLIREGEV----RAQVKLAFENANGKKYTITRSLAILENVIf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 457 --QEELNDTFAELkaIGAYSAearARRILAGLGFskemqdrptnkfsggwrmRVSLARALYLEPTLLMLDEPTNHLD--- 531
Cdd:cd03240 100 chQGESNWPLLDM--RGRCSG---GEKVLASLII------------------RLALAETFGSNCGILALDEPTTNLDeen 156
|
170 180 190
....*....|....*....|....*....|...
gi 24641342 532 ----LNAVIwlDNYLQGWKKTLLIVSHDQSFLD 560
Cdd:cd03240 157 ieesLAEII--EERKSQKNFQLIVITHDEELVD 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
349-598 |
8.27e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.48 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 349 AVDIKIENFTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIatRAFAIPPNIDvllceQEVVATDKTAINTI 428
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLI--NGLLLPDDNP-----NSKITVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 429 LEADVRRTE--MLKKADeleKQFVAGdlTVQEELndtfaelkaigAYSAEARA----------RRILAGLGFSKEMQDRP 496
Cdd:PRK13640 78 TVWDIREKVgiVFQNPD---NQFVGA--TVGDDV-----------AFGLENRAvprpemikivRDVLADVGMLDYIDSEP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 497 TNkFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNA---VIWLDNYLQGwKKTLLIVS--HDqsfLD--NVCNEIIHL 569
Cdd:PRK13640 142 AN-LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqILKLIRKLKK-KNNLTVISitHD---IDeaNMADQVLVL 216
|
250 260
....*....|....*....|....*....
gi 24641342 570 DQKKLQYYKGNYSMFKKMyvqkrrEMIKE 598
Cdd:PRK13640 217 DDGKLLAQGSPVEIFSKV------EMLKE 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
501-554 |
8.56e-04 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 41.76 E-value: 8.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLDLN--AVIW--LDNYLQGwkKTLLIVSH 554
Cdd:cd03249 141 SGGQKQRIAIARALLRNPKILLLDEATSALDAEseKLVQeaLDRAMKG--RTTIVIAH 196
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
793-889 |
8.73e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 793 SGGQKA------RVALAELCLSAPDVLILDEPTNNLDIESID----ALAEAINEYEGG----VIIVSHDERLIRETGCTL 858
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIEslahALVEIIKSRSQQrnfqLLVITHDEDFVELLGRSE 1280
|
90 100 110
....*....|....*....|....*....|.
gi 24641342 859 YVIEDQTINEIVGEFDDYRKEVLDSLGEVVN 889
Cdd:TIGR00606 1281 YVEKFYRLKKNEDQCSEIVKCSPSSLGKRVH 1311
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
369-613 |
9.28e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 42.30 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 369 NANLLIAHGRRYGLVGPNGHGKTTLLRhiATRAFAIPPNIDVLLCEQEVVATDKTaintileadVRRTEMLKKADELEKQ 448
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQ--LTNGLIISETGQTIVGDYAIPANLKK---------IKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 449 FVAGDL---TVQEELndTFAELKaIGAYSAEARAR--RILAGLGFSKEMQDRPTNKFSGGWRMRVSLARALYLEPTLLML 523
Cdd:PRK13645 98 FPEYQLfqeTIEKDI--AFGPVN-LGENKQEAYKKvpELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 524 DEPTNHLD-------LNAVIWLDnylQGWKKTLLIVSHDQSFLDNVCNEIIHLDQKKLQYYKGNYSMFKKMYVQKRREMi 596
Cdd:PRK13645 175 DEPTGGLDpkgeedfINLFERLN---KEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEI- 250
|
250
....*....|....*..
gi 24641342 597 kEYEKQEKRLRELKAHG 613
Cdd:PRK13645 251 -DPPKLYQLMYKLKNKG 266
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
374-562 |
9.43e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.03 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 374 IAHGRRYGLVGPNGHGKTTLLRHIatrafaippniDVLLcEQE----VVATDKTAINTILEADVRRTEMLKKADeleKQF 449
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLI-----------DGLL-EAEsgqiIIDGDLLTEENVWDIRHKIGMVFQNPD---NQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 450 VAGdlTVQEELndTFA-ELKAIGAYSAEARARRILAGLGFSkEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTN 528
Cdd:PRK13650 95 VGA--TVEDDV--AFGlENKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 24641342 529 HLDLNAVIWLDNYLQGWKK----TLLIVSHDqsfLDNV 562
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDdyqmTVISITHD---LDEV 204
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
376-560 |
1.09e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 376 HGRRYGLVGPNGHGKTTLLRHIAtrAFAIPPNIDVLlceqeVVATDKTAINTILEADVRRTEMLKKADELEKqfvagdlt 455
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA--RELGPPGGGVI-----YIDGEDILEEVLDQLLLIIVGGKKASGSGEL-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 456 vqeelndtfaelkaigaysaeararrilaglgfskemqdrptnkfsggwRMRVSLARALYLEPTLLMLDEPTNHLD---- 531
Cdd:smart00382 66 -------------------------------------------------RLRLALALARKLKPDVLILDEITSLLDaeqe 96
|
170 180 190
....*....|....*....|....*....|....
gi 24641342 532 -----LNAVIWLDNYLQGWKKTLLIVSHDQSFLD 560
Cdd:smart00382 97 allllLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
362-531 |
1.10e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 362 KGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLRHIAtRAFAiPPNIDVLLCEQE---------------VVATDKTAIN 426
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIE-RLYD-PTEGDIIINDSHnlkdinlkwwrskigVVSQDPLLFS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 427 TILEADVRRT-EMLKKADELEKQF--------------------VAGDL------TVQEELNDTFAELKAIGAYSAEARA 479
Cdd:PTZ00265 474 NSIKNNIKYSlYSLKDLEALSNYYnedgndsqenknkrnscrakCAGDLndmsntTDSNELIEMRKNYQTIKDSEVVDVS 553
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 480 RRILAGlGFSKEMQDR-------PTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD 531
Cdd:PTZ00265 554 KKVLIH-DFVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
501-531 |
1.14e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 41.99 E-value: 1.14e-03
10 20 30
....*....|....*....|....*....|.
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLD 531
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
769-847 |
1.36e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 769 EKARKALGsfglvshahtIKMKD-------LSGGQKARVALAElCLSA-PDVLILDEPTNNLDIES---IDALAEAINEY 837
Cdd:PRK15439 384 ERYRRALN----------IKFNHaeqaartLSGGNQQKVLIAK-CLEAsPQLLIVDEPTRGVDVSArndIYQLIRSIAAQ 452
|
90
....*....|
gi 24641342 838 EGGVIIVSHD 847
Cdd:PRK15439 453 NVAVLFISSD 462
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
351-587 |
1.53e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 42.31 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 351 DIKIEN--FTISAKGNDLFVNANLLIAHGRRYGLVGPNGHGKTTLLrHIATRAFAIppnidvllceqevvatDKTAIntI 428
Cdd:PRK11176 341 DIEFRNvtFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA-NLLTRFYDI----------------DEGEI--L 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 429 LEA-DVRRTEMlkkaDELEKQFVagdLTVQEE--LNDTFAELKAIGA---YSAE--ARARRILAGLGFSKEMQD------ 494
Cdd:PRK11176 402 LDGhDLRDYTL----ASLRNQVA---LVSQNVhlFNDTIANNIAYARteqYSREqiEEAARMAYAMDFINKMDNgldtvi 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 495 -RPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK--TLLIVSHDQSFLDNVcNEIIHLDQ 571
Cdd:PRK11176 475 gENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAHRLSTIEKA-DEILVVED 553
|
250 260
....*....|....*....|....*
gi 24641342 572 ---------KKLQYYKGNYSMFKKM 587
Cdd:PRK11176 554 geivergthAELLAQNGVYAQLHKM 578
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
501-532 |
1.69e-03 |
|
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: 41.38 E-value: 1.69e-03
10 20 30
....*....|....*....|....*....|..
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLDL 532
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
792-847 |
2.24e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.92 E-value: 2.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 792 LSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEY--EGGVIIVSHD 847
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHN 209
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
501-574 |
2.93e-03 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 39.72 E-value: 2.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAV--IW---LDNYLQGwkKTLLIVSHDQSFLDNVCNEIIHLDQKKL 574
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKaeIYrliRELADAG--KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
477-531 |
4.51e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.21 E-value: 4.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 24641342 477 ARARRILaGLGfskEMQDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD 531
Cdd:PRK11650 116 AEAARIL-ELE---PLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
792-853 |
4.78e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.11 E-value: 4.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24641342 792 LSGGQKARVALAELCLSAPDVLILDEPTNNLDI----ESIDALAEAINEYEGGVIIVSHDERLIRE 853
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALVAE 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
494-560 |
6.59e-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: 38.46 E-value: 6.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24641342 494 DRPTNKFSGGWRMRVSLARALY--LEPTLLMLDEPTNHLDLNAVIWLDNYLQGW---KKTLLIVSHDQSFLD 560
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVLS 153
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
478-534 |
6.61e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.03 E-value: 6.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 478 RARRILaGLGFSKEmqDRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNA 534
Cdd:PRK15439 385 RYRRAL-NIKFNHA--EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
662-845 |
6.66e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.10 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 662 RFPEPSQlQPP--ILGVHNVTFAfpsQKPLFIKVDFGIDLTSRVAIVGPNGVGKSTFLKLLLGELEPQEGEQRknhrLHV 739
Cdd:PRK10982 238 RFPDKEN-KPGevILEVRNLTSL---RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTIT----LHG 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 740 GRFDQHS-------GEHLTAEESAA----EYLQRLFNLPHEKARKALGSFGLVSHA-------------------HTIKM 789
Cdd:PRK10982 310 KKINNHNaneainhGFALVTEERRStgiyAYLDIGFNSLISNIRNYKNKVGLLDNSrmksdtqwvidsmrvktpgHRTQI 389
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24641342 790 KDLSGGQKARVALAELCLSAPDVLILDEPTNNLDIESIDALAEAINEY---EGGVIIVS 845
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELakkDKGIIIIS 448
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
792-862 |
7.29e-03 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 7.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24641342 792 LSGGQKARVALAELcLSAPD----VLILDEPTNNLDIESIDALAEAINEY-EGG--VIIVSHDERLIRetgCTLYVIE 862
Cdd:cd03271 170 LSGGEAQRIKLAKE-LSKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLvDKGntVVVIEHNLDVIK---CADWIID 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
494-527 |
8.15e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 39.62 E-value: 8.15e-03
10 20 30
....*....|....*....|....*....|....
gi 24641342 494 DRPTNKFSGGWRMRVSLARALYLEPTLLMLDEPT 527
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
704-836 |
8.36e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.44 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24641342 704 AIVGPNGVGKSTFL---KLLLGElepqegeqRKNHRLHVGRFDQHSGEHLTAEESA---AEYLQRLFNLPHEKARKAlgs 777
Cdd:cd03239 26 AIVGPNGSGKSNIVdaiCFVLGG--------KAAKLRRGSLLFLAGGGVKAGINSAsveITFDKSYFLVLQGKVEQI--- 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24641342 778 fglvshahtikmkdLSGGQKARVALAEL-----CLSAPdVLILDEPTNNLDIESIDALAEAINE 836
Cdd:cd03239 95 --------------LSGGEKSLSALALIfalqeIKPSP-FYVLDEIDAALDPTNRRRVSDMIKE 143
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
501-555 |
9.06e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 38.99 E-value: 9.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 24641342 501 SGGWRMRVSLARALYLEPTLLMLDEPTNHLDLNAVIWLDNYLQGWKK--TLLIVSHD 555
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
491-531 |
9.91e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 38.86 E-value: 9.91e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 24641342 491 EMQDR---PTNKFSGGWRMRVSLARALYLEPTLLMLDEPTNHLD 531
Cdd:COG1117 143 EVKDRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| |
