|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-516 |
8.04e-118 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 357.07 E-value: 8.04e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG--RVALARQILRAGADETIAD-VFGA---- 87
Cdd:COG0488 10 GRPLLDDVSLSINPgDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDLTVLDtVLDGdael 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 88 TQAVAVLRRAEKGDASV-----------EELETAD-WTVEERIVSALARLGL-EARADTLLNQLSGGQRTRAVLAAAIFS 154
Cdd:COG0488 90 RALEAELEELEAKLAEPdedlerlaelqEEFEALGgWEAEARAEEILSGLGFpEEDLDRPVSELSGGWRRRVALARALLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 155 EPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGAIVVSHDRELLEEM-DAIIELTSLGTKRYGGGWSAYQAARAVELEAAQ 233
Cdd:COG0488 170 EPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVaTRILELDRGKLTLYPGNYSAYLEQRAERLEQEA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 234 qsltlarKTADEVDRKARALAERLDKRDAsgtrKAakgdmprilvgrRKSNAEESRgksvelaeRRRAGALDAVTAAKAR 313
Cdd:COG0488 250 -------AAYAKQQKKIAKEEEFIRRFRA----KA------------RKAKQAQSR--------IKALEKLEREEPPRRD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 314 ievlQPFSIRLPRTElPAGRQVLAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTV 393
Cdd:COG0488 299 ----KTVEIRFPPPE-RLGKKVLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 394 --SVNVPFTLLDQSVSILERGETILENFKRLNPGASDNACRAALASFRFRADAALQRVEALSGGQvlRAGLACALGGSDP 471
Cdd:COG0488 373 klGETVKIGYFDQHQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGE--KARLALAKLLLSP 450
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 14524463 472 PSLLILDEPTNHLDIDSIEAVEAGLLSYDGALVVVSHDETFLANI 516
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRV 495
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
12-522 |
1.94e-51 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 183.55 E-value: 1.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 12 SKPdgehVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG--RVALARQILRAGADETIADV--FG 86
Cdd:PRK15064 13 AKP----LFENISVKFGGgNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPneRLGKLRQDQFAFEEFTVLDTviMG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 87 ATQ--AVAVLRRA--EKGDAS------VEELETA-----DWTVEERIVSALARLGLEARADT-LLNQLSGGQRTRAVLAA 150
Cdd:PRK15064 89 HTElwEVKQERDRiyALPEMSeedgmkVADLEVKfaemdGYTAEARAGELLLGVGIPEEQHYgLMSEVAPGWKLRVLLAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 151 AIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGAIVVSHDRELLE-------EMDaiieltsLGTKR-YGGGWSAYq 222
Cdd:PRK15064 169 ALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNsvcthmaDLD-------YGELRvYPGNYDEY- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 223 aaraveLEAAqqslTLARktadevdrkaralaERLDKRDAsgtRKAAKGDMPRILVGRRKSNAEESRGKSvelaerRRAG 302
Cdd:PRK15064 241 ------MTAA----TQAR--------------ERLLADNA---KKKAQIAELQSFVSRFSANASKAKQAT------SRAK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 303 ALDavtaaKARIEVLQPFS-----IRLPRTElPAGRQVLAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTS 377
Cdd:PRK15064 288 QID-----KIKLEEVKPSSrqnpfIRFEQDK-KLHRNALEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTT 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 378 LLKVVTGELPPFKGTV----SVNVPFTLLDQSvSILERGETILE---NFKRlnPGASDNACRAALASFRFRADAALQRVE 450
Cdd:PRK15064 361 LLRTLVGELEPDSGTVkwseNANIGYYAQDHA-YDFENDLTLFDwmsQWRQ--EGDDEQAVRGTLGRLLFSQDDIKKSVK 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14524463 451 ALSGGQVLRAglacaLGGS---DPPSLLILDEPTNHLDIDSIEAVEAGLLSYDGALVVVSHDETFLAniGIGTRV 522
Cdd:PRK15064 438 VLSGGEKGRM-----LFGKlmmQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVS--SLATRI 505
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
30-513 |
7.29e-51 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 184.22 E-value: 7.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALA--RQILRAGADETIADVFGAT----QAVAVLRRA-EKGD- 101
Cdd:PRK10636 28 QKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAwvNQETPALPQPALEYVIDGDreyrQLEAQLHDAnERNDg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 102 ---ASVE-ELETAD-WTVEERIVSALARLGL-EARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDgrrA 175
Cdd:PRK10636 108 haiATIHgKLDAIDaWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---A 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 176 VIGL---LSGWRSGAIVVSHDRELLEEM-DAIIELTSLGTKRYGGGWSAYQAARAVELeAAQQSLTLARKtadevdRKAR 251
Cdd:PRK10636 185 VIWLekwLKSYQGTLILISHDRDFLDPIvDKIIHIEQQSLFEYTGNYSSFEVQRATRL-AQQQAMYESQQ------ERVA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 252 ALAERLDKRDASGTrkaakgdmprilvgrrKSNAEESRGKSVELAERrragaldavtAAKARIEVLQPFSIRLPRTeLPa 331
Cdd:PRK10636 258 HLQSYIDRFRAKAT----------------KAKQAQSRIKMLERMEL----------IAPAHVDNPFHFSFRAPES-LP- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 332 gRQVLAFDGVTAGYDPaRPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVPFTL---LDQSVSI 408
Cdd:PRK10636 310 -NPLLKMEKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLgyfAQHQLEF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 LERGETILENFKRLNPGASDNACRAALASFRFRADAALQRVEALSGGQvlRAGLACALGGSDPPSLLILDEPTNHLDIDS 488
Cdd:PRK10636 388 LRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGE--KARLVLALIVWQRPNLLLLDEPTNHLDLDM 465
|
490 500
....*....|....*....|....*
gi 14524463 489 IEAVEAGLLSYDGALVVVSHDETFL 513
Cdd:PRK10636 466 RQALTEALIDFEGALVVVSHDRHLL 490
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-516 |
3.50e-50 |
|
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: 180.52 E-value: 3.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 5 TLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQ-----GRVALARQIlragaD 78
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPgAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpgikvGYLPQEPQL-----D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 79 ETiADVFGATQA-----VAVLRR------------------AEKGDASVEELETAD-WTVEERIVSALARLGLEArADTL 134
Cdd:TIGR03719 81 PT-KTVRENVEEgvaeiKDALDRfneisakyaepdadfdklAAEQAELQEIIDAADaWDLDSQLEIAMDALRCPP-WDAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 135 LNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGAIVVSHDRELLEEMDA-IIELTSLGTKR 213
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGwILELDRGRGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 214 YGGGWSAYqaaraveLEAAQQSLTLARKTADEvdrKARALAERLDkrdasGTRKAAKGdmprilvGRRKSNAEESRGKSV 293
Cdd:TIGR03719 239 WEGNYSSW-------LEQKQKRLEQEEKEESA---RQKTLKRELE-----WVRQSPKG-------RQAKSKARLARYEEL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 294 ELAERRRagaldavtaakaRIEVLQpfsIRLPrtelPA---GRQVLAFDGVTAGYDpARPIIRDLSFSLvgPRR--VSVT 368
Cdd:TIGR03719 297 LSQEFQK------------RNETAE---IYIP----PGprlGDKVIEAENLTKAFG-DKLLIDDLSFKL--PPGgiVGVI 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 369 GPNGSGKTSLLKVVTGELPPFKGTVSV--NVPFTLLDQSVSILERGETILENFK----RLNPGASDNACRAALASFRFRA 442
Cdd:TIGR03719 355 GPNGAGKSTLFRMITGQEQPDSGTIEIgeTVKLAYVDQSRDALDPNKTVWEEISggldIIKLGKREIPSRAYVGRFNFKG 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 443 DAALQRVEALSGGQVLRAGLACAL--GGSdppsLLILDEPTNHLDIDSIEAVEAGLLSYDGALVVVSHDETFLANI 516
Cdd:TIGR03719 435 SDQQKKVGQLSGGERNRVHLAKTLksGGN----VLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRI 506
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
25-510 |
1.51e-49 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 181.60 E-value: 1.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 25 LAFGpERTGLVGRNGIGKTSVLNIIA-----GTLRP-----------SSGTVAIQ-------GRVALAR---QILRAGAD 78
Cdd:PLN03073 200 LAFG-RHYGLVGRNGTGKTTFLRYMAmhaidGIPKNcqilhveqevvGDDTTALQcvlntdiERTQLLEeeaQLVAQQRE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 79 ETIADVFGATQAVavLRRAEKGDASVEELETA--------DWTVEERIVSALARLGLEARADT-LLNQLSGGQRTRAVLA 149
Cdd:PLN03073 279 LEFETETGKGKGA--NKDGVDKDAVSQRLEEIykrlelidAYTAEARAASILAGLSFTPEMQVkATKTFSGGWRMRIALA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 150 AAIFSEPDFLLLDEPTNNLDRdgrRAVIGL---LSGWRSGAIVVSHDRELLEEM-DAIIELTSLGTKRYGGGWSAYQAAR 225
Cdd:PLN03073 357 RALFIEPDLLLLDEPTNHLDL---HAVLWLetyLLKWPKTFIVVSHAREFLNTVvTDILHLHGQKLVTYKGDYDTFERTR 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 226 AVELEAAQQsltlarktADEVDRKARA-LAERLDKRDASGTRKAakgdmpriLVgrrksnaeESRGKSVElaerrRAGAL 304
Cdd:PLN03073 434 EEQLKNQQK--------AFESNERSRShMQAFIDKFRYNAKRAS--------LV--------QSRIKALD-----RLGHV 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 305 DAVtaakarieVLQP-FSIRLPRTELPAGRQVLAFDGVTAGYdPARPII-RDLSFSLVGPRRVSVTGPNGSGKTSLLKVV 382
Cdd:PLN03073 485 DAV--------VNDPdYKFEFPTPDDRPGPPIISFSDASFGY-PGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLI 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 383 TGELPPFKGTV--SVNVPFTLLDQS-VSILERGETILENFKRLNPGASDNACRAALASFRFRADAALQRVEALSGGQVLR 459
Cdd:PLN03073 556 SGELQPSSGTVfrSAKVRMAVFSQHhVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSR 635
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 14524463 460 agLACALGGSDPPSLLILDEPTNHLDIDSIEAVEAGLLSYDGALVVVSHDE 510
Cdd:PLN03073 636 --VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDE 684
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-515 |
2.60e-45 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 168.59 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALAR--------------QILRAGADEtIADVFGATQAVAVLR 95
Cdd:PRK11147 30 ERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdpprnvegtvyDFVAEGIEE-QAEYLKRYHDISHLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 96 RAEKGDASVEELETAD--------WTVEERIVSALARLGLEAraDTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNN 167
Cdd:PRK11147 109 ETDPSEKNLNELAKLQeqldhhnlWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 168 LDRDGRRAVIGLLSGWRsGAIV-VSHDRELLEEMDAII------ELTSlgtkrYGGGWSAYQAARAVEL--EAAQQSltl 238
Cdd:PRK11147 187 LDIETIEWLEGFLKTFQ-GSIIfISHDRSFIRNMATRIvdldrgKLVS-----YPGNYDQYLLEKEEALrvEELQNA--- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 239 arktadEVDRKaraLAErldkrDASGTRKAAKGdmprilvgRRKSNaeESRGKS-----VELAERR-RAGaldavtaaKA 312
Cdd:PRK11147 258 ------EFDRK---LAQ-----EEVWIRQGIKA--------RRTRN--EGRVRAlkalrRERSERReVMG--------TA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 313 RIEVLQpfSIRlprtelpAGRQVlaFDGVTAGYD-PARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKG 391
Cdd:PRK11147 306 KMQVEE--ASR-------SGKIV--FEMENVNYQiDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 392 TVSVNvpfTLL-----DQSVSILERGETILENF----KRLNPGASDNACRAALASFRFRADAALQRVEALSGGQVLRAGL 462
Cdd:PRK11147 375 RIHCG---TKLevayfDQHRAELDPEKTVMDNLaegkQEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLL 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 14524463 463 ACALggSDPPSLLILDEPTNHLDIDSIEAVEAGLLSYDGALVVVSHDETFLAN 515
Cdd:PRK11147 452 ARLF--LKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDN 502
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-513 |
1.12e-41 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 157.20 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 14 PDGEHVFSDLDLAFGPE-RTGLVGRNGIGKTSVLNIIAGTLRPSSGTVaiqgrvalarqILRAGA-----------DETi 81
Cdd:PRK11819 17 PPKKQILKDISLSFFPGaKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA-----------RPAPGIkvgylpqepqlDPE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 82 ADVFGATQ-----AVAVLRR--------AE---KGDASVEE-------LETAD-WTVEERIVSALARLGLEArADTLLNQ 137
Cdd:PRK11819 85 KTVRENVEegvaeVKAALDRfneiyaayAEpdaDFDALAAEqgelqeiIDAADaWDLDSQLEIAMDALRCPP-WDAKVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 138 LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDgrrAVIGL---LSGWrSGAIV-VSHDRELLEEMDA-IIELtslgtK 212
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLeqfLHDY-PGTVVaVTHDRYFLDNVAGwILEL-----D 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 213 R-----YGGGWSAYqaaraveLEAAQQSLTLARKTADEvdrKARALAERLDkrdasGTRKAAKGdmprilvgRR-KSNAE 286
Cdd:PRK11819 235 RgrgipWEGNYSSW-------LEQKAKRLAQEEKQEAA---RQKALKRELE-----WVRQSPKA--------RQaKSKAR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 287 ESRGKsvELAERrragaldavtAAKARIEVLQ---PFSIRLprtelpaGRQVLAFDGVTAGYDpARPIIRDLSFSLvgPR 363
Cdd:PRK11819 292 LARYE--ELLSE----------EYQKRNETNEifiPPGPRL-------GDKVIEAENLSKSFG-DRLLIDDLSFSL--PP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 364 R--VSVTGPNGSGKTSLLKVVTGELPPFKGTVSV--NVPFTLLDQSVSILERGETILENFK----RLNPGASDNACRAAL 435
Cdd:PRK11819 350 GgiVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgeTVKLAYVDQSRDALDPNKTVWEEISggldIIKVGNREIPSRAYV 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 436 ASFRFRADAALQRVEALSGGQVLRAGLACAL--GGSdppsLLILDEPTNHLDIDSIEAVEAGLLSYDGALVVVSHDETFL 513
Cdd:PRK11819 430 GRFNFKGGDQQKKVGVLSGGERNRLHLAKTLkqGGN----VLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFL 505
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
336-516 |
9.22e-37 |
|
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: 132.96 E-value: 9.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVnvpftllDQSVSILergeti 415
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------GSTVKIG------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 416 lenfkrlnpgasdnacraalasfrfradaalqRVEALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAVEAG 495
Cdd:cd03221 67 --------------------------------YFEQLSGGEKMRLALAKLL--LENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180
....*....|....*....|.
gi 14524463 496 LLSYDGALVVVSHDETFLANI 516
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLDQV 133
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-509 |
1.27e-36 |
|
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: 142.35 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGE-HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPS---SGTVAIQGRVALARQILRAG 76
Cdd:COG1123 3 PLLEVRDLSVRYPGGDvPAVDGVSLTIAPgETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 77 ADetIADVFGatQAVAVLRRAEKGDASVEELETADWTVEE---RIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIF 153
Cdd:COG1123 83 RR--IGMVFQ--DPMTQLNPVTVGDQIAEALENLGLSRAEaraRVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 154 SEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS----GAIVVSHDRELLEEM-DAIIELtslgtkrygggwsayQAARAVE 228
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRergtTVLLITHDLGVVAEIaDRVVVM---------------DDGRIVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 229 leaaqqsltlaRKTADEVDRKARALAERLDKRDASGTrkaakgdmprilvgrrksnaeesrgksvelaerrragaldavt 308
Cdd:COG1123 224 -----------DGPPEEILAAPQALAAVPRLGAARGR------------------------------------------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 309 aakarievlqpfsirlPRTELPAGRQVLAFDGVTAGYD----PARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTG 384
Cdd:COG1123 250 ----------------AAPAAAAAEPLLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 385 ELPPFKGTVSVN---------------------V---PFTLLDQSVSIlerGETI---LENFKRLNPGASDNACRAALAS 437
Cdd:COG1123 314 LLRPTSGSILFDgkdltklsrrslrelrrrvqmVfqdPYSSLNPRMTV---GDIIaepLRLHGLLSRAERRERVAELLER 390
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 438 FRFRADAALQRVEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDIdSIEAVEAGLL-----SYDGALVVVSHD 509
Cdd:COG1123 391 VGLPPDLADRYPHELSGGQRQRVAIARALALE--PKLLILDEPTSALDV-SVQAQILNLLrdlqrELGLTYLFISHD 464
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
15-203 |
3.02e-35 |
|
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: 131.06 E-value: 3.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG------RVALARQILRAGADETIADVFGA 87
Cdd:COG4133 13 GERLLFSGLSFTLAAgEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 88 TQAVAVLRRAEKGDASveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNN 167
Cdd:COG4133 93 RENLRFWAALYGLRAD-----------REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 14524463 168 LDRDGRRAVIGLLSGWRS--GAIVV-SHDRELLEEMDAI 203
Cdd:COG4133 162 LDAAGVALLAELIAAHLArgGAVLLtTHQPLELAAARVL 200
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
15-208 |
4.21e-34 |
|
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: 125.64 E-value: 4.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIqgrvalarqilraGADETIAdvfgatqavav 93
Cdd:cd03221 11 GGKLLLKDISLTINPgDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------------GSTVKIG----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 94 lrraekgdasveeletadwtveerivsalarlglearadtLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR 173
Cdd:cd03221 67 ----------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180 190
....*....|....*....|....*....|....*.
gi 14524463 174 RAVIGLLSGWRSGAIVVSHDRELLEEM-DAIIELTS 208
Cdd:cd03221 107 EALEEALKEYPGTVILVSHDRYFLDQVaTKIIELED 142
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-206 |
1.40e-33 |
|
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: 126.43 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 6 LSALSWSKPDGEH-VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRAGadETIAD 83
Cdd:cd03225 2 LKNLSFSYPDGARpALDDISLTIKKgEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR--RKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 84 VF--GATQAVAvlrraekgdASVEE-----LETADW---TVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIF 153
Cdd:cd03225 80 VFqnPDDQFFG---------PTVEEevafgLENLGLpeeEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 154 SEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS---GAIVVSHDRELLEE-MDAIIEL 206
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLElADRVIVL 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-199 |
3.80e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.36 E-value: 3.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSWSKpDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-VALARQIL----- 73
Cdd:COG1121 4 MPAIELENLTVSY-GGRPVLEDVSLTIPPgEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpPRRARRRIgyvpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 74 RAGADE----TIADVF--GATQAVAVLRRAEKGDasveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAV 147
Cdd:COG1121 83 RAEVDWdfpiTVRDVVlmGRYGRRGLFRRPSRAD-------------REAVDEALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14524463 148 LAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS---GAIVVSHDRELLEE 199
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVRE 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-206 |
1.11e-32 |
|
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: 124.75 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-------VALARQIlra 75
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKgEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlRELRRKV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 76 G-----AD-----ETIA-DV-FGATQAVavLRRAEkgdasveeletadwtVEERIVSALARLGLEARADTLLNQLSGGQR 143
Cdd:COG1122 78 GlvfqnPDdqlfaPTVEeDVaFGPENLG--LPREE---------------IRERVEEALELVGLEHLADRPPHELSGGQK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 144 TRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS---GAIVVSHDRELLEEM-DAIIEL 206
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELaDRVIVL 207
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-206 |
2.11e-30 |
|
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: 117.98 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGE---HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVAL-----ARQILR 74
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKgEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 75 AgadETIADVFgatQAVAVLRraekgDASVEE--------LETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRA 146
Cdd:cd03255 81 R---RHIGFVF---QSFNLLP-----DLTALEnvelplllAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14524463 147 VLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA----IVVSHDRELLEEMDAIIEL 206
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgttiVVVTHDPELAEYADRIIEL 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-206 |
2.69e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 117.63 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAF-GPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG--------RVALARQilRAGADE----TI 81
Cdd:cd03235 10 GGHPVLEDVSFEVkPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQ--RRSIDRdfpiSV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 82 ADV--FGATQAVAVLRRAEKgdasveeletADWtveERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFL 159
Cdd:cd03235 88 RDVvlMGLYGHKGLFRRLSK----------ADK---AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14524463 160 LLDEPTNNLDRDGRRAVIGLLSGWRS---GAIVVSHDRELLEE-MDAIIEL 206
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEyFDRVLLL 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-206 |
2.89e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 115.14 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGE---HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRV-------ALAR 70
Cdd:COG1136 3 PLLELRNLTKSYGTGEgevTALRGVSLSIEAgEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDisslserELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 71 qiLRAgadETIADVFgatQA---------------VAVLRRAEKGDAsveeletadwtvEERIVSALARLGLEARADTLL 135
Cdd:COG1136 83 --LRR---RHIGFVF---QFfnllpeltalenvalPLLLAGVSRKER------------RERARELLERVGLGDRLDHRP 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14524463 136 NQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW--RSGA--IVVSHDRELLEEMDAIIEL 206
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTtiVMVTHDPELAARADRVIRL 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-193 |
6.40e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 114.76 E-value: 6.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSkPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-------VALARQI--- 72
Cdd:COG1120 2 LEAENLSVG-YGGRPVLDDVSLSLPPgEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrRELARRIayv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 73 ---LRAGADETIADV--FGATQAVAVLRRAEKGDasveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAV 147
Cdd:COG1120 81 pqePPAPFGLTVRELvaLGRYPHLGLFGRPSAED-------------REAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14524463 148 LAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS----GAIVVSHD 193
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARergrTVVMVLHD 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-204 |
7.35e-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: 111.49 E-value: 7.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSwSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVAlarQILRAGADETIA 82
Cdd:COG4555 2 IEVENLS-KKYGKVPALKDVSFTAKDgEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV---RKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 83 DVFGATQAVAVLrraekgdaSVEEL--------ETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFS 154
Cdd:COG4555 78 VLPDERGLYDRL--------TVRENiryfaelyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14524463 155 EPDFLLLDEPTNNLDRDGRRAVIGLLSGWR-SGAIVV--SHDRELLEEM-DAII 204
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLfsSHIMQEVEALcDRVV 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-203 |
8.35e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 111.31 E-value: 8.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarqilragadetiaDVfgATQAVAVLRR---- 96
Cdd:COG1131 18 GVSLTVEPgEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE-----------------DV--ARDPAEVRRRigyv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 97 AEK----GDASVEEL--------ETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEP 164
Cdd:COG1131 79 PQEpalyPDLTVRENlrffarlyGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14524463 165 TNNLDRDGRRAVIGLLSGWRS-GAIVV--SHdreLLEEMDAI 203
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAeGKTVLlsTH---YLEEAERL 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-206 |
2.18e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.86 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGPER-TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG--RVALARQILRagadetIADVFGAT--Q 89
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSlTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSE------VPDSLPLTvrD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 90 AVAVLRRAEKGdaSVEELETADwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:NF040873 77 LVAMGRWARRG--LWRRLTRDD---RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14524463 170 RDGRRAVIGLLSGWRS---GAIVVSHDRELLEEMDAIIEL 206
Cdd:NF040873 152 AESRERIIALLAEEHArgaTVVVVTHDLELVRRADPCVLL 191
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-206 |
6.55e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.98 E-value: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWsKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-------------RVALA 69
Cdd:COG4619 1 LELEGLSF-RVGGKPILSPVSLTLEAgECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 70 RQILRAGADeTIADVFgatqAVAVLRRAEKGDasveeletadwtvEERIVSALARLGLEARA-DTLLNQLSGGQRTRAVL 148
Cdd:COG4619 80 PQEPALWGG-TVRDNL----PFPFQLRERKFD-------------RERALELLERLGLPPDIlDKPVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 149 AAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA----IVVSHDRELLEEM-DAIIEL 206
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgravLWVSHDPEQIERVaDRVLTL 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-200 |
2.81e-25 |
|
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: 103.43 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGeHVFSDLDLAFGPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALA-RQILRA-----GA 77
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqPQKLRRrigylPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 78 DETIADVFGATQAV---AVLRRAEKGDasveeletadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFS 154
Cdd:cd03264 80 EFGVYPNFTVREFLdyiAWLKGIPSKE------------VKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14524463 155 EPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGAIVV--SHDRELLEEM 200
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESL 195
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-206 |
7.27e-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: 108.31 E-value: 7.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-------VALARQIL 73
Cdd:COG4988 335 PSIELEDVSFSYPGGRPALDGLSLTIPPgERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 74 RAGADETIadvFGATQAvAVLRRAeKGDASVEELETADWTVE-ERIVSALARlGLearaDTLLN----QLSGGQRTRAVL 148
Cdd:COG4988 415 WVPQNPYL---FAGTIR-ENLRLG-RPDASDEELEAALEAAGlDEFVAALPD-GL----DTPLGeggrGLSGGQAQRLAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 149 AAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA--IVVSHDRELLEEMDAIIEL 206
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRtvILITHRLALLAQADRILVL 544
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
303-515 |
7.54e-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: 108.31 E-value: 7.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 303 ALDAVTAAKARIEVL--QPFSIRLPRTELPAGRQV-LAFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLL 379
Cdd:COG4988 301 RANGIAAAEKIFALLdaPEPAAPAGTAPLPAAGPPsIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 380 KVVTGELPPFKGTVSVN-VPFTLLDQSvSILER-----------GETILENFKRLNPGASDNACRAALAsfRFRADAALQ 447
Cdd:COG4988 381 NLLLGFLPPYSGSILINgVDLSDLDPA-SWRRQiawvpqnpylfAGTIRENLRLGRPDASDEELEAALE--AAGLDEFVA 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 448 RVEA------------LSGGQVLRAGLACALGgsDPPSLLILDEPTNHLDIDSIEAVEAGL--LSYDGALVVVSHDETFL 513
Cdd:COG4988 458 ALPDgldtplgeggrgLSGGQAQRLALARALL--RDAPLLLLDEPTAHLDAETEAEILQALrrLAKGRTVILITHRLALL 535
|
..
gi 14524463 514 AN 515
Cdd:COG4988 536 AQ 537
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-166 |
8.73e-25 |
|
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: 100.03 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 20 FSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAGadetIADVFgatQAVAVLRR 96
Cdd:pfam00005 1 LKNVSLTLNPgEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdlTDDERKSLRKE----IGYVF---QDPQLFPR 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 97 AEKGDASVEELETADWT---VEERIVSALARLGLEARADTLL----NQLSGGQRTRAVLAAAIFSEPDFLLLDEPTN 166
Cdd:pfam00005 74 LTVRENLRLGLLLKGLSkreKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-197 |
9.16e-25 |
|
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: 101.95 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 9 LSWSKPDGEHVFSDLDLAF-GPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRAGA---DETIADV 84
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLyAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGyvmQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 85 FGATQAVAVLRRAEKGDASVEELETAdwtveerivsaLARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEP 164
Cdd:cd03226 85 FTDSVREELLLGLKELDAGNEQAETV-----------LKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 14524463 165 TNNLDRDGRRAV---IGLLSGWRSGAIVVSHDRELL 197
Cdd:cd03226 154 TSGLDYKNMERVgelIRELAAQGKAVIVITHDYEFL 189
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-200 |
1.17e-24 |
|
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: 102.57 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALS---WSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvALARQILRAGAdE 79
Cdd:COG1124 2 LEVRNLSvsyGQGGRRVPVLKDVSLEVAPgESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR-PVTRRRRKAFR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIADVFgatQavavlrraekgD--ASVEELETADWTVEE------------RIVSALARLGLEAR-ADTLLNQLSGGQRT 144
Cdd:COG1124 80 RVQMVF---Q-----------DpyASLHPRHTVDRILAEplrihglpdreeRIAELLEQVGLPPSfLDRYPHQLSGGQRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 145 RAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS----GAIVVSHDRELLEEM 200
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerglTYLFVSHDLAVVAHL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
335-515 |
1.95e-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: 101.02 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-----VPFTLLDQSVSIL 409
Cdd:COG4133 2 MLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepirDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 410 E------RGETILEN----FKRLNPGASDNACRAALASFRFrADAALQRVEALSGGQVLRAGLACALGGsdPPSLLILDE 479
Cdd:COG4133 81 GhadglkPELTVRENlrfwAALYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLS--PAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 14524463 480 PTNHLDIDSIEAVE---AGLLSYDGALVVVSHDETFLAN 515
Cdd:COG4133 158 PFTALDAAGVALLAeliAAHLARGGAVLLTTHQPLELAA 196
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-193 |
2.18e-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: 99.82 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvALARQILRAGAdetiadvfgatQAVAV 93
Cdd:cd03214 10 GGRTVLDDLSLSIEAgEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK-DLASLSPKELA-----------RKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 94 LRRAekgdasveeletadwtveerivsaLARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR 173
Cdd:cd03214 78 VPQA------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180
....*....|....*....|....
gi 14524463 174 RAVIGLLSGWRS----GAIVVSHD 193
Cdd:cd03214 134 IELLELLRRLARergkTVVMVLHD 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-206 |
3.21e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 106.39 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGEH-VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRValarqiLRAGADE 79
Cdd:COG4987 332 PSLELEDVSFRYPGAGRpVLDGLSLTLPPgERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD------LRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIADVFG-ATQAVAVLrraekgDASVEE-----LETADwtvEERIVSALARLGLEARADTL---LN--------QLSGGQ 142
Cdd:COG4987 406 DLRRRIAvVPQRPHLF------DTTLREnlrlaRPDAT---DEELWAALERVGLGDWLAALpdgLDtwlgeggrRLSGGE 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 143 RTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA--IVVSHDRELLEEMDAIIEL 206
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRtvLLITHRLAGLERMDRILVL 542
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-206 |
4.81e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.13 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDLDLAFGPertG----LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvALARqiLRAGAde 79
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEK---GefvfLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQ-DLSR--LKRRE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 tiadvfgatqaVAVLRRaeK-G----------DASVEE-----LETADWT---VEERIVSALARLGLEARADTLLNQLSG 140
Cdd:COG2884 74 -----------IPYLRR--RiGvvfqdfrllpDRTVYEnvalpLRVTGKSrkeIRRRVREVLDLVGLSDKAKALPHELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 141 GQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW-RSGA--IVVSHDRELLEEMDA-IIEL 206
Cdd:COG2884 141 GEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTtvLIATHDLELVDRMPKrVLEL 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
301-514 |
5.63e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 105.62 E-value: 5.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 301 AGALDAVTAAKARIEVL--QPFSIRLPRTELPAGRQV-LAFDGVTAGYDPA-RPIIRDLSFSLVGPRRVSVTGPNGSGKT 376
Cdd:COG4987 296 AQHLGRVRAAARRLNELldAPPAVTEPAEPAPAPGGPsLELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 377 SLLKVVTGELPPFKGTVSVN-VP------------FTLLDQSVSILErgETILENFKRLNPGASDNACRAALAsfRFRAD 443
Cdd:COG4987 376 TLLALLLRFLDPQSGSITLGgVDlrdldeddlrrrIAVVPQRPHLFD--TTLRENLRLARPDATDEELWAALE--RVGLG 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 444 AALQRV------------EALSGGQVLRAGLACALGgSDPPsLLILDEPTNHLDIDSIEAVEAGLLSY--DGALVVVSHD 509
Cdd:COG4987 452 DWLAALpdgldtwlgeggRRLSGGERRRLALARALL-RDAP-ILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHR 529
|
....*
gi 14524463 510 ETFLA 514
Cdd:COG4987 530 LAGLE 534
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
338-509 |
8.45e-24 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 99.14 E-value: 8.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-------------VP-FTLLD 403
Cdd:cd03235 2 VEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkplekerkrigyVPqRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 404 QS--VSILERGETILENFKRLNPGASdNACRAalasfrfRADAALQRVEA----------LSGGQVLRAGLACALGGsdP 471
Cdd:cd03235 81 RDfpISVRDVVLMGLYGHKGLFRRLS-KADKA-------KVDEALERVGLseladrqigeLSGGQQQRVLLARALVQ--D 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14524463 472 PSLLILDEPTNHLDIDSIEAVEAGL--LSYDG-ALVVVSHD 509
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLreLRREGmTILVVTHD 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
15-195 |
8.70e-24 |
|
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: 99.13 E-value: 8.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRagadETIADVFgatQAVAV 93
Cdd:cd03259 11 GSVRALDDLSLTVEPgEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER----RNIGMVF---QDYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 94 -------------LRRAEKGDAsveeletadwTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLL 160
Cdd:cd03259 84 fphltvaeniafgLKLRGVPKA----------EIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 14524463 161 LDEPTNNLD---RDG-RRAVIGLLSGWRSGAIVVSHDRE 195
Cdd:cd03259 154 LDEPLSALDaklREElREELKELQRELGITTIYVTHDQE 192
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-206 |
4.79e-23 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 95.93 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrvalarQILRAGADETIADVFGATQAVAVLrr 96
Cdd:cd03230 14 TALDDISLTVEKgEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIGYLPEEPSLY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 97 aekgdasveeletADWTVEERIvsalarlglearadtllnQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAV 176
Cdd:cd03230 86 -------------ENLTVRENL------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190
....*....|....*....|....*....|....
gi 14524463 177 IGLLSGWRS-GAIVV--SHDRELLEEM-DAIIEL 206
Cdd:cd03230 135 WELLRELKKeGKTILlsSHILEEAERLcDRVAIL 168
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-208 |
5.25e-23 |
|
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: 97.50 E-value: 5.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGE---HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VAL---ARQI 72
Cdd:COG4181 7 PIIELRGLTKTVGTGAgelTILKGISLEVEAgESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdlFALdedARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 73 LRAGAdetIADVF---------GATQAVAV-LRRAEKGDAsveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQ 142
Cdd:COG4181 87 LRARH---VGFVFqsfqllptlTALENVMLpLELAGRRDA------------RARARALLERVGLGHRLDHYPAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 143 RTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW--RSGA--IVVSHDRELLEEMDAIIELTS 208
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnrERGTtlVLVTHDPALAARCDRVLRLRA 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-509 |
9.58e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 97.08 E-value: 9.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-------------VP-FT 400
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprrarrrigyVPqRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 401 LLDQS--VSILE------RGETILenFKRlnPGASDNAcraalasfrfRADAALQRVEA----------LSGGQVLRAGL 462
Cdd:COG1121 85 EVDWDfpITVRDvvlmgrYGRRGL--FRR--PSRADRE----------AVDEALERVGLedladrpigeLSGGQQQRVLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14524463 463 ACALGGsdPPSLLILDEPTNHLDIDSIEAVEA---GLLSYDGALVVVSHD 509
Cdd:COG1121 151 ARALAQ--DPDLLLLDEPFAGVDAATEEALYEllrELRREGKTILVVTHD 198
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-206 |
1.44e-22 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 101.83 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWS-KPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-------RVALARQI 72
Cdd:COG2274 472 GDIELENVSFRyPGDSPPVLDNISLTIKPgERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidPASLRRQI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 73 --------LRAGadeTIAD--VFGATqavavlrraekgDASveeletadwtvEERIVSALARLGLEARA-------DTLL 135
Cdd:COG2274 552 gvvlqdvfLFSG---TIREniTLGDP------------DAT-----------DEEIIEAARLAGLHDFIealpmgyDTVV 605
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 136 ----NQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA--IVVSHDRELLEEMDAIIEL 206
Cdd:COG2274 606 geggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRtvIIIAHRLSTIRLADRIIVL 682
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-206 |
2.65e-22 |
|
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: 95.58 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRV---ALARQILRAGadetIADVFGATQ---- 89
Cdd:cd03219 14 VALDDVSFSVRPgEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHEIARLG----IGRTFQIPRlfpe 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 90 -------AVAVLRRaEKGDASVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLD 162
Cdd:cd03219 90 ltvlenvMVAAQAR-TGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14524463 163 EPTNNLDRDGRRAVIGLLSGWRSGAI---VVSHDrelleeMDAIIEL 206
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGItvlLVEHD------MDVVMSL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
18-206 |
2.92e-22 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 93.08 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRagadetiadvfgatqavavLRR 96
Cdd:cd00267 13 TALDNVSLTLKAgEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-------------------LRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 97 aekgdasveeletadwtveeRIVsalarlglearadtLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAV 176
Cdd:cd00267 74 --------------------RIG--------------YVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....
gi 14524463 177 IGLLSGWRSGA---IVVSHDRELLEE-MDAIIEL 206
Cdd:cd00267 120 LELLRELAEEGrtvIIVTHDPELAELaADRVIVL 153
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-200 |
2.93e-22 |
|
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: 95.17 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 6 LSALSWSKPDGEHVFsdldlafgpertgLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrVALARQILRAGA--DETIAD 83
Cdd:cd03292 17 LDGINISISAGEFVF-------------LVGPSGAGKSTLLKLIYKEELPTSGTIRVNG-QDVSDLRGRAIPylRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 84 VFGATQAVAVLRRAEKGDASVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDE 163
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14524463 164 PTNNLDRDGRRAVIGLLSGW-RSGAIVV--SHDRELLEEM 200
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKInKAGTTVVvaTHAKELVDTT 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-169 |
1.15e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.39 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALS--WSKPDGE-HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAG 76
Cdd:COG1116 5 APALELRGVSkrFPTGGGGvTALDDVSLTVAAgEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK-----PVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 77 ADetIADVFgatQAVAVL--RraekgdaSVEE-----LETADWT---VEERIVSALARLGLEARADTLLNQLSGGQRTRA 146
Cdd:COG1116 80 PD--RGVVF---QEPALLpwL-------TVLDnvalgLELRGVPkaeRRERARELLELVGLAGFEDAYPHQLSGGMRQRV 147
|
170 180
....*....|....*....|...
gi 14524463 147 VLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALD 170
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-169 |
1.39e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.99 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKpDGEHVFSDLDLAFGPER-TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-VA------LARQ--IL 73
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGiTALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLdVAttpsreLAKRlaIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 74 RagadetiadvfgatQAVAVLRRAekgdaSVEEL-------------ETADWtveERIVSALARLGLEARADTLLNQLSG 140
Cdd:COG4604 81 R--------------QENHINSRL-----TVRELvafgrfpyskgrlTAEDR---EIIDEAIAYLDLEDLADRYLDELSG 138
|
170 180
....*....|....*....|....*....
gi 14524463 141 GQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-206 |
1.81e-21 |
|
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: 93.61 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSG-TVAIQGRV------------------ALARQILR 74
Cdd:COG1119 14 GGKTILDDISWTVKPgEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedvwelrkriglvspALQLRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 75 agaDETIADVF--GATQAVAVLRRAEKGDasveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAI 152
Cdd:COG1119 94 ---DETVLDVVlsGFFDSIGLYREPTDEQ-------------RERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 153 FSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW-RSGA---IVVSHDRE-LLEEMDAIIEL 206
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAptlVLVTHHVEeIPPGITHVLLL 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
335-486 |
2.74e-21 |
|
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: 93.18 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVsvnvpfTLLDQSVSILERGE- 413
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEV------LLDGRDLASLSRREl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 414 -----------------TILE-----------NFKRLNPgASDNACRAALAsfRFRADA-ALQRVEALSGGQVLRAGLAC 464
Cdd:COG1120 74 arriayvpqeppapfglTVRElvalgryphlgLFGRPSA-EDREAVEEALE--RTGLEHlADRPVDELSGGERQRVLIAR 150
|
170 180
....*....|....*....|..
gi 14524463 465 ALgGSDPPsLLILDEPTNHLDI 486
Cdd:COG1120 151 AL-AQEPP-LLLLDEPTSHLDL 170
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
338-517 |
5.51e-21 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 89.61 E-value: 5.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYdPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvpftlldqsvsilerGETILE 417
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID---------------GKDIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 418 NFKRlnpgasdnacraalasfrfRADAALQRVEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDIDSIEAVEAGL- 496
Cdd:cd00267 66 LPLE-------------------ELRRRIGYVPQLSGGQRQRVALARALLLN--PDLLLLDEPTSGLDPASRERLLELLr 124
|
170 180
....*....|....*....|...
gi 14524463 497 -LSYDG-ALVVVSHDETFLANIG 517
Cdd:cd00267 125 eLAEEGrTVIIVTHDPELAELAA 147
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
303-515 |
5.99e-21 |
|
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: 96.20 E-value: 5.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 303 ALDAVTAAKARIEVL----QPFSIRLPRTELPAgrQVLAFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSL 378
Cdd:TIGR02857 287 RADGVAAAEALFAVLdaapRPLAGKAPVTAAPA--SSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 379 LKVVTGELPPFKGTVSVN-VPFTLLD------------QSVSILErgETILENFKRLNPGASDNACRAALAsfrfraDAA 445
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNgVPLADADadswrdqiawvpQHPFLFA--GTIAENIRLARPDASDAEIREALE------RAG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 446 LQRVEA----------------LSGGQVLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAVEAGLLSYDG--ALVVVS 507
Cdd:TIGR02857 437 LDEFVAalpqgldtpigeggagLSGGQAQRLALARAF--LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVT 514
|
....*...
gi 14524463 508 HDETFLAN 515
Cdd:TIGR02857 515 HRLALAAL 522
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-203 |
1.34e-20 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 90.26 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 13 KPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarqilragadetiadvFGATQAV 91
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKgEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY-------------------SIRTDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 92 AVLRR---AEKGDASVEELetadwTVEE-----------------RIVSALAR-LGLEARADTLLNQLSGGQRTRAVLAA 150
Cdd:cd03263 72 AARQSlgyCPQFDALFDEL-----TVREhlrfyarlkglpkseikEEVELLLRvLGLTDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14524463 151 AIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGAIVV--SHDrelLEEMDAI 203
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIIltTHS---MDEAEAL 198
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
30-200 |
4.32e-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: 89.10 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-VALARQILRAGADETIADVF----GA--------TQAVAVLRR 96
Cdd:cd03257 32 ETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdLLKLSRRLRKIRRKEIQMVFqdpmSSlnprmtigEQIAEPLRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 97 AEKGDASVEEletadwtvEERIVSALARLGL-EARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRA 175
Cdd:cd03257 112 HGKLSKKEAR--------KEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQ 183
|
170 180
....*....|....*....|....*....
gi 14524463 176 VIGLLSGWRS----GAIVVSHDRELLEEM 200
Cdd:cd03257 184 ILDLLKKLQEelglTLLFITHDLGVVAKI 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-206 |
5.04e-20 |
|
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: 89.71 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 21 SDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR---------VA---LAR--QILRAGADETIAD-V 84
Cdd:COG0411 21 DDVSLEVERgEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRditglpphrIArlgIARtfQNPRLFPELTVLEnV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 85 fgatqAVAVLRRAEKGDASV---------EELEtadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSE 155
Cdd:COG0411 101 -----LVAAHARLGRGLLAAllrlprarrEERE-----ARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14524463 156 PDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA----IVVSHDrelleeMDAIIEL 206
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIRRLRDERgitiLLIEHD------MDLVMGL 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-206 |
6.23e-20 |
|
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: 87.27 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEH-VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrvalarqilragadeti 81
Cdd:cd03246 1 LEVENVSFRYPGAEPpVLRNVSFSIEPgESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 82 advfgatQAVAVLRRAEKGDasveeletadwtveerivsalaRLGLEARADTLL------NQLSGGQRTRAVLAAAIFSE 155
Cdd:cd03246 64 -------ADISQWDPNELGD----------------------HVGYLPQDDELFsgsiaeNILSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14524463 156 PDFLLLDEPTNNLDRDGRRAV---IGLLSGWRSGAIVVSHDRELLEEMDAIIEL 206
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALnqaIAALKAAGATRIVIAHRPETLASADRILVL 168
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-206 |
6.97e-20 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 87.05 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEH-VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRV--ALARQILRagadE 79
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPgEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrDLDLESLR----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIADVFgatQAVAVLrraekgDASVEEletadwtveerivsalarlglearadtllNQLSGGQRTRAVLAAAIFSEPDFL 159
Cdd:cd03228 77 NIAYVP---QDPFLF------SGTIRE-----------------------------NILSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14524463 160 LLDEPTNNLDRDGRRAVIGLLSGWRSG--AIVVSHDRELLEEMDAIIEL 206
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGktVIVIAHRLSTIRDADRIIVL 167
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
339-509 |
9.30e-20 |
|
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: 86.72 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 339 DGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVsvnvpfTLLDQSVSILERGE----- 413
Cdd:cd03214 3 ENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI------LLDGKDLASLSPKElarki 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 414 ----TILEnfkRLNpgasdnacraaLASFRFRadaalqRVEALSGGQVLRAGLACALgGSDPPsLLILDEPTNHLDID-S 488
Cdd:cd03214 76 ayvpQALE---LLG-----------LAHLADR------PFNELSGGERQRVLLARAL-AQEPP-ILLLDEPTSHLDIAhQ 133
|
170 180
....*....|....*....|....*.
gi 14524463 489 IEAVEagLL-----SYDGALVVVSHD 509
Cdd:cd03214 134 IELLE--LLrrlarERGKTVVMVLHD 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
18-199 |
1.14e-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: 87.53 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAGADetIADVFgatQAVAVL-- 94
Cdd:cd03293 18 TALEDISLSVEEgEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPD--RGYVF---QQDALLpw 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 95 RraekgdaSVEE-----LETADWT---VEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTN 166
Cdd:cd03293 88 L-------TVLDnvalgLELQGVPkaeARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 14524463 167 NLD----RDGRRAVIGLLSGWRSGAIVVSHDrelLEE 199
Cdd:cd03293 161 ALDaltrEQLQEELLDIWRETGKTVLLVTHD---IDE 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
16-203 |
1.17e-19 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 87.27 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAGADETIADVFGATQAVA 92
Cdd:cd03268 12 KKRVLDDISLHVKKgEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKsyQKNIEALRRIGALIEAPGFYPNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 93 VLRRAEKGdASVEEletadwtveERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDG 172
Cdd:cd03268 92 NLRLLARL-LGIRK---------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190
....*....|....*....|....*....|....
gi 14524463 173 RRAVIGLLSGWRSGAIVV---SHdreLLEEMDAI 203
Cdd:cd03268 162 IKELRELILSLRDQGITVlisSH---LLSEIQKV 192
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-189 |
1.26e-19 |
|
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: 87.03 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG------RVALARQILRAGAdetiadvfga 87
Cdd:TIGR01189 11 GERMLFEGLSFTLNAgEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqRDEPHENILYLGH---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 88 tqavavlRRAEKGDASVEE--------LETADWTVEErivsALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFL 159
Cdd:TIGR01189 81 -------LPGLKPELSALEnlhfwaaiHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190
....*....|....*....|....*....|..
gi 14524463 160 LLDEPTNNLDRDGRRAVIGLLSGW--RSGAIV 189
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAHlaRGGIVL 181
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
336-509 |
1.44e-19 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 87.77 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------VPFTLLDQSVSIL 409
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkditkKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 410 ----ER---GETILEN--FKRLNPGASDNACRAalasfrfRADAALQRVE----------ALSGGQVLRAGLACALGGSd 470
Cdd:COG1122 81 fqnpDDqlfAPTVEEDvaFGPENLGLPREEIRE-------RVEEALELVGlehladrpphELSGGQKQRVAIAGVLAME- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14524463 471 pPSLLILDEPTNHLDIDSIEAVEAGLLSYDGA---LVVVSHD 509
Cdd:COG1122 153 -PEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHD 193
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-206 |
1.54e-19 |
|
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: 87.30 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG---------RVALARQil 73
Cdd:TIGR02673 2 IEFHNVSKAYPGGVAALHDVSLHIRKgEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGedvnrlrgrQLPLLRR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 74 ragadeTIADVFgatQAVAVLrraekGDASVEE-----LETADW---TVEERIVSALARLGLEARADTLLNQLSGGQRTR 145
Cdd:TIGR02673 80 ------RIGVVF---QDFRLL-----PDRTVYEnvalpLEVRGKkerEIQRRVGAALRQVGLEHKADAFPEQLSGGEQQR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14524463 146 AVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW-RSGA--IVVSHDRELLEEMDA-IIEL 206
Cdd:TIGR02673 146 VAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLnKRGTtvIVATHDLSLVDRVAHrVIIL 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
338-516 |
1.81e-19 |
|
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: 86.75 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGY-DPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvpftllDQSV---SILERGE 413
Cdd:cd03225 2 LKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD------GKDLtklSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 414 TI-----------------------LENFKrLNPGASDNACRAALASFRFrADAALQRVEALSGGQVLRAGLACALggSD 470
Cdd:cd03225 76 KVglvfqnpddqffgptveeevafgLENLG-LPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVL--AM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14524463 471 PPSLLILDEPTNHLDIDSIEAVEAGL--LSYDG-ALVVVSHDETFLANI 516
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLkkLKAEGkTIIIVTHDLDLLLEL 200
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-200 |
2.18e-19 |
|
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: 91.12 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 12 SKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAGADE--------- 79
Cdd:COG1123 273 RGKGGVRAVDDVSLTLRRgETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdlTKLSRRSLRELRRRvqmvfqdpy 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 -------TIADvfgatqAVA-VLRRAEKGDASveeletadwTVEERIVSALARLGLEAR-ADTLLNQLSGGQRTRAVLAA 150
Cdd:COG1123 353 sslnprmTVGD------IIAePLRLHGLLSRA---------ERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14524463 151 AIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS----GAIVVSHDRELLEEM 200
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelglTYLFISHDLAVVRYI 471
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
326-515 |
2.45e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 91.43 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 326 RTELPAGRQVLAFDGVTAGYDPA-RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLD 403
Cdd:COG2274 464 KLSLPRLKGDIELENVSFRYPGDsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDgIDLRQID 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 404 ------------QSVSILERgeTILENFKRLNPGASD----NACR-AALASFRFRADAALQRV-----EALSGGQVLRAG 461
Cdd:COG2274 544 paslrrqigvvlQDVFLFSG--TIRENITLGDPDATDeeiiEAARlAGLHDFIEALPMGYDTVvgeggSNLSGGQRQRLA 621
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 462 LACALGGSdpPSLLILDEPTNHLDIDSIEAVEAGLLSYDG--ALVVVSHDETFLAN 515
Cdd:COG2274 622 IARALLRN--PRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTIRL 675
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
336-507 |
2.76e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 87.04 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPaRPIIRDLSFSLvgpRRVSVT---GPNGSGKTSLLKVVTGELPPFKGTVSVNvPFTLLDQSVSILER- 411
Cdd:COG1131 1 IEVRGLTKRYGD-KTALDGVSLTV---EPGEIFgllGPNGAGKTTTIRMLLGLLRPTSGEVRVL-GEDVARDPAEVRRRi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 412 -----------GETILEN------FKRLNPGASDNACRAALASFRFrADAALQRVEALSGGQVLRAGLACALGGSdpPSL 474
Cdd:COG1131 76 gyvpqepalypDLTVRENlrffarLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHD--PEL 152
|
170 180 190
....*....|....*....|....*....|....*
gi 14524463 475 LILDEPTNHLDIDSIEAVEAGLLSY--DGALVVVS 507
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELaaEGKTVLLS 187
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
349-509 |
4.14e-19 |
|
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: 86.84 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------VPFTLLDQsVSIL--ERG----ETIL 416
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkEPREARRQ-IGVLpdERGlydrLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 417 EN---FKRLNPGASDNACRAA---LASFRFRADAAlQRVEALSGGQVLRAGLACALgGSDPPsLLILDEPTNHLDIDSIE 490
Cdd:COG4555 93 ENiryFAELYGLFDEELKKRIeelIELLGLEEFLD-RRVGELSTGMKKKVALARAL-VHDPK-VLLLDEPTNGLDVMARR 169
|
170 180
....*....|....*....|..
gi 14524463 491 AVEAGLLSY--DGALVVVS-HD 509
Cdd:COG4555 170 LLREILRALkkEGKTVLFSsHI 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-197 |
4.15e-19 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 91.07 E-value: 4.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGEHVFSDLDlaFGPE---RTGLVGRNGIGKTSVLNIIAGTLRPSSGTV--AIQGRVALARQILRAG 76
Cdd:PLN03073 507 PIISFSDASFGYPGGPLLFKNLN--FGIDldsRIAMVGPNGIGKSTILKLISGELQPSSGTVfrSAKVRMAVFSQHHVDG 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 77 ADETiadvfgaTQAVAVLRRAEKGdasveeletadwTVEERIVSALARLGLEAR-ADTLLNQLSGGQRTRAVLAAAIFSE 155
Cdd:PLN03073 585 LDLS-------SNPLLYMMRCFPG------------VPEQKLRAHLGSFGVTGNlALQPMYTLSGGQKSRVAFAKITFKK 645
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14524463 156 PDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGAIVVSHDRELL 197
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLI 687
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
349-516 |
5.54e-19 |
|
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: 84.37 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvpftlldqSVSILERGETILENFKRL--NPGA 426
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL--------GKDIKKEPEEVKRRIGYLpeEPSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 427 SDNacraalasfrFRADAALQrveaLSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDIDSIEAVEAGLLSY--DGALV 504
Cdd:cd03230 85 YEN----------LTVRENLK----LSGGMKQRLALAQALLHD--PELLILDEPTSGLDPESRREFWELLRELkkEGKTI 148
|
170
....*....|...
gi 14524463 505 VV-SHDETFLANI 516
Cdd:cd03230 149 LLsSHILEEAERL 161
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
364-522 |
6.07e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 90.39 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 364 RVSVTGPNGSGKTSLLKVVTGEL---------------------PP--FKGTV---------------------SVNVpf 399
Cdd:PRK11147 31 RVCLVGRNGAGKSTLMKILNGEVllddgriiyeqdlivarlqqdPPrnVEGTVydfvaegieeqaeylkryhdiSHLV-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 400 tLLDQSVSILERGETILENFKRLNPGASDNACRAALASFRFRADAALQrveALSGGQVLRAGLACALGGSdpPSLLILDE 479
Cdd:PRK11147 109 -ETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAALS---SLSGGWLRKAALGRALVSN--PDVLLLDE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 480 PTNHLDIDSIEAVEAGLLSYDGALVVVSHDETFLANigIGTRV 522
Cdd:PRK11147 183 PTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRN--MATRI 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-206 |
6.68e-19 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 89.65 E-value: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvALArQILRAGADET 80
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRPALRPVSFTVPPgERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGV-PLA-DADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 81 IADV------FGATQAVAVlrRAEKGDASVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFS 154
Cdd:TIGR02857 398 IAWVpqhpflFAGTIAENI--RLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14524463 155 EPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA--IVVSHDRELLEEMDAIIEL 206
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRtvLLVTHRLALAALADRIVVL 529
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-195 |
6.93e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 88.23 E-value: 6.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSwsKPDGEH-VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALA-----RQI- 72
Cdd:COG3842 3 MPALELENVS--KRYGDVtALDDVSLSIEPgEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppekRNVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 73 -----------LragadeTIAD--VFGATQavavlRRAEKGDAsveeletadwtvEERIVSALARLGLEARADTLLNQLS 139
Cdd:COG3842 81 mvfqdyalfphL------TVAEnvAFGLRM-----RGVPKAEI------------RARVAELLELVGLEGLADRYPHQLS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 140 GGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW--RSG--AIVVSHDRE 195
Cdd:COG3842 138 GGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqrELGitFIYVTHDQE 197
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
15-193 |
9.80e-19 |
|
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: 85.25 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-VALARQILRAGADETIADVF--GA--- 87
Cdd:cd03261 11 GGRTVLKGVDLDVRRgEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdISGLSEAELYRLRRRMGMLFqsGAlfd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 88 ----TQAVAVLRRaekgdasvEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDE 163
Cdd:cd03261 91 sltvFENVAFPLR--------EHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14524463 164 PTNNLD-----------RDGRRAvIGLLSgwrsgaIVVSHD 193
Cdd:cd03261 163 PTAGLDpiasgviddliRSLKKE-LGLTS------IMVTHD 196
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
336-508 |
1.03e-18 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 83.59 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDP-ARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VP------------FTL 401
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDgVDlrdldleslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 402 LDQSVSILERgeTILENFkrlnpgasdnacraalasfrfradaalqrveaLSGGQVLRAGLACALGGsdPPSLLILDEPT 481
Cdd:cd03228 81 VPQDPFLFSG--TIRENI--------------------------------LSGGQRQRIAIARALLR--DPPILILDEAT 124
|
170 180
....*....|....*....|....*....
gi 14524463 482 NHLDIDSIEAVEAGLLSYDG--ALVVVSH 508
Cdd:cd03228 125 SALDPETEALILEALRALAKgkTVIVIAH 153
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
301-510 |
3.35e-18 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 87.42 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 301 AGALDAVTAAKARIEVLQPFSIRLPRTELPAGRQV------LAFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSG 374
Cdd:TIGR02868 294 AQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVglgkptLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 375 KTSLLKVVTGELPPFKGTVSVN-VPFTLLDQS-----VSILER-----GETILENFKRLNPGASDNACRAALASFRFRAD 443
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLDgVPVSSLDQDevrrrVSVCAQdahlfDTTVRENLRLARPDATDEELWAALERVGLADW 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 444 AA-----LQRV-----EALSGGQVLRAGLACALgGSDPPsLLILDEPTNHLDIDSIEAVEAGLLSYDG--ALVVVSHDE 510
Cdd:TIGR02868 454 LRalpdgLDTVlgeggARLSGGERQRLALARAL-LADAP-ILLLDEPTEHLDAETADELLEDLLAALSgrTVVLITHHL 530
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-169 |
1.66e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 83.97 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSWSKpDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQIlragADE 79
Cdd:COG3839 1 MASLELENVSKSY-GGVEALKDIDLDIEDgEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP----KDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIADVFgatQAVAV---------------LRRAEKGDasveeletadwtVEERIVSALARLGLEARADTLLNQLSGGQRT 144
Cdd:COG3839 76 NIAMVF---QSYALyphmtvyeniafplkLRKVPKAE------------IDRRVREAAELLGLEDLLDRKPKQLSGGQRQ 140
|
170 180
....*....|....*....|....*
gi 14524463 145 RAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLD 165
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
15-195 |
1.79e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 83.66 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRagadE-------------- 79
Cdd:COG1118 13 GSFTLLDDVSLEIASgELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPR----Errvgfvfqhyalfp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 --TIAD--VFGATqaVAVLRRAEKgDASVEELetadwtveerivsaLARLGLEARADTLLNQLSGGQRTRAVLAAAIFSE 155
Cdd:COG1118 89 hmTVAEniAFGLR--VRPPSKAEI-RARVEEL--------------LELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14524463 156 PDFLLLDEPTNNLD----RDGRRAVIGLLSGWRSGAIVVSHDRE 195
Cdd:COG1118 152 PEVLLLDEPFGALDakvrKELRRWLRRLHDELGGTTVFVTHDQE 195
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
352-482 |
1.92e-17 |
|
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: 79.23 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 352 IRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------VPFTLLDQSVSILE------RGETILEN- 418
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdDERKSLRKEIGYVFqdpqlfPRLTVRENl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14524463 419 -----FKRLNPGASDNACRAALASFR---FRADAALQRVEALSGGQVLRAGLACALggSDPPSLLILDEPTN 482
Cdd:pfam00005 81 rlgllLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARAL--LTKPKLLLLDEPTA 150
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-200 |
2.17e-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: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVAL--ARQILRAGADETIADVF---------GATQA 90
Cdd:cd03297 16 KIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsRKKINLPPQQRKIGLVFqqyalfphlNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 91 VA----VLRRAEKGDaSVEELetadwtveerivsaLARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTN 166
Cdd:cd03297 96 LAfglkRKRNREDRI-SVDEL--------------LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 14524463 167 NLDRDGRRAVIGLLSGWRSG----AIVVSHDRELLEEM 200
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlnipVIFVTHDLSEAEYL 198
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
339-516 |
3.56e-17 |
|
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: 79.99 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 339 DGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVPFT----------LLDQSVSI 408
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerrksigYVMQDVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 LERGETILENFKRLNPGASDNACRAA--LASFRFrADAALQRVEALSGGQVLRAGLACALGgSDPPsLLILDEPTNHLDI 486
Cdd:cd03226 83 QLFTDSVREELLLGLKELDAGNEQAEtvLKDLDL-YALKERHPLSLSGGQKQRLAIAAALL-SGKD-LLIFDEPTSGLDY 159
|
170 180 190
....*....|....*....|....*....|....
gi 14524463 487 DSIEAVeAGLL----SYDGALVVVSHDETFLANI 516
Cdd:cd03226 160 KNMERV-GELIrelaAQGKAVIVITHDYEFLAKV 192
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-200 |
3.64e-17 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 79.15 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPdGEHVFSDLDLAF-GPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-VALARQILRAgADETI 81
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIeAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdLTDLEDELPP-LRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 82 ADVFgatQAVAVLRRAekgdasveeletadwTVEERIVSALarlglearadtllnqlSGGQRTRAVLAAAIFSEPDFLLL 161
Cdd:cd03229 79 GMVF---QDFALFPHL---------------TVLENIALGL----------------SGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 162 DEPTNNLDRDGRRAVIGLLSGWRSGA----IVVSHDRELLEEM 200
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLgitvVLVTHDLDEAARL 167
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
336-508 |
4.25e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 78.80 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGY-DPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV-NVPFTLLD---------- 403
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISQWDpnelgdhvgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 404 --QSVSILErgETILENFkrlnpgasdnacraalasfrfradaalqrveaLSGGQVLRAGLACALGGSdpPSLLILDEPT 481
Cdd:cd03246 81 lpQDDELFS--GSIAENI--------------------------------LSGGQRQRLGLARALYGN--PRILVLDEPN 124
|
170 180 190
....*....|....*....|....*....|
gi 14524463 482 NHLDID---SIEAVEAGLLSYDGALVVVSH 508
Cdd:cd03246 125 SHLDVEgerALNQAIAALKAAGATRIVIAH 154
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
15-193 |
6.13e-17 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 80.41 E-value: 6.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRA-----------GA--- 77
Cdd:COG1127 16 GDRVVLDGVSLDVPRgEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQdiTGLSEKELYElrrrigmlfqgGAlfd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 78 DETIADvfgatqAVAV-LRraEKGDASVEEletadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEP 156
Cdd:COG1127 96 SLTVFE------NVAFpLR--EHTDLSEAE-------IRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14524463 157 DFLLLDEPTNNLDRDGRRAVIGLLSGWRSG----AIVVSHD 193
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElgltSVVVTHD 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-180 |
7.94e-17 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 79.93 E-value: 7.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAgADETIADVFgatQAVAVL 94
Cdd:cd03258 19 TALKDVSLSVPKgEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdlTLLSGKELRK-ARRRIGMIF---QHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 95 RRAEKGDASVEELETADWT---VEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRD 171
Cdd:cd03258 95 SSRTVFENVALPLEIAGVPkaeIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
....*....
gi 14524463 172 GRRAVIGLL 180
Cdd:cd03258 175 TTQSILALL 183
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
335-485 |
1.49e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.56 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGYDPARPIIRDLSFSLvgPRR--VSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvpftllDQSVSILERG 412
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEI--EKGefVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN------GQDLSRLKRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 413 E---------TILENFKRLN----------P----GASDNACRAalasfrfRADAALQRV----------EALSGGQVLR 459
Cdd:COG2884 73 EipylrrrigVVFQDFRLLPdrtvyenvalPlrvtGKSRKEIRR-------RVREVLDLVglsdkakalpHELSGGEQQR 145
|
170 180
....*....|....*....|....*.
gi 14524463 460 AGLACALGGSdpPSLLILDEPTNHLD 485
Cdd:COG2884 146 VAIARALVNR--PELLLADEPTGNLD 169
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-207 |
1.50e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.30 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG------RVALARQILRAGADETIAdvfGA 87
Cdd:cd03231 11 DGRALFSGLSFTLAAgEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqRDSIARGLLYLGHAPGIK---TT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 88 TQAVAVLR--RAEKGDASVEEletadwtveerivsALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPT 165
Cdd:cd03231 88 LSVLENLRfwHADHSDEQVEE--------------ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14524463 166 NNLDRDGRRAVIGLLSGW--RSGAIVVS--HDRELLEEMDAIIELT 207
Cdd:cd03231 154 TALDKAGVARFAEAMAGHcaRGGMVVLTthQDLGLSEAGARELDLG 199
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-204 |
1.90e-16 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 78.92 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQIlragADETIADVFgatQAVAVLR----- 95
Cdd:cd03296 20 DVSLDIPSgELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV----QERNVGFVF---QHYALFRhmtvf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 96 -------RAEKGDASVEELEtadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNL 168
Cdd:cd03296 93 dnvafglRVKPRSERPPEAE-----IRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14524463 169 D----RDGRRAVIGLLSGWRSGAIVVSHDR-ELLEEMDAII 204
Cdd:cd03296 168 DakvrKELRRWLRRLHDELHVTTVFVTHDQeEALEVADRVV 208
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-206 |
1.92e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.67 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 11 WSKPDGEHVFSDLDLAFGPER-TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-VALARQILRAgADETIADVFGAT 88
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPvTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpLDYSKRGLLA-LRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 89 QAVAVLRRAEKGDA-SVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNN 167
Cdd:PRK13638 87 EQQIFYTDIDSDIAfSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 168 LDRDGRR---AVIGLLSGWRSGAIVVSHDRELLEEM-DAIIEL 206
Cdd:PRK13638 167 LDPAGRTqmiAIIRRIVAQGNHVIISSHDIDLIYEIsDAVYVL 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-190 |
2.40e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.54 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHV-FSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRValarqiLRAGADETIADVFGATQAVAV 93
Cdd:PRK13538 12 DERIlFSGLSFTLNAgELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP------IRRQRDEYHQDLLYLGHQPGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 94 lrraeKGDASVEE-----LETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNL 168
Cdd:PRK13538 86 -----KTELTALEnlrfyQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|...
gi 14524463 169 DRDGRRAVIGLLSG-WRSGAIVV 190
Cdd:PRK13538 161 DKQGVARLEALLAQhAEQGGMVI 183
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-204 |
3.21e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 77.63 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 3 SITLSALSWSKPDGE-HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrvALARQI----LRAG 76
Cdd:cd03245 2 RIEFRNVSFSYPNQEiPALDNVSLTIRAgEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG--TDIRQLdpadLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 77 ADETIADV--FGATqavavLRraekgdasvEELETADWTVE-ERIVSALARLGLEARADTLLN-----------QLSGGQ 142
Cdd:cd03245 80 IGYVPQDVtlFYGT-----LR---------DNITLGAPLADdERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14524463 143 RTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSG--AIVVSHDRELLEEMDAII 204
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLVDRII 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-180 |
3.22e-16 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 78.17 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALA---RQILRAGA 77
Cdd:COG3638 1 PMLELRNLSKRYPGGTPALDDVSLEIERgEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrgRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 78 DetIADVF--------------------GATQAVAVLRRAekgdasveeletadWTVEERI--VSALARLGLEARADTLL 135
Cdd:COG3638 81 R--IGMIFqqfnlvprlsvltnvlagrlGRTSTWRSLLGL--------------FPPEDREraLEALERVGLADKAYQRA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14524463 136 NQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL 180
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLL 189
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-169 |
5.38e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 77.98 E-value: 5.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSWSKPDG---EHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAG 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpQPALQDVSLTIESgEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-----PVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 77 ADEtiADVF---------GATQAVAV-LRRAekGDASVEELETADwtveerivSALARLGLEARADTLLNQLSGGQRTRA 146
Cdd:COG4525 76 ADR--GVVFqkdallpwlNVLDNVAFgLRLR--GVPKAERRARAE--------ELLALVGLADFARRRIWQLSGGMRQRV 143
|
170 180
....*....|....*....|...
gi 14524463 147 VLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALD 166
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-169 |
5.69e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.89 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSWSKPDgEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-------VALARQI 72
Cdd:PRK09536 1 MPMIDVSDLSVEFGD-TTVLDGVDLSVREgSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaRAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 73 LRAGADETIADVFGATQAVAVLRRAEKGdasveELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAI 152
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRTPHRS-----RFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170
....*....|....*..
gi 14524463 153 FSEPDFLLLDEPTNNLD 169
Cdd:PRK09536 155 AQATPVLLLDEPTASLD 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-486 |
7.04e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.62 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQgrvalarqilrAGADETIaDVFGAT--------------------QAV 91
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEEE-----------PSWDEVL-KRFRGTelqnyfkklyngeikvvhkpQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 92 AVLRRAEKGDASvEELETADwtvEERIVSALA-RLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDR 170
Cdd:PRK13409 170 DLIPKVFKGKVR-ELLKKVD---ERGKLDEVVeRLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 171 DGRRAVIGLLsgwRSGA-----IVVSHDRELLEEMDAIIELTslgtkrYGGGwSAYQaaraveleaaqqsltlarktade 245
Cdd:PRK13409 246 RQRLNVARLI---RELAegkyvLVVEHDLAVLDYLADNVHIA------YGEP-GAYG----------------------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 246 VDRKARalaerldkrdasGTRKAA----KGDMP----RIlvgrrksnaeesrgksvelaeRRRAgaldavtaakarIEvl 317
Cdd:PRK13409 293 VVSKPK------------GVRVGIneylKGYLPeenmRI---------------------RPEP------------IE-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 318 qpFSIRLPRTElPAGRQVLAFDGVTAGYDparpiirdlSFSL-VGP---RR---VSVTGPNGSGKTSLLKVVTGELPPFK 390
Cdd:PRK13409 326 --FEERPPRDE-SERETLVEYPDLTKKLG---------DFSLeVEGgeiYEgevIGIVGPNGIGKTTFAKLLAGVLKPDE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 391 GTVSVNVPFTLLDQSVSIlERGETILENFKRLNPGASDNACRAALASfRFRADAALQR-VEALSGGQVLRAGLACALggS 469
Cdd:PRK13409 394 GEVDPELKISYKPQYIKP-DYDGTVEDLLRSITDDLGSSYYKSEIIK-PLQLERLLDKnVKDLSGGELQRVAIAACL--S 469
|
490
....*....|....*..
gi 14524463 470 DPPSLLILDEPTNHLDI 486
Cdd:PRK13409 470 RDADLYLLDEPSAHLDV 486
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
350-512 |
8.25e-16 |
|
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: 76.37 E-value: 8.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 350 PIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLDQSVSILERGETI------------- 415
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgTDISKLSEKELAAFRRRHIgfvfqsfnllpdl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 416 --LEN------FKRLNPGASDNACRAALASFRFrADAALQRVEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDID 487
Cdd:cd03255 98 taLENvelpllLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALAND--PKIILADEPTGNLDSE 174
|
170 180
....*....|....*....|....*....
gi 14524463 488 SIEAVEAGLLS----YDGALVVVSHDETF 512
Cdd:cd03255 175 TGKEVMELLRElnkeAGTTIVVVTHDPEL 203
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-196 |
1.07e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.36 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 9 LSWSKPDGEHVFSDL---DLAFGPERT-GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVAL-----ARQILRAgadE 79
Cdd:PRK10584 12 LKKSVGQGEHELSILtgvELVVKRGETiALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeeARAKLRA---K 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIADVFGATQAVAVLRRAEKGDASVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFL 159
Cdd:PRK10584 89 HVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14524463 160 LLDEPTNNLDRD-GRRAVIGLLSGWRSGA---IVVSHDREL 196
Cdd:PRK10584 169 FADEPTGNLDRQtGDKIADLLFSLNREHGttlILVTHDLQL 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
24-208 |
1.14e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 76.60 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 24 DLAFGPER---TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQI--LRagadeTIADVFGATQAV------- 91
Cdd:cd03267 39 GISFTIEKgeiVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKkfLR-----RIGVVFGQKTQLwwdlpvi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 92 ---AVLRRaekgdasVEELETADWTveERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNL 168
Cdd:cd03267 114 dsfYLLAA-------IYDLPPARFK--KRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14524463 169 DRDGRRAVIGLLsgwrsgaivvshdRELLEEMDAIIELTS 208
Cdd:cd03267 185 DVVAQENIRNFL-------------KEYNRERGTTVLLTS 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
33-200 |
1.24e-15 |
|
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: 75.78 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 33 GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRAG---------ADETIADVFgatQAVAVLRRAEKGDAs 103
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGylpeerglyPKMKVIDQL---VYLAQLKGLKKEEA- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 104 veeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD---RDGRRAVIGLL 180
Cdd:cd03269 106 -----------RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIREL 174
|
170 180
....*....|....*....|
gi 14524463 181 SGWRSGAIVVSHDRELLEEM 200
Cdd:cd03269 175 ARAGKTVILSTHQMELVEEL 194
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
30-195 |
1.34e-15 |
|
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: 77.11 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRAGA-----------------DETIA-DV------F 85
Cdd:TIGR04521 32 EFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDlrkkvglvfqfpehqlfEETVYkDIafgpknL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 86 GATQavavlrraekgdasvEEletadwtVEERIVSALARLGLEaraDTLLNQ----LSGGQRTRAVLAAAIFSEPDFLLL 161
Cdd:TIGR04521 112 GLSE---------------EE-------AEERVKEALELVGLD---EEYLERspfeLSGGQMRRVAIAGVLAMEPEVLIL 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 14524463 162 DEPTNNLDRDGRRAVIGLLSGWRSGA----IVVSHDRE 195
Cdd:TIGR04521 167 DEPTAGLDPKGRKEILDLFKRLHKEKgltvILVTHSME 204
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-481 |
1.56e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-VALA--RQILRAGadetIADVFgatQAVAVLrrae 98
Cdd:COG1129 24 SLELRPG-EVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpVRFRspRDAQAAG----IAIIH---QELNLV---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 99 kGDASVEE-------LETA---DW-TVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNN 167
Cdd:COG1129 92 -PNLSVAEniflgrePRRGgliDWrAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 168 LDRDGRRAVIGLLSGWRSG--AIV-VSHDrelLEEMdaiieltslgtkrygggwsayqaaraveleaaqqsltlarktad 244
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQgvAIIyISHR---LDEV-------------------------------------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 245 evdrkaRALAER---LdkRDAS--GTRKAAKGDMPRI---LVGRrksnaeesrgksvELAERRragaldavtaakariev 316
Cdd:COG1129 204 ------FEIADRvtvL--RDGRlvGTGPVAELTEDELvrlMVGR-------------ELEDLF----------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 317 lqpfsirlPRTELPAGRQVLAFDGVTagydpARPIIRDLSFSLvgpRR---VSVTGPNGSGKTSLLKVVTGELPPFKGTV 393
Cdd:COG1129 246 --------PKRAAAPGEVVLEVEGLS-----VGGVVRDVSFSV---RAgeiLGIAGLVGAGRTELARALFGADPADSGEI 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 394 SVN---VPFT----------------------LLDQSV------SILERgetiLENFKRLNPGASDNACRAALASFRFRA 442
Cdd:COG1129 310 RLDgkpVRIRsprdairagiayvpedrkgeglVLDLSIrenitlASLDR----LSRGGLLDRRRERALAEEYIKRLRIKT 385
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 14524463 443 DAALQRVEALSGG--Q-VLragLACALGGSdpPSLLILDEPT 481
Cdd:COG1129 386 PSPEQPVGNLSGGnqQkVV---LAKWLATD--PKVLILDEPT 422
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-180 |
2.17e-15 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 75.68 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG--RVALARQILRAGADEt 80
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPgEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdINKLKGKALRQLRRQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 81 IADVF---------GATQAVAVLRRAEK-------GDASVEELETAdwtveeriVSALARLGLEARADTLLNQLSGGQRT 144
Cdd:cd03256 80 IGMIFqqfnlierlSVLENVLSGRLGRRstwrslfGLFPKEEKQRA--------LAALERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 14524463 145 RAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL 180
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLL 187
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-165 |
2.28e-15 |
|
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: 75.16 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR---VALARQILRAGadetIA------DVFga 87
Cdd:cd03224 14 QILFGVSLTVPEgEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditGLPPHERARAG----IGyvpegrRIF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 88 tqavavlrraekGDASVEE-LETADWT-----VEERIVSALARL-GLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLL 160
Cdd:cd03224 88 ------------PELTVEEnLLLGAYArrrakRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
....*
gi 14524463 161 LDEPT 165
Cdd:cd03224 156 LDEPS 160
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-509 |
3.32e-15 |
|
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: 78.29 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPSSGtvaIQGRVALARQILRAGADETIADVFGA-----------TQAVAVLRRAEKG 100
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLG---DYDEEPSWDEVLKRFRGTELQDYFKKlangeikvahkPQYVDLIPKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 101 DASvEELETADwtvEERIVSALA-RLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR----RA 175
Cdd:COG1245 179 TVR-ELLEKVD---ERGKLDELAeKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRlnvaRL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 176 VIGLLSGWRSgAIVVSHDRELLEEMDAIIELTslgtkrYGGGwSAYQaaraveleaaqqsltlarktadeVDRKARalae 255
Cdd:COG1245 255 IRELAEEGKY-VLVVEHDLAILDYLADYVHIL------YGEP-GVYG-----------------------VVSKPK---- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 256 rldkrdasGTRKAA----KGDMP----RIlvgrrksnaeesRGKSVElaerrragaldavtaakarievlqpFSIRLPRT 327
Cdd:COG1245 300 --------SVRVGInqylDGYLPeenvRI------------RDEPIE-------------------------FEVHAPRR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 328 ElPAGRQVLAFDGVTAGYDparpiirdlSFSL-VGP---RR---VSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVPFT 400
Cdd:COG1245 335 E-KEEETLVEYPDLTKSYG---------GFSLeVEGgeiREgevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKIS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 401 LLDQSVSIlERGETILENFKRLNPGASDNACRAALASFRFRADAALQR-VEALSGGQVLRAGLACALggSDPPSLLILDE 479
Cdd:COG1245 405 YKPQYISP-DYDGTVEEFLRSANTDDFGSSYYKTEIIKPLGLEKLLDKnVKDLSGGELQRVAIAACL--SRDADLYLLDE 481
|
490 500 510
....*....|....*....|....*....|....*.
gi 14524463 480 PTNHLDIDsiEAVEAG------LLSYDGALVVVSHD 509
Cdd:COG1245 482 PSAHLDVE--QRLAVAkairrfAENRGKTAMVVDHD 515
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-190 |
3.87e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDL-AFGPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarqilragaDETIADVFGATQAVAvL 94
Cdd:PRK13539 14 GRVLFSGLSFtLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------------DIDDPDVAEACHYLG-H 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 95 RRAEKGDASVEE-LETadW-----TVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNL 168
Cdd:PRK13539 81 RNAMKPALTVAEnLEF--WaaflgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|...
gi 14524463 169 DRDGRRAVIGLLSGWR-SGAIVV 190
Cdd:PRK13539 159 DAAAVALFAELIRAHLaQGGIVI 181
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-200 |
3.91e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRAG---------ADETIADvfgatQAV--AVLRRAEKG 100
Cdd:COG4152 30 FGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGylpeerglyPKMKVGE-----QLVylARLKGLSKA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 101 DAsveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL 180
Cdd:COG4152 105 EA------------KRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVI 172
|
170 180
....*....|....*....|...
gi 14524463 181 SGWR-SGAIVV--SHDRELLEEM 200
Cdd:COG4152 173 RELAaKGTTVIfsSHQMELVEEL 195
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-175 |
3.96e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.68 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSDLDLAFgPERT--GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQIlragADETIADVFgatQAVAVLRR 96
Cdd:PRK11432 21 VIDNLNLTI-KQGTmvTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI----QQRDICMVF---QSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 97 AEKGDA---SVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR 173
Cdd:PRK11432 93 MSLGENvgyGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
..
gi 14524463 174 RA 175
Cdd:PRK11432 173 RS 174
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-204 |
1.05e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.25 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRaGADETIA 82
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKgEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQ-GIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 83 DVFGATQAVAVLRRAEKGDA-SVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLL 161
Cdd:PRK13644 81 IVFQNPETQFVGRTVEEDLAfGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14524463 162 DEPTNNLDRDGRRAVIGLLSGW-RSGAIVV--SHDRELLEEMDAII 204
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLhEKGKTIVyiTHNLEELHDADRII 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-193 |
1.89e-14 |
|
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: 75.86 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG------RVALARQILR 74
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPgERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvsslDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 75 AGADEtiADVFGATqavavLR---RAEKGDASVEELETADWTVeeRIVSALARL--GLEARADTLLNQLSGGQRTRAVLA 149
Cdd:TIGR02868 413 VCAQD--AHLFDTT-----VRenlRLARPDATDEELWAALERV--GLADWLRALpdGLDTVLGEGGARLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14524463 150 AAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSG--AIVVSHD 193
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHH 529
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-193 |
2.02e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 75.98 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRAGADETIADvfgatqavaVLRraekgDASVEELET 109
Cdd:COG1245 367 EVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYISPDYDGTVEE---------FLR-----SANTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 110 ADWtvEERIVSalaRLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR----RAVIGLLSGWRS 185
Cdd:COG1245 433 SYY--KTEIIK---PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRRFAENRGK 507
|
....*...
gi 14524463 186 GAIVVSHD 193
Cdd:COG1245 508 TAMVVDHD 515
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
340-516 |
2.10e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 340 GVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKG-----------------------TVSVN 396
Cdd:PRK11819 11 RVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGearpapgikvgylpqepqldpekTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 397 VPFTLLDQsVSILERGETILENFKrlNPGASDNACRAALASFRFRADA---------------AL------QRVEALSGG 455
Cdd:PRK11819 91 VEEGVAEV-KAALDRFNEIYAAYA--EPDADFDALAAEQGELQEIIDAadawdldsqleiamdALrcppwdAKVTKLSGG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14524463 456 QVLRAGLaCALGGSDPpSLLILDEPTNHLDIDSIEAVEAGLLSYDGALVVVSHDETFLANI 516
Cdd:PRK11819 168 ERRRVAL-CRLLLEKP-DMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNV 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
336-508 |
2.11e-14 |
|
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: 72.01 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN---VPFTLLDQSVSILERG 412
Cdd:TIGR01189 1 LAARNLACSRG-ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNgtpLAEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 413 E--------TILENFKRLNP--GASDNACRAALASFRFRADAALQrVEALSGGQVLRAGLACALggSDPPSLLILDEPTN 482
Cdd:TIGR01189 80 HlpglkpelSALENLHFWAAihGGAQRTIEDALAAVGLTGFEDLP-AAQLSAGQQRRLALARLW--LSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 14524463 483 HLDIDSIEAVEAGL---LSYDGALVVVSH 508
Cdd:TIGR01189 157 ALDKAGVALLAGLLrahLARGGIVLLTTH 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-169 |
2.45e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.12 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSDLDLAFGPER-TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-------------RVALARQILRAGADETIADV 84
Cdd:PRK11231 17 ILNDLSLSLPTGKiTALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGITVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 85 --FGATQAVAVLRRaekgdasveeLETADwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLD 162
Cdd:PRK11231 97 vaYGRSPWLSLWGR----------LSAED---NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
....*..
gi 14524463 163 EPTNNLD 169
Cdd:PRK11231 164 EPTTYLD 170
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-207 |
2.54e-14 |
|
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: 72.47 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQ---GRVALA----RQILRAGADeTIADVfgaTQA 90
Cdd:COG4778 26 VLDGVSFSVAAgECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdgGWVDLAqaspREILALRRR-TIGYV---SQF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 91 VAVLRR-------AEKGDASVEELETAdwtvEERIVSALARLGLEARadtlLNQL-----SGGQRTRAVLAAAIFSEPDF 158
Cdd:COG4778 102 LRVIPRvsaldvvAEPLLERGVDREEA----RARARELLARLNLPER----LWDLppatfSGGEQQRVNIARGFIADPPL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14524463 159 LLLDEPTNNLDRDGRRAVIGLLSGWRSG--AIV-VSHDRELLEEM-DAIIELT 207
Cdd:COG4778 174 LLLDEPTASLDAANRAVVVELIEEAKARgtAIIgIFHDEEVREAVaDRVVDVT 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
347-510 |
3.65e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.11 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 347 PARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV--NVPFTLLDQSVSILERGETILENFKRLNP 424
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRagGARVAYVPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 425 GASDNACRAALASFRFRADAALQRV----------EALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAVEA 494
Cdd:NF040873 83 WARRGLWRRLTRDDRAAVDDALERVgladlagrqlGELSGGQRQRALLAQGL--AQEADLLLLDEPTTGLDAESRERIIA 160
|
170
....*....|....*....
gi 14524463 495 GL--LSYDGALVV-VSHDE 510
Cdd:NF040873 161 LLaeEHARGATVVvVTHDL 179
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
328-508 |
4.60e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.82 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 328 ELPAGRQVLAFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VP---FTLLD 403
Cdd:COG1132 332 PLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgVDirdLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 404 ---------QSVSILERgeTILENFKRLNPGASD----NACRAALASFRFRA-----DAAL-QRVEALSGGQVLRAGLAC 464
Cdd:COG1132 412 lrrqigvvpQDTFLFSG--TIRENIRYGRPDATDeeveEAAKAAQAHEFIEAlpdgyDTVVgERGVNLSGGQRQRIAIAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14524463 465 ALgGSDPPsLLILDEPTNHLDIDSIEAVEAGL--LSYDGALVVVSH 508
Cdd:COG1132 490 AL-LKDPP-ILILDEATSALDTETEALIQEALerLMKGRTTIVIAH 533
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-204 |
6.61e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.09 E-value: 6.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGEH-VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAga 77
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQpVLKGLSLQIKAgEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiADYSEAALRQ-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 78 deTIA------DVFGATqavavLRraekgdasvEELETADWTV-EERIVSALARLGLEARADTL--LN--------QLSG 140
Cdd:PRK11160 415 --AISvvsqrvHLFSAT-----LR---------DNLLLAAPNAsDEALIEVLQQVGLEKLLEDDkgLNawlgeggrQLSG 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 141 GQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA--IVVSHDRELLEEMDAII 204
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKtvLMITHRLTGLEQFDRIC 544
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-172 |
6.76e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.65 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKpDGEHVFSDLDLAFGPERTGLV-GRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVAlarqilragadeT 80
Cdd:PRK13543 10 PLLAAHALAFSR-NEEPVFGPLDFHVDAGEALLVqGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA------------T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 81 IADvfgATQAVAVLRRAEKGDASVEELETADWT-------VEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIF 153
Cdd:PRK13543 77 RGD---RSRFMAYLGHLPGLKADLSTLENLHFLcglhgrrAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWL 153
|
170
....*....|....*....
gi 14524463 154 SEPDFLLLDEPTNNLDRDG 172
Cdd:PRK13543 154 SPAPLWLLDEPYANLDLEG 172
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
336-508 |
6.85e-14 |
|
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: 71.11 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV------NVPFTLLDQSVSIL 409
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirEVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 410 ER-----GETILENFKRLNPGASD----NACRAA-----LASFRFRADAAL-QRVEALSGGQVLRAGLACALgGSDPPsL 474
Cdd:cd03253 81 PQdtvlfNDTIGYNIRYGRPDATDeeviEAAKAAqihdkIMRFPDGYDTIVgERGLKLSGGEKQRVAIARAI-LKNPP-I 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 14524463 475 LILDEPTNHLDIDSIEAVEAGL--LSYDGALVVVSH 508
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALrdVSKGRTTIVIAH 194
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-200 |
6.91e-14 |
|
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: 73.21 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAF---GPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRV------------------------AL-----A 69
Cdd:COG4148 15 TLDVDFtlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflpphrrrigyvfqeaRLfphlsV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 70 RQILRAGadetiadvfgatqavavLRRAEKGDASVEeletadwtvEERIVsalARLGLEAradtLLN----QLSGGQRTR 145
Cdd:COG4148 95 RGNLLYG-----------------RKRAPRAERRIS---------FDEVV---ELLGIGH----LLDrrpaTLSGGERQR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 146 AVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA---IV-VSHDrelLEEM 200
Cdd:COG4148 142 VAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELdipILyVSHS---LDEV 197
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-208 |
7.00e-14 |
|
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: 70.96 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAGADETIadVF---------GATQAV 91
Cdd:TIGR01184 3 GVNLTIQQgEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-----QITEPGPDRMV--VFqnysllpwlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 92 AVLRRAEKGDASVEELETadwTVEERIvsalARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRD 171
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRA---IVEEHI----ALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14524463 172 GRRAVI-GLLSGW---RSGAIVVSHD-RELLEEMDAIIELTS 208
Cdd:TIGR01184 149 TRGNLQeELMQIWeehRVTVLMVTHDvDEALLLSDRVVMLTN 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-192 |
7.34e-14 |
|
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: 70.60 E-value: 7.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAF-GPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQIlragADETIADVFGATQAVAVLRRAEKG 100
Cdd:cd03298 16 HFDLTFaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP----ADRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 101 DASVE---ELETADwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVI 177
Cdd:cd03298 92 GLGLSpglKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170
....*....|....*....
gi 14524463 178 GLLSGWRS----GAIVVSH 192
Cdd:cd03298 169 DLVLDLHAetkmTVLMVTH 187
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
369-507 |
7.37e-14 |
|
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: 70.71 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 369 GPNGSGKTSLLKVVTGELPPFKGTVSVNVPFTLLDQSV-----SILERGE-----TILENFKRLN--PGASDNACRAALA 436
Cdd:cd03268 33 GPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAlrrigALIEAPGfypnlTARENLRLLArlLGIRKKRIDEVLD 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 437 SFRFRaDAALQRVEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDIDSIEAVEAGLLSY--DGALVVVS 507
Cdd:cd03268 113 VVGLK-DSAKKKVKGFSLGMKQRLGIALALLGN--PDLLILDEPTNGLDPDGIKELRELILSLrdQGITVLIS 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-198 |
7.85e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.03 E-value: 7.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarqilragaDETIADVFgatqavavlRR 96
Cdd:cd03218 14 KVVNGVSLSVKQgEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ------------DITKLPMH---------KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 97 AEKG------------DASVEE-----LETA---DWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEP 156
Cdd:cd03218 73 ARLGigylpqeasifrKLTVEEnilavLEIRglsKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14524463 157 DFLLLDEPTNNLD----RDGRRaVIGLLSGWRSGAIVVSHD-RELLE 198
Cdd:cd03218 153 KFLLLDEPFAGVDpiavQDIQK-IIKILKDRGIGVLITDHNvRETLS 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-169 |
7.94e-14 |
|
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: 70.75 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQilraGADETIADVFgatQAVAV-------- 93
Cdd:cd03301 20 NLDIADG-EFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP----PKDRDIAMVF---QNYALyphmtvyd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 94 -------LRRAEKGdasveeletadwTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTN 166
Cdd:cd03301 92 niafglkLRKVPKD------------EIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
...
gi 14524463 167 NLD 169
Cdd:cd03301 160 NLD 162
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
33-208 |
9.04e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 70.48 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 33 GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALA------RQILRAGADETIADVFGATQAVAVLRRaekgdasVEE 106
Cdd:cd03265 30 GLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVReprevrRRIGIVFQDLSVDDELTGWENLYIHAR-------LYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 107 LETADWTveERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVigllsgWRsg 186
Cdd:cd03265 103 VPGAERR--ERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV------WE-- 172
|
170 180
....*....|....*....|..
gi 14524463 187 aivvsHDRELLEEMDAIIELTS 208
Cdd:cd03265 173 -----YIEKLKEEFGMTILLTT 189
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-206 |
9.97e-14 |
|
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: 70.19 E-value: 9.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 9 LSWSKPDGEHVF--SDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQ---ILRAgadeTIA 82
Cdd:cd03250 8 FTWDSGEQETSFtlKDINLEVPKgELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQepwIQNG----TIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 83 D--VFGAT-------QAVAV--LRRaekgDasVEELETADWT-VEERIVSalarlglearadtllnqLSGGQRTRAVLAA 150
Cdd:cd03250 84 EniLFGKPfdeeryeKVIKAcaLEP----D--LEILPDGDLTeIGEKGIN-----------------LSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14524463 151 AIFSEPDFLLLDEPTNNLDRD-GRR----AVIGLLSGWRSgAIVVSHDRELLEEMDAIIEL 206
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHvGRHifenCILGLLLNNKT-RILVTHQLQLLPHADQIVVL 200
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
9.98e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.80 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPS--ITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGtvaiqgrvalarQILRAGA 77
Cdd:PRK13636 1 MEDyiLKVEELNYNYSDGTHALKGININIKKgEVTAILGGNGAGKSTLFQNLNGILKPSSG------------RILFDGK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 78 --DETIADVFGATQAVAVLRRAEKG---DASVEE--------LETADWTVEERIVSALARLGLEARADTLLNQLSGGQRT 144
Cdd:PRK13636 69 piDYSRKGLMKLRESVGMVFQDPDNqlfSASVYQdvsfgavnLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 145 RAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLsgwrsgaivvshdRELLEEMDAII 204
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLL-------------VEMQKELGLTI 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
320-485 |
1.05e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 320 FSIRLPRTElPAGRQVLAFdGVTAGyDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVPF 399
Cdd:COG2401 17 YSSVLDLSE-RVAIVLEAF-GVELR-VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 400 TLLDQSVSILE---RGETILENFKRLNpgasdnacRAALasfrfrADAAL--QRVEALSGGQVLRAGLACALGGSdpPSL 474
Cdd:COG2401 94 NQFGREASLIDaigRKGDFKDAVELLN--------AVGL------SDAVLwlRRFKELSTGQKFRFRLALLLAER--PKL 157
|
170
....*....|.
gi 14524463 475 LILDEPTNHLD 485
Cdd:COG2401 158 LVIDEFCSHLD 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-200 |
1.37e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.50 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVA--LArqiLRAG--ADET-------IADVF 85
Cdd:COG1134 40 WALKDVSFEVERgESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSalLE---LGAGfhPELTgreniylNGRLL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 86 GatqavavLRRAEkgdasVEEletadwtVEERIVsALArlGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEpt 165
Cdd:COG1134 117 G-------LSRKE-----IDE-------KFDEIV-EFA--ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14524463 166 nNL---DRDGRRAVIGLLSG-WRSGAIV--VSHDRELLEEM 200
Cdd:COG1134 173 -VLavgDAAFQKKCLARIRElRESGRTVifVSHSMGAVRRL 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-169 |
1.40e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-------VALARQILR------AG--ADETIADVFgatqAVAVLRRAE 98
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdvtklpeYKRAKYIGRvfqdpmMGtaPSMTIEENL----ALAYRRGKR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 99 KG----------DASVEELETADwtveerivsalarLGLEARADTLLNQLSGGQRtRAV-LAAAIFSEPDFLLLDEPTNN 167
Cdd:COG1101 113 RGlrrgltkkrrELFRELLATLG-------------LGLENRLDTKVGLLSGGQR-QALsLLMATLTKPKLLLLDEHTAA 178
|
..
gi 14524463 168 LD 169
Cdd:COG1101 179 LD 180
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-191 |
1.43e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.09 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-RVALARQILRAGadetIADVFGATQAVAVLR 95
Cdd:cd03266 19 QAVDGVSFTVKPgEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARRR----LGFVSDSTGLYDRLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 96 RAE-----------KGDAsveeletadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEP 164
Cdd:cd03266 95 AREnleyfaglyglKGDE-----------LTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180
....*....|....*....|....*....
gi 14524463 165 TNNLDRDGRRAVIGLLSGWRSG--AIVVS 191
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALgkCILFS 192
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
15-174 |
1.52e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 69.96 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAGADE-TIADVF------- 85
Cdd:cd03300 11 GGFVALDGVSLDIKEgEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK-----DITNLPPHKrPVNTVFqnyalfp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 86 --GATQAVAV-LRRAEKGDAsveeletadwTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLD 162
Cdd:cd03300 86 hlTVFENIAFgLRLKKLPKA----------EIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170
....*....|..
gi 14524463 163 EPTNNLDRDGRR 174
Cdd:cd03300 156 EPLGALDLKLRK 167
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
369-485 |
1.64e-13 |
|
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: 69.53 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 369 GPNGSGKTSLLKVVTGELPPFKGTVSVNvpftlldqSVSILERGETILE-------------NF------------KRLN 423
Cdd:cd03264 32 GPNGAGKTTLMRILATLTPPSSGTIRID--------GQDVLKQPQKLRRrigylpqefgvypNFtvrefldyiawlKGIP 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14524463 424 PGASDNACRAALASFRFrADAALQRVEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLD 485
Cdd:cd03264 104 SKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGD--PSILIVDEPTAGLD 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-193 |
1.76e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.92 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 33 GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRAGADETIADvfgatqavaVLRRAekgdasVEELETADW 112
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKPDYDGTVED---------LLRSI------TDDLGSSYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 113 TVEerIVSalaRLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR----RAVIGLLSGWRSGAI 188
Cdd:PRK13409 434 KSE--IIK---PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRRIAEEREATAL 508
|
....*
gi 14524463 189 VVSHD 193
Cdd:PRK13409 509 VVDHD 513
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
31-200 |
1.78e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.99 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 31 RTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAGADE---TIADVFGATQAVAVLRRAEKGDA-SVEE 106
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE-----PITKENIREvrkFVGLVFQNPDDQIFSPTVEQDIAfGPIN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 107 LETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW--R 184
Cdd:PRK13652 107 LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpeT 186
|
170
....*....|....*...
gi 14524463 185 SGAIVV--SHDRELLEEM 200
Cdd:PRK13652 187 YGMTVIfsTHQLDLVPEM 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
15-206 |
1.86e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.43 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPssgTVAIQGRVALARQILRAGADE-------------- 79
Cdd:COG4136 12 GGRPLLAPLSLTVAPgEILTLMGPSGSGKSTLLAAIAGTLSP---AFSASGEVLLNGRRLTALPAEqrrigilfqddllf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 ---TIAD--VFGATQAVavlRRAEKgdasveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFS 154
Cdd:COG4136 89 phlSVGEnlAFALPPTI---GRAQR---------------RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 155 EPDFLLLDEPTNNLDRDGRRAVigllSGW------RSG--AIVVSHDRELLEEMDAIIEL 206
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQF----REFvfeqirQRGipALLVTHDEEDAPAAGRVLDL 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-211 |
2.07e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.53 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGtLRPS-SGTVA----------------IQ 63
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPgERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIArpagarvlflpqrpylPL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 64 GRvaLARQILRAGADETIADvfgaTQAVAVLRRAEKGDAsVEEL-ETADWTveerivsalarlglearadtllNQLSGGQ 142
Cdd:COG4178 440 GT--LREALLYPATAEAFSD----AELREALEAVGLGHL-AERLdEEADWD----------------------QVLSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14524463 143 RTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGAIVVS--HDRELLEEMDAIIELTSLGT 211
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISvgHRSTLAAFHDRVLELTGDGS 561
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
349-508 |
2.08e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 69.06 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVpfTLLDQSVSILERG-------------ETI 415
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG--GPLDFQRDSIARGllylghapgikttLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 416 LENFKRLNPGASDNACRAALASFRFRA--DAAlqrVEALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAVE 493
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALARVGLNGfeDRP---VAQLSAGQQRRVALARLL--LSGRPLWILDEPTTALDKAGVARFA 165
|
170
....*....|....*...
gi 14524463 494 ---AGLLSYDGALVVVSH 508
Cdd:cd03231 166 eamAGHCARGGMVVLTTH 183
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
33-164 |
2.13e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.67 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 33 GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarqilragadetiaDVfgaTqAVAVLRRAEKG------DAS--- 103
Cdd:COG1137 33 GLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE-----------------DI---T-HLPMHKRARLGigylpqEASifr 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14524463 104 ---VEE-----LETADWTVEER---IVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEP 164
Cdd:COG1137 92 kltVEDnilavLELRKLSKKEReerLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-204 |
2.45e-13 |
|
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: 70.09 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalARQILRAGADETIADVFGAT-----------QAVAVLRRAEKG 100
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPD---WDEILDEFRGSELQNYFTKLlegdvkvivkpQYVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 101 DASvEELETADWT-VEERIVSalaRLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR----RA 175
Cdd:cd03236 106 KVG-ELLKKKDERgKLDELVD---QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaRL 181
|
170 180
....*....|....*....|....*....
gi 14524463 176 VIGLLSGWRSgAIVVSHDRELLEEMDAII 204
Cdd:cd03236 182 IRELAEDDNY-VLVVEHDLAVLDYLSDYI 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-208 |
2.64e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG------RVALARQIlraGAdetiadVFG----------ATQAVAV 93
Cdd:COG4586 49 EIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrRKEFARRI---GV------VFGqrsqlwwdlpAIDSFRL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 94 LRRaekgdasVEELETADWtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR 173
Cdd:COG4586 120 LKA-------IYRIPDAEY--KKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190
....*....|....*....|....*....|....*
gi 14524463 174 RAVIGLLsgwrsgaivvshdRELLEEMDAIIELTS 208
Cdd:COG4586 191 EAIREFL-------------KEYNRERGTTILLTS 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
16-169 |
2.92e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.80 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-------VALARQIlragadetiadvfga 87
Cdd:PRK13548 14 GRTLLDDVSLTLRPgEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspAELARRR--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 88 tqavAVLRRAekgdASVeeleTADWTVEE-----------------RIV-SALARLGLEARADTLLNQLSGGQRTRAVLA 149
Cdd:PRK13548 79 ----AVLPQH----SSL----SFPFTVEEvvamgraphglsraeddALVaAALAQVDLAHLAGRDYPQLSGGEQQRVQLA 146
|
170 180
....*....|....*....|....*.
gi 14524463 150 ------AAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK13548 147 rvlaqlWEPDGPPRWLLLDEPTSALD 172
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-206 |
2.94e-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: 69.10 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGE----HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALarqILRAG 76
Cdd:cd03220 16 GSSSLKKLGILGRKGEvgefWALKDVSFEVPRgERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS---LLGLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 77 A----DET-------IADVFGatqavavLRRAEKGDasveeletadwtVEERIVsALArlGLEARADTLLNQLSGGQRTR 145
Cdd:cd03220 93 GgfnpELTgreniylNGRLLG-------LSRKEIDE------------KIDEII-EFS--ELGDFIDLPVKTYSSGMKAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14524463 146 AVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA---IVVSHDRELLEEM-DAIIEL 206
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGktvILVSHDPSSIKRLcDRALVL 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-169 |
3.00e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 69.40 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 24 DLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQIlragADETIADVF---------GATQAVAV 93
Cdd:COG3840 19 DLTIAAgERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AERPVSMLFqennlfphlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 94 -------LRRAEKgdasveeletadwtveERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTN 166
Cdd:COG3840 95 glrpglkLTAEQR----------------AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
...
gi 14524463 167 NLD 169
Cdd:COG3840 159 ALD 161
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
349-508 |
3.11e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvpftlldqsvsilERGETILENFKRLNPGASD 428
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD-------------GGDIDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 429 NACRAAL---------ASFR----FRADAALQRVE----------ALSGGQVLRAGLACALGGSDPpsLLILDEPTNHLD 485
Cdd:PRK13539 82 NAMKPALtvaenlefwAAFLggeeLDIAAALEAVGlaplahlpfgYLSAGQKRRVALARLLVSNRP--IWILDEPTAALD 159
|
170 180
....*....|....*....|....*..
gi 14524463 486 IDSIEAVeAGLLSY----DGALVVVSH 508
Cdd:PRK13539 160 AAAVALF-AELIRAhlaqGGIVIAATH 185
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
30-204 |
3.16e-13 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 72.21 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrVALaRQIlragadetiadvfgatqAVAVLRRA------------ 97
Cdd:TIGR03375 492 EKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG-VDI-RQI-----------------DPADLRRNigyvpqdprlfy 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 98 -------EKGDASVEEletadwtveERIVSALARLGLEARADTLLN-----------QLSGGQRTRAVLAAAIFSEPDFL 159
Cdd:TIGR03375 553 gtlrdniALGAPYADD---------EEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPIL 623
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14524463 160 LLDEPTNNLDRDGRRAVIGLLSGWRSGA--IVVSHDRELLEEMDAII 204
Cdd:TIGR03375 624 LLDEPTSAMDNRSEERFKDRLKRWLAGKtlVLVTHRTSLLDLVDRII 670
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
335-508 |
3.70e-13 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 69.34 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGYDpARPIIRDLSFSlVGPR-RVSVTGPNGSGKTSLLKVVTGELPPFKGTVsvnvpFTLLDQ---SVSILE 410
Cdd:COG1119 3 LLELRNVTVRRG-GKTILDDISWT-VKPGeHWAILGPNGAGKSTLLSLITGDLPPTYGND-----VRLFGErrgGEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 411 -----------------RGETILE-----------NFKRLNPGASDNAcRAALASFRFrADAALQRVEALSGGQVLRAGL 462
Cdd:COG1119 76 lrkriglvspalqlrfpRDETVLDvvlsgffdsigLYREPTDEQRERA-RELLELLGL-AHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14524463 463 ACALGGSdpPSLLILDEPTNHLDIDSIEAVEAGL--LSYDG--ALVVVSH 508
Cdd:COG1119 154 ARALVKD--PELLILDEPTAGLDLGARELLLALLdkLAAEGapTLVLVTH 201
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-180 |
3.85e-13 |
|
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: 70.91 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 23 LDLAF---GPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRV-ALARQILRAGADE-TIADVFGATQAVAVLRRA 97
Cdd:TIGR02142 14 LDADFtlpGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlFDSRKGIFLPPEKrRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 98 EKGDASVEELETADWTVEERIVSALarLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVI 177
Cdd:TIGR02142 94 GNLRYGMKRARPSERRISFERVIEL--LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
...
gi 14524463 178 GLL 180
Cdd:TIGR02142 172 PYL 174
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-173 |
3.95e-13 |
|
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: 70.60 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrvalARQILRAGADETIADVF---------GATQAVAVLRRAEKGDASv 104
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG----EDVTNVPPHLRHINMVFqsyalfphmTVEENVAFGLKMRKVPRA- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 105 eeletadwTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR 173
Cdd:TIGR01187 76 --------EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLR 136
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
15-193 |
4.08e-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: 68.75 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFgPER--TGLVGRNGIGKTSVLNIIAGTL-----RPSSGTVAIQGRVALARQILRAGADETIADVFga 87
Cdd:cd03260 11 GDKHALKDISLDI-PKGeiTALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLELRRRVGMVF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 88 tQAVAVLR-------------RAEKGDASVEELetadwtVEErivsALARLGLEARADTLLN--QLSGGQRTRAVLAAAI 152
Cdd:cd03260 88 -QKPNPFPgsiydnvayglrlHGIKLKEELDER------VEE----ALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 153 FSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS--GAIVVSHD 193
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
336-514 |
5.02e-13 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 68.39 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPA-RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV-NVPFTLLDQSV------- 406
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdGTDIRQLDPADlrrnigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 407 ----SILERGeTILENFKRLNPGASDN-----ACRAALASFRFRADAALQ-----RVEALSGGQVLRAGLACALGGSdpP 472
Cdd:cd03245 83 vpqdVTLFYG-TLRDNITLGAPLADDErilraAELAGVTDFVNKHPNGLDlqigeRGRGLSGGQRQAVALARALLND--P 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 14524463 473 SLLILDEPTNHLDIDSIEAVEAGLLSY--DGALVVVSHDETFLA 514
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLD 203
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-192 |
6.07e-13 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 66.68 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVAL---ARQILRAGadetIADVFgatqav 91
Cdd:cd03216 12 GVKALDGVSLSVRRgEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfasPRDARRAG----IAMVY------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 92 avlrraekgdasveeletadwtveerivsalarlglearadtllnQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRD 171
Cdd:cd03216 82 ---------------------------------------------QLSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180
....*....|....*....|....
gi 14524463 172 GRRAVIGLLSGWRS---GAIVVSH 192
Cdd:cd03216 117 EVERLFKVIRRLRAqgvAVIFISH 140
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-206 |
6.19e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-----VALARQILRAGADETIADV------FG 86
Cdd:PRK11629 24 VLHNVSFSIGEgEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklSSAAKAELRNQKLGFIYQFhhllpdFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 87 ATQAVAV------LRRAEkgdasveeletadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLL 160
Cdd:PRK11629 104 ALENVAMplligkKKPAE---------------INSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14524463 161 LDEPTNNLDRDGRRAVIGLLS--GWRSGA--IVVSHDRELLEEMDAIIEL 206
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGelNRLQGTafLVVTHDLQLAKRMSRQLEM 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-215 |
6.76e-13 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 70.84 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEH-VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrvALARQILRAGADETI 81
Cdd:TIGR01842 317 LSVENVTIVPPGGKKpTLRGISFSLQAgEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG--ADLKQWDRETFGKHI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 82 A------DVFGATQAVAVLRRAEKGDAS--VEELETADwtVEERIvsalarLGLEARADTLLNQ----LSGGQRTRAVLA 149
Cdd:TIGR01842 395 GylpqdvELFPGTVAENIARFGENADPEkiIEAAKLAG--VHELI------LRLPDGYDTVIGPggatLSGGQRQRIALA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 150 AAIFSEPDFLLLDEPTNNLDRDGRRAV---IGLLSGWRSGAIVVSHDRELLEEMDAIIELTSLGTKRYG 215
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALanaIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFG 535
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
34-211 |
7.01e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.89 E-value: 7.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVAlarqilragADETIAD-------VF--------GATQAVAVLRRAE 98
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVL---------SEETVWDvrrqvgmVFqnpdnqfvGATVQDDVAFGLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 99 KGDASVEELetadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIG 178
Cdd:PRK13635 109 NIGVPREEM-------VERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14524463 179 LLSGWR--SGAIVVS--HDRELLEEMDAII-----ELTSLGT 211
Cdd:PRK13635 182 TVRQLKeqKGITVLSitHDLDEAAQADRVIvmnkgEILEEGT 223
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
9-180 |
7.10e-13 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 68.48 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 9 LSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAGADE------TI 81
Cdd:TIGR02315 7 LSKVYPNGKQALKNINLNINPgEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGT-----DITKLRGKKlrklrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 82 ADVF---------GATQAVAVLRRAEKG--DASVEELETADwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAA 150
Cdd:TIGR02315 82 GMIFqhynlierlTVLENVLHGRLGYKPtwRSLLGRFSEED---KERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190
....*....|....*....|....*....|
gi 14524463 151 AIFSEPDFLLLDEPTNNLDRDGRRAVIGLL 180
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYL 188
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
336-509 |
7.14e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.50 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTL-----LDQSVSIL 409
Cdd:PRK11231 3 LRTENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdKPISMlssrqLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 410 ERGETILENFK-----------------RLnpGASDNAcRAALASFRFRADA-ALQRVEALSGGQVLRAGLACALGGSDP 471
Cdd:PRK11231 82 PQHHLTPEGITvrelvaygrspwlslwgRL--SAEDNA-RVNQAMEQTRINHlADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 472 psLLILDEPTNHLDIDsiEAVE----AGLLSYDGALVV-VSHD 509
Cdd:PRK11231 159 --VVLLDEPTTYLDIN--HQVElmrlMRELNTQGKTVVtVLHD 197
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-195 |
8.91e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.19 E-value: 8.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPdGEHVFSDLDLAFGPERTGLV-GRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAGADETIa 82
Cdd:PRK11248 2 LQISHLYADYG-GKPALEDINLTLESGELLVVlGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGV- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 83 dVFgatQAVAVLRRAEKGDASVEELETADWTVEERIVSA---LARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFL 159
Cdd:PRK11248 75 -VF---QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAhqmLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14524463 160 LLDEPTNNLDRDGRRAVIG-LLSGWRSGA---IVVSHDRE 195
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTlLLKLWQETGkqvLLITHDIE 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-203 |
8.94e-13 |
|
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: 70.55 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 3 SITLSALSWSKPDGE-HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-------RVALARQI- 72
Cdd:COG4618 330 RLSVENLTVVPPGSKrPILRGVSFSLEPgEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGadlsqwdREELGRHIg 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 73 -------LRAGadeTIADV---FGATQAVAVLRRAEKgdASVEELetadwtveerIvsalarLGLEARADTLL----NQL 138
Cdd:COG4618 410 ylpqdveLFDG---TIAENiarFGDADPEKVVAAAKL--AGVHEM----------I------LRLPDGYDTRIgeggARL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14524463 139 SGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS-GA--IVVSHDRELLEEMDAI 203
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGAtvVVITHRPSLLAAVDKL 536
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-193 |
8.97e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 3 SITLSALSWSKPdGEHVFSDLDLAFGPER-TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRV-------ALARQILR 74
Cdd:PRK10575 11 TFALRNVSFRVP-GRTLLHPLSLTFPAGKvTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 75 AGADETIADVFGATQAVAVLRRAEKGdaSVEELETADwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFS 154
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIGRYPWHG--ALGRFGAAD---REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 155 EPDFLLLDEPTNNLDRDGRRAVIGL---LSGWRS-GAIVVSHD 193
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALvhrLSQERGlTVIAVLHD 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-201 |
9.39e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.73 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSD--LDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-----------RV-------ALARQIlragad 78
Cdd:PRK10851 17 VLNDisLDIPSG-QMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVgfvfqhyALFRHM------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 79 eTIAD--VFGATqavaVLRRAEKGDASVeeletadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEP 156
Cdd:PRK10851 90 -TVFDniAFGLT----VLPRRERPNAAA---------IKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 14524463 157 DFLLLDEPTNNLD----RDGRRAVIGLLSGWRSGAIVVSHDREllEEMD 201
Cdd:PRK10851 156 QILLLDEPFGALDaqvrKELRRWLRQLHEELKFTSVFVTHDQE--EAME 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-192 |
9.55e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.58 E-value: 9.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 3 SITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRagadE 79
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPgETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVdiRDLTLESLR----R 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIADVFgatQAVAVLRR--AE-----KGDASVEELETAdwtveerivSALARL-----GLEARADTLLNQ----LSGGQR 143
Cdd:COG1132 415 QIGVVP---QDTFLFSGtiREnirygRPDATDEEVEEA---------AKAAQAhefieALPDGYDTVVGErgvnLSGGQR 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14524463 144 TRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSG--AIVVSH 192
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH 533
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-169 |
1.03e-12 |
|
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: 68.44 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAGADETIADVFgatQAVA------VLRRAEKGdasve 105
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQdiAAMSRKELRELRRKKISMVF---QSFAllphrtVLENVAFG----- 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 106 eLETADWTVEERI---VSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:cd03294 127 -LEVQGVPRAEREeraAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
16-169 |
1.15e-12 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 67.17 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRAGADETIADVF--------- 85
Cdd:cd03262 12 DFHVLKGIDLTVKKgEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGMVFqqfnlfphl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 86 ----GATQAVAVLRRAEKGDAsveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLL 161
Cdd:cd03262 92 tvleNITLAPIKVKGMSKAEA------------EERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
....*...
gi 14524463 162 DEPTNNLD 169
Cdd:cd03262 160 DEPTSALD 167
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
349-486 |
1.20e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.87 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTV--------------------------SVNVPFTLL 402
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrpladwspaelarrravlpqhsSLSFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 403 DqsvsILERGetilenfkrLNPGASDNACRAALasfrfrADAALQRVE----------ALSGGQVLRAGLACAL----GG 468
Cdd:PRK13548 95 E----VVAMG---------RAPHGLSRAEDDAL------VAAALAQVDlahlagrdypQLSGGEQQRVQLARVLaqlwEP 155
|
170
....*....|....*...
gi 14524463 469 SDPPSLLILDEPTNHLDI 486
Cdd:PRK13548 156 DGPPRWLLLDEPTSALDL 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
350-509 |
1.36e-12 |
|
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: 67.36 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 350 PIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN--VPFTLLDQSVSIL-----ERGETILEnfkrL 422
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglVPWKRRKKFLRRIgvvfgQKTQLWWD----L 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 423 NPGASDNACRA--ALASFRFRAD----AAL--------QRVEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDIDS 488
Cdd:cd03267 111 PVIDSFYLLAAiyDLPPARFKKRldelSELldleelldTPVRQLSLGQRMRAEIAAALLHE--PEILFLDEPTIGLDVVA 188
|
170 180
....*....|....*....|....*
gi 14524463 489 IEAVEAGLLSYD---GALVVV-SHD 509
Cdd:cd03267 189 QENIRNFLKEYNrerGTTVLLtSHY 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
1.45e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.84 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDLDLAFgPE--RTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQI--LRAGADE 79
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSI-PEgsKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIAD----VFGAT--QAVAV------LRRAEkgdasveeletadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAV 147
Cdd:PRK13647 84 VFQDpddqVFSSTvwDDVAFgpvnmgLDKDE---------------VERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 148 LAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW-RSGA--IVVSHDREL-LEEMDAIIELTSLGTKRYGG 216
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKtvIVATHDVDLaAEWADQVIVLKEGRVLAEGD 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
337-509 |
1.49e-12 |
|
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: 67.46 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 337 AFDGVTAgydparpiIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLD------------ 403
Cdd:cd03219 9 RFGGLVA--------LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgEDITGLPpheiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 404 -QSVSILERGeTILEN-----FKRLNPGASDNACRAALASFRFRADAALQRV----------EALSGGQVLRAGLACALG 467
Cdd:cd03219 81 fQIPRLFPEL-TVLENvmvaaQARTGSGLLLARARREEREARERAEELLERVgladladrpaGELSYGQQRRLEIARALA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14524463 468 GSdpPSLLILDEPT---NHLDIDSIEAVEAGLLSYDGALVVVSHD 509
Cdd:cd03219 160 TD--PKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHD 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-206 |
1.69e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 69.75 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 6 LSALSWSKPDGEH---VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGT--VAIQGRVALARQILRAGADE 79
Cdd:PRK10535 7 LKDIRRSYPSGEEqveVLKGISLDIYAgEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrVAGQDVATLDADALAQLRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIADVFGATQAVAVLRRAEKGDASVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFL 159
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14524463 160 LLDEPTNNLDRDGRRAVIGLLSGWRS---GAIVVSHDRELLEEMDAIIEL 206
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQVAAQAERVIEI 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
349-509 |
1.99e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.06 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVPFTL--LDQSVSILERGETILENFKRLNPGA 426
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIgyVPQKLYLDTTLPLTVNRFLRLRPGT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 427 SDNACRAALAsfRFRA----DAALQRveaLSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDI-------DSIEAVEAG 495
Cdd:PRK09544 97 KKEDILPALK--RVQAghliDAPMQK---LSGGETQRVLLARALLNR--PQLLVLDEPTQGVDVngqvalyDLIDQLRRE 169
|
170
....*....|....
gi 14524463 496 LlsyDGALVVVSHD 509
Cdd:PRK09544 170 L---DCAVLMVSHD 180
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-202 |
2.06e-12 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 66.80 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--------VALARQILRAGADETIaDVFGA-----TQAVAVLRR 96
Cdd:TIGR03771 7 ELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAspgkgwrhIGYVPQRHEFAWDFPI-SVAHTvmsgrTGHIGWLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 97 AEKgdasveeletADWTVeerIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAV 176
Cdd:TIGR03771 86 PCV----------ADFAA---VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152
|
170 180
....*....|....*....|....*....
gi 14524463 177 IGL---LSGWRSGAIVVSHDreLLEEMDA 202
Cdd:TIGR03771 153 TELfieLAGAGTAILMTTHD--LAQAMAT 179
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
349-518 |
2.36e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvpftlldqSVSILERGE--------------- 413
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ--------GEPIRRQRDeyhqdllylghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 414 ----TILEN---FKRLNPGASDNACRAALASF--RFRADAAlqrVEALSGGQVLRAGLAcALGGSDPPsLLILDEPTNHL 484
Cdd:PRK13538 86 ktelTALENlrfYQRLHGPGDDEALWEALAQVglAGFEDVP---VRQLSAGQQRRVALA-RLWLTRAP-LWILDEPFTAI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 14524463 485 DIDSIEAVEAGL---LSYDGALVVVSHDETFLANIGI 518
Cdd:PRK13538 161 DKQGVARLEALLaqhAEQGGMVILTTHQDLPVASDKV 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-516 |
2.39e-12 |
|
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: 69.16 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGYDP-ARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPfKGTVSVNVPFTLLD-QSVSILERG 412
Cdd:COG1123 4 LLEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPH-GGRISGEVLLDGRDlLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 413 ETILENFKrlNPGASDN----------ACRAALASF---RFRADAALQRVE----------ALSGGQVLRAGLACALggS 469
Cdd:COG1123 83 RRIGMVFQ--DPMTQLNpvtvgdqiaeALENLGLSRaeaRARVLELLEAVGlerrldryphQLSGGQRQRVAIAMAL--A 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14524463 470 DPPSLLILDEPTNHLDIDSIEAVEAGLLS----YDGALVVVSHDETFLANI 516
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRElqreRGTTVLLITHDLGVVAEI 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-204 |
2.53e-12 |
|
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: 70.04 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 13 KPDGEHVFSDLDLAFGPER-TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-----VALARQILRAGADETIAdVFG 86
Cdd:TIGR01257 939 EPSGRPAVDRLNITFYENQiTAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnLDAVRQSLGMCPQHNIL-FHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 87 ATQAVAVLRRAEKGDASVEELETadwtveeRIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTN 166
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAQL-------EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 167 NLDRDGRRAVIGLLSGWRSGAIVV--SH---DRELLEEMDAII 204
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIImsTHhmdEADLLGDRIAII 1133
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-228 |
2.58e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.15 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTV--AIQGRVALARQILRA--GADETIADVFGATq 89
Cdd:PRK15064 330 DNGPLFKNLNLLLEAgERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQDHAYdfENDLTLFDWMSQW- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 90 avavlrRAEKGDasveeletadwtvEERIVSALARLglearadtLLNQ---------LSGGQRTRAVLAAAIFSEPDFLL 160
Cdd:PRK15064 409 ------RQEGDD-------------EQAVRGTLGRL--------LFSQddikksvkvLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 161 LDEPTNNLDRDGRRAVIGLLSGWRSGAIVVSHDRELLEEMDA-IIELTSLGTKRYGGGWSAYQAARAVE 228
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATrIIEITPDGVVDFSGTYEEYLRSQGIE 530
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
349-485 |
2.61e-12 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 66.37 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSlVGPRRV-SVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVPFTLLD-----QSVSI------LERGETIL 416
Cdd:cd03263 15 KPAVDDLSLN-VYKGEIfGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDrkaarQSLGYcpqfdaLFDELTVR 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14524463 417 EN------FKRLNPGASDNACRAALASFRFRaDAALQRVEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLD 485
Cdd:cd03263 94 EHlrfyarLKGLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGG--PSVLLLDEPTSGLD 165
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
9-196 |
2.72e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.41 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 9 LSWSKPDGEHVFSDLDL-AFGPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--------VALARQ---ILRAG 76
Cdd:PRK13639 7 LKYSYPDGTEALKGINFkAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksLLEVRKtvgIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 77 ADETIadvFGATQAVAVLRRAEKGDASVEEletadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEP 156
Cdd:PRK13639 87 PDDQL---FAPTVEEDVAFGPLNLGLSKEE-------VEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 157 DFLLLDEPTNNLDRDGRRAVIGLLSGW-RSG-AIVVS-HDREL 196
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLnKEGiTIIIStHDVDL 199
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
355-496 |
3.38e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.72 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 355 LSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELpPFKGTVSVN-VPFTLLD------------QSVSILErgETILENFKR 421
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINgIELRELDpeswrkhlswvgQNPQLPH--GTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 422 LNPGASDNACRAALAsfrfRADAA--LQRVEA------------LSGGQVLRAGLACALGGsdPPSLLILDEPTNHLDID 487
Cdd:PRK11174 446 GNPDASDEQLQQALE----NAWVSefLPLLPQgldtpigdqaagLSVGQAQRLALARALLQ--PCQLLLLDEPTASLDAH 519
|
....*....
gi 14524463 488 SIEAVEAGL 496
Cdd:PRK11174 520 SEQLVMQAL 528
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-204 |
3.39e-12 |
|
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: 65.03 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGE-HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQilragadETI 81
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQgEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-------KAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 82 ADVFGA-TQAVAVLrraekgdasveeletadwtveerivsalarlglearADTLLN----QLSGGQRTRAVLAAAIFSEP 156
Cdd:cd03247 74 SSLISVlNQRPYLF------------------------------------DTTLRNnlgrRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14524463 157 DFLLLDEPTNNLDRDGRRAVIGLL-SGWRSGAIV-VSHDRELLEEMDAII 204
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIfEVLKDKTLIwITHHLTGIEHMDKIL 167
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
335-509 |
3.61e-12 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 65.99 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGYDP---ARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN--------------- 396
Cdd:cd03257 1 LLEVKNLSVSFPTgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 397 ------V---PFTLLDQSVSIlerGETILENFKRLNPGASDNACRAALASFRFRADAALQRVEA----LSGGQVLRAGLA 463
Cdd:cd03257 81 rkeiqmVfqdPMSSLNPRMTI---GEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRypheLSGGQRQRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 14524463 464 CALGGSdpPSLLILDEPTNHLDIDsieaVEAGLL--------SYDGALVVVSHD 509
Cdd:cd03257 158 RALALN--PKLLIADEPTSALDVS----VQAQILdllkklqeELGLTLLFITHD 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
336-485 |
3.68e-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: 65.76 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPARpIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLDQS-VSIL--ER 411
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgKPLDIAARNrIGYLpeER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 412 G----ETILEN------FKRLNPGASDNACRAALASFRFRaDAALQRVEALSGGQVLRAGLACALggSDPPSLLILDEPT 481
Cdd:cd03269 80 GlypkMKVIDQlvylaqLKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAV--IHDPELLILDEPF 156
|
....
gi 14524463 482 NHLD 485
Cdd:cd03269 157 SGLD 160
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-198 |
3.96e-12 |
|
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: 66.75 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAgADETIADVF-GATQAVAVL 94
Cdd:TIGR02769 26 VLTNVSLSIEEgETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlYQLDRKQRRA-FRRDVQLVFqDSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 95 RRAEKGDAS-VEELETADWTVEERIVSALARL-GLEAR-ADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRD 171
Cdd:TIGR02769 105 MTVRQIIGEpLRHLTSLDESEQKARIAELLDMvGLRSEdADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190
....*....|....*....|....*....|.
gi 14524463 172 GRRAVIGLLSGWRS----GAIVVSHDRELLE 198
Cdd:TIGR02769 185 LQAVILELLRKLQQafgtAYLFITHDLRLVQ 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-169 |
4.00e-12 |
|
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: 66.17 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDLDLAF-GPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-------VALARQIlra 75
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIaKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdpVELRRKI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 76 gadetiadvfG-ATQAVAVL--RRAEKGDASVEELEtaDW---TVEERIVSALARLGLEAR--ADTLLNQLSGGQRTRAV 147
Cdd:cd03295 78 ----------GyVIQQIGLFphMTVEENIALVPKLL--KWpkeKIRERADELLALVGLDPAefADRYPHELSGGQQQRVG 145
|
170 180
....*....|....*....|..
gi 14524463 148 LAAAIFSEPDFLLLDEPTNNLD 169
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALD 167
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-193 |
4.39e-12 |
|
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: 66.28 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-RVALARQILRAGADETIADVFgatqavavlrrAEKGDASveeLE 108
Cdd:cd03237 26 EVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLL-----------SSITKDF---YT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 109 TADWTVEerivsALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR----RAVIGLLSGWR 184
Cdd:cd03237 92 HPYFKTE-----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFAENNE 166
|
....*....
gi 14524463 185 SGAIVVSHD 193
Cdd:cd03237 167 KTAFVVEHD 175
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
349-513 |
4.40e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 68.73 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLK----------------------VVTGELPPFKGTVSVNVPFT-LLDQS 405
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhaidgipkncqilhveqeVVGDDTTALQCVLNTDIERTqLLEEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 406 VSILER--------------------------GETILENFKRLNPGASDNA-CRAA--LASFRFRADAALQRVEALSGGQ 456
Cdd:PLN03073 270 AQLVAQqrelefetetgkgkgankdgvdkdavSQRLEEIYKRLELIDAYTAeARAAsiLAGLSFTPEMQVKATKTFSGGW 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 457 VLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAVEAGLLSYDGALVVVSHDETFL 513
Cdd:PLN03073 350 RMRIALARAL--FIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFL 404
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
338-498 |
5.61e-12 |
|
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: 65.32 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------VPFTLLDQSVSI--- 408
Cdd:cd03254 5 FENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDgidirdISRKSLRSMIGVvlq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 ---LERGeTILENFKRLNPGASD----NACRAA-LASF-RFRAD----AALQRVEALSGGQ-----VLRAGLAcalggsd 470
Cdd:cd03254 85 dtfLFSG-TIMENIRLGRPNATDeeviEAAKEAgAHDFiMKLPNgydtVLGENGGNLSQGErqllaIARAMLR------- 156
|
170 180
....*....|....*....|....*...
gi 14524463 471 PPSLLILDEPTNHLDIDSIEAVEAGLLS 498
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEK 184
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-165 |
5.93e-12 |
|
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: 65.39 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvALAR----QILRAGadetIA------DVFg 86
Cdd:COG0410 17 HVLHGVSLEVEEgEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGE-DITGlpphRIARLG----IGyvpegrRIF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 87 atqavavlrraekGDASVEE-LETADWTV--EERIVSALARLG-----LEARADTLLNQLSGGQRTRAVLAAAIFSEPDF 158
Cdd:COG0410 91 -------------PSLTVEEnLLLGAYARrdRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
....*..
gi 14524463 159 LLLDEPT 165
Cdd:COG0410 158 LLLDEPS 164
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-173 |
6.67e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.37 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSWSKPDGEHVFSDlDLAFGPERT---GLVGRNGIGKTSVLNIIAGTLRPSSGTVA-----IQGRVALARQi 72
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVD-GLSFHVQRGecfGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepVPSRARHARQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 73 lRAGA----DETIADvFGATQAVAVLRRAEKGDASveeletadwTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVL 148
Cdd:PRK13537 81 -RVGVvpqfDNLDPD-FTVRENLLVFGRYFGLSAA---------AARALVPPLLEFAKLENKADAKVGELSGGMKRRLTL 149
|
170 180
....*....|....*....|....*
gi 14524463 149 AAAIFSEPDFLLLDEPTNNLDRDGR 173
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQAR 174
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-206 |
9.78e-12 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 64.80 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 12 SKPDgEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-------------VALARQ--ILRA 75
Cdd:cd03248 23 TRPD-TLVLQDVSFTLHPgEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQepVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 76 GA-DETIADVFGATQAVAVLRRAEKGDAS--VEELETADWTveerivsalarlgleaRADTLLNQLSGGQRTRAVLAAAI 152
Cdd:cd03248 102 RSlQDNIAYGLQSCSFECVKEAAQKAHAHsfISELASGYDT----------------EVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 153 FSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW--RSGAIVVSHDRELLEEMDAIIEL 206
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVERADQILVL 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-195 |
1.19e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.45 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG------RVALARQILRAGA----------DETIA-DV-FGATQav 91
Cdd:PRK13637 34 EFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkKVKLSDIRKKVGLvfqypeyqlfEETIEkDIaFGPIN-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 92 avlrraekgdasveeLETADWTVEERIVSALARLGL--EARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK13637 112 ---------------LGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190
....*....|....*....|....*....|
gi 14524463 170 RDGRRAVIGLLSG----WRSGAIVVSHDRE 195
Cdd:PRK13637 177 PKGRDEILNKIKElhkeYNMTIILVSHSME 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-169 |
1.21e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.51 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSWSKpDGEHVFSDLDLA-FGPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRV-----ALARQIlr 74
Cdd:PRK09452 12 SPLVELRGISKSF-DGKEVISNLDLTiNNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithvpAENRHV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 75 agadETI---------ADVFgatQAVAVLRRAEKgdasVEELEtadwtVEERIVSALARLGLEARADTLLNQLSGGQRTR 145
Cdd:PRK09452 89 ----NTVfqsyalfphMTVF---ENVAFGLRMQK----TPAAE-----ITPRVMEALRMVQLEEFAQRKPHQLSGGQQQR 152
|
170 180
....*....|....*....|....
gi 14524463 146 AVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
336-517 |
1.26e-11 |
|
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: 63.36 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYdPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLDQSVSILERGET 414
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgEDLTDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 415 ILENFKRLNPGAS--DNacraalasfrfradaalqRVEALSGGQVLRAGLACALGgSDPPsLLILDEPTNHLD---IDSI 489
Cdd:cd03229 80 MVFQDFALFPHLTvlEN------------------IALGLSGGQQQRVALARALA-MDPD-VLLLDEPTSALDpitRREV 139
|
170 180
....*....|....*....|....*....
gi 14524463 490 EAVEAGLLSYDG-ALVVVSHDETFLANIG 517
Cdd:cd03229 140 RALLKSLQAQLGiTVVLVTHDLDEAARLA 168
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
349-514 |
1.31e-11 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 64.84 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVS---VNVP----------FTLLDQSVS-------- 407
Cdd:TIGR03873 14 RLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagVDLHglsrrararrVALVEQDSDtavpltvr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 408 -ILERGETILENFKRLNPGASDNACRAALASFRFrADAALQRVEALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDI 486
Cdd:TIGR03873 94 dVVALGRIPHRSLWAGDSPHDAAVVDRALARTEL-SHLADRDMSTLSGGERQRVHVARAL--AQEPKLLLLDEPTNHLDV 170
|
170 180 190
....*....|....*....|....*....|.
gi 14524463 487 DSIEAVEAGL--LSYDGALVVVS-HDETFLA 514
Cdd:TIGR03873 171 RAQLETLALVreLAATGVTVVAAlHDLNLAA 201
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-204 |
1.56e-11 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 66.66 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 14 PDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrVALA--------RQILRAGA-----DE 79
Cdd:TIGR02203 342 GRDRPALDSISLVIEPgETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG-HDLAdytlaslrRQVALVSQdvvlfND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIADvfgatqAVAVLRRAEKGDASVEELETADWTVEerIVSALArLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFL 159
Cdd:TIGR02203 421 TIAN------NIAYGRTEQADRAEIERALAAAYAQD--FVDKLP-LGLDTPIGENGVLLSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 14524463 160 LLDEPTNNLDRDGRRAVIGLLSGWRSG--AIVVSHDRELLEEMDAII 204
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLMQGrtTLVIAHRLSTIEKADRIV 538
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
367-523 |
2.03e-11 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 63.40 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 367 VTGPNGSGKTSLLKVV----TGELPP------------FKGTVS--VNVPFTLLDQSVSILERGETILENFKRLNPGASD 428
Cdd:cd03240 27 IVGQNGAGKTTIIEALkyalTGELPPnskggahdpkliREGEVRaqVKLAFENANGKKYTITRSLAILENVIFCHQGESN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 429 nacraalasfrfraDAALQRVEALSGGQ------VLRAGLACALGGSDPPslLILDEPTNHLDIDSI-----EAVEAGLL 497
Cdd:cd03240 107 --------------WPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGI--LALDEPTTNLDEENIeeslaEIIEERKS 170
|
170 180
....*....|....*....|....*.
gi 14524463 498 SYDGALVVVSHDETFLANIGIGTRVE 523
Cdd:cd03240 171 QKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
335-509 |
3.19e-11 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 63.52 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAgydparpiIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVsvnvpfTLLDQSVS------I 408
Cdd:COG0411 11 TKRFGGLVA--------VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRI------LFDGRDITglpphrI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 LERG-------------ETILEN-----FKRLNPGASDNAC-----RAALASFRFRADAALQRVE----------ALSGG 455
Cdd:COG0411 77 ARLGiartfqnprlfpeLTVLENvlvaaHARLGRGLLAALLrlpraRREEREARERAEELLERVGladradepagNLSYG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14524463 456 QVLRAGLACALGGSdpPSLLILDEPT---NHLDIDSIEAVEAGLLSYDG-ALVVVSHD 509
Cdd:COG0411 157 QQRRLEIARALATE--PKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHD 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-169 |
3.22e-11 |
|
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: 63.06 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPS---SGTVAIQG----------RVALARQilragaDETIADVFGATQAV---AVLR 95
Cdd:cd03234 36 MAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGqprkpdqfqkCVAYVRQ------DDILLPGLTVRETLtytAILR 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14524463 96 RAEKGDASVEELETADwtveerivSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:cd03234 110 LPRKSSDAIRKKRVED--------VLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
338-515 |
3.72e-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: 62.81 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFT-LLDQSVSILERG-ET 414
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgQDVSdLRGRAIPYLRRKiGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 415 ILENFKRL-NPGASDNACRAALAS------FRFRADAALQRV----------EALSGGQVLRAGLACALGGSdpPSLLIL 477
Cdd:cd03292 83 VFQDFRLLpDRNVYENVAFALEVTgvppreIRKRVPAALELVglshkhralpAELSGGEQQRVAIARAIVNS--PTILIA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14524463 478 DEPTNHLDIDSIEAVEAGLLSYD--GALVVVS-HDETFLAN 515
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVDT 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-173 |
4.42e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.47 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSWSKPDGEH-VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-----RVALARQil 73
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKaVVNGLSFTVASgECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpaRARLARA-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 74 RAGAD---ETIADVFGATQAVAVLRRAEKGDASveeletadwTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAA 150
Cdd:PRK13536 115 RIGVVpqfDNLDLEFTVRENLLVFGRYFGMSTR---------EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLAR 185
|
170 180
....*....|....*....|...
gi 14524463 151 AIFSEPDFLLLDEPTNNLDRDGR 173
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHAR 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-181 |
4.43e-11 |
|
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: 62.57 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARqilrAGADETIADVFGATQAVAVLRRAEKGD 101
Cdd:TIGR01277 18 DLNVADG-EIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL----APYQRPVSMLFQENNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 102 ASVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLS 181
Cdd:TIGR01277 93 LGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
336-485 |
4.60e-11 |
|
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: 62.49 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGY---DPARPIIRDLSFSlVGPRR-VSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN--------VPFTLLD 403
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLS-VEEGEfVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgepvtgpgPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 404 QSVSILE-RgeTILEN--FKRLNPGASDNACRAalasfrfRADAALQRVE----------ALSGGQVLRAGLACALGGSd 470
Cdd:cd03293 80 QQDALLPwL--TVLDNvaLGLELQGVPKAEARE-------RAEELLELVGlsgfenayphQLSGGMRQRVALARALAVD- 149
|
170
....*....|....*
gi 14524463 471 pPSLLILDEPTNHLD 485
Cdd:cd03293 150 -PDVLLLDEPFSALD 163
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
34-193 |
5.22e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.60 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQI--LRagadETIADVF--------GATQAVAVLRRAEKGDAS 103
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdIR----HKIGMVFqnpdnqfvGATVEDDVAFGLENKGIP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 104 VEELEtadwtveERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW 183
Cdd:PRK13650 114 HEEMK-------ERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGI 186
|
170
....*....|....
gi 14524463 184 RSG----AIVVSHD 193
Cdd:PRK13650 187 RDDyqmtVISITHD 200
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-169 |
5.71e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.09 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQilraGADE 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKGIDLDVADgEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE----PADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIADVFgatQAVAV---------------LRRAEKGDasveeletadwtVEERIVSALARLGLEARADTLLNQLSGGQRT 144
Cdd:PRK11650 77 DIAMVF---QNYALyphmsvrenmayglkIRGMPKAE------------IEERVAEAARILELEPLLDRKPRELSGGQRQ 141
|
170 180
....*....|....*....|....*
gi 14524463 145 RAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-169 |
5.77e-11 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 63.92 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRP---SSGTVAIQGR--VALARQILRA--GADetIADVF--------- 85
Cdd:COG0444 25 SFDVRRG-ETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEdlLKLSEKELRKirGRE--IQMIFqdpmtslnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 86 ----GaTQAVAVLRRAEKGDASveeletadwTVEERIVSALARLGL---EARADTLLNQLSGGQRTRAVLAAAIFSEPDF 158
Cdd:COG0444 102 vmtvG-DQIAEPLRIHGGLSKA---------EARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKL 171
|
170
....*....|.
gi 14524463 159 LLLDEPTNNLD 169
Cdd:COG0444 172 LIADEPTTALD 182
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
336-509 |
5.82e-11 |
|
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: 62.15 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPARpIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvpftllDQSVSIL--ERGE 413
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID------GRDVTGVppERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 414 --------------TILEN----FKRLNPGASDNACRAALASFRFRADAALQR-VEALSGGQVLRAGLACALGGSdpPSL 474
Cdd:cd03259 74 igmvfqdyalfphlTVAENiafgLKLRGVPKAEIRARVRELLELVGLEGLLNRyPHELSGGQQQRVALARALARE--PSL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 14524463 475 LILDEPTNHLDIDSIEAVEAGLLSYDGAL----VVVSHD 509
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELgittIYVTHD 190
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-198 |
9.21e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.40 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAgADETIADVF-GATQAV--- 91
Cdd:PRK10419 27 VLNNVSLSLKSgETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplAKLNRAQRKA-FRRDIQMVFqDSISAVnpr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 92 ----AVLRRAEKGDASVEELETadwtvEERIVSALARLGLEAR-ADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTN 166
Cdd:PRK10419 106 ktvrEIIREPLRHLLSLDKAER-----LARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 14524463 167 NLDRDGRRAVIGLLSGWR----SGAIVVSHDRELLE 198
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQqqfgTACLFITHDLRLVE 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
336-508 |
1.03e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 61.86 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPA-RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------VPFTLLDQSVSI 408
Cdd:cd03251 1 VEFKNVTFRYPGDgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvrdYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 LER-----GETILENFKRLNPGASD----NACRAALA-SFRFRADAALQ-----RVEALSGGQVLRAGLACALGgSDPPs 473
Cdd:cd03251 81 VSQdvflfNDTVAENIAYGRPGATReeveEAARAANAhEFIMELPEGYDtvigeRGVKLSGGQRQRIAIARALL-KDPP- 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 14524463 474 LLILDEPTNHLDIDSIEAVEAGL--LSYDGALVVVSH 508
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALerLMKNRTTFVIAH 195
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-507 |
1.05e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.82 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAgydparpiIRDLSFSLvgpRRVSVT---GPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLD-QSVSIL--E 410
Cdd:COG4152 11 FGDKTA--------VDDVSFTV---PKGEIFgllGPNGAGKTTTIRIILGILAPDSGEVLWDgEPLDPEDrRRIGYLpeE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 411 RG----ETILEN---FKRLNpGASDNACRAALASF--RFR-ADAALQRVEALSGGQVLRAGLACALGGSdpPSLLILDEP 480
Cdd:COG4152 80 RGlypkMKVGEQlvyLARLK-GLSKAEAKRRADEWleRLGlGDRANKKVEELSKGNQQKVQLIAALLHD--PELLILDEP 156
|
170 180
....*....|....*....|....*....
gi 14524463 481 TNHLDIDSIEAVEAGLLSY--DGALVVVS 507
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELaaKGTTVIFS 185
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
335-527 |
1.17e-10 |
|
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: 61.92 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGYDPaRPIIRDLSFSLvgPR--RVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVnvpftlLDQSVSILERG 412
Cdd:COG1127 5 MIEVRNLTKSFGD-RVVLDGVSLDV--PRgeILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV------DGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 413 E---------------------TILEN-------FKRLNPGASDNACRAALASFRFRaDAALQRVEALSGGQVLRAGLAC 464
Cdd:COG1127 76 ElyelrrrigmlfqggalfdslTVFENvafplreHTDLSEAEIRELVLEKLELVGLP-GAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 465 ALgGSDPPsLLILDEPTNHLD-IDSIEAVEagLL-----SYDGALVVVSHDET----------FLAN---IGIGTRVELS 525
Cdd:COG1127 155 AL-ALDPE-ILLYDEPTAGLDpITSAVIDE--LIrelrdELGLTSVVVTHDLDsafaiadrvaVLADgkiIAEGTPEELL 230
|
..
gi 14524463 526 TS 527
Cdd:COG1127 231 AS 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-197 |
1.34e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSDLDLAFGPERT-GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG--RVALARQILRagadetiadvFGATQAVAVLR 95
Cdd:PRK09544 19 VLSDVSLELKPGKIlTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQKLY----------LDTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 96 --RAEKGdasveeLETADwtveerIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR 173
Cdd:PRK09544 89 flRLRPG------TKKED------ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|....*...
gi 14524463 174 RAVIGLLSGWRS----GAIVVSHDRELL 197
Cdd:PRK09544 157 VALYDLIDQLRReldcAVLMVSHDLHLV 184
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-492 |
1.56e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.51 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-VALA--RQILRAGadetI---------ADVFGATQ 89
Cdd:COG3845 25 SLTVRPG-EIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpVRIRspRDAIALG----IgmvhqhfmlVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 90 AVAVLRraEKGDASVEELETAdwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:COG3845 100 NIVLGL--EPTKGGRLDRKAA----RARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 170 RDGRRAVIGLLSGWRSG--AIV-VSHDrelLEEmdaIIELtslgtkrygggwsayqaaraveleaaqqsltlarktADEV 246
Cdd:COG3845 174 PQEADELFEILRRLAAEgkSIIfITHK---LRE---VMAI------------------------------------ADRV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 247 D--RKARaLAERLDKRDASgtrkaaKGDMPRILVGRrksnaeesrgkSVELAERRRAGaldavtaakarievlqpfsirl 324
Cdd:COG3845 212 TvlRRGK-VVGTVDTAETS------EEELAELMVGR-----------EVLLRVEKAPA---------------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 325 prtelPAGRQVLAFDGVTAGYDPARPIIRDLSFSLvgpRR---VSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFT 400
Cdd:COG3845 252 -----EPGEVVLEVENLSVRDDRGVPALKDVSLEV---RAgeiLGIAGVAGNGQSELAEALAGLRPPASGSIRLDgEDIT 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 401 LLDQSvSILERG-----E-----------TILEN----------FKR---LNPGASDNACRAALASFRFRADAALQRVEA 451
Cdd:COG3845 324 GLSPR-ERRRLGvayipEdrlgrglvpdmSVAENlilgryrrppFSRggfLDRKAIRAFAEELIEEFDVRTPGPDTPARS 402
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 14524463 452 LSGGQVLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAV 492
Cdd:COG3845 403 LSGGNQQKVILAREL--SRDPKLLIAAQPTRGLDVGAIEFI 441
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
19-193 |
1.83e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.70 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSDLDLAFgPER--TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQIL-----------RAGADETIAD 83
Cdd:PRK11831 22 IFDNISLTV-PRGkiTAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEniPAMSRSRLytvrkrmsmlfQSGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 84 VFgatQAVAVLRRaekgdasvEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDE 163
Cdd:PRK11831 101 VF---DNVAYPLR--------EHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190
....*....|....*....|....*....|....
gi 14524463 164 PTNNLDRDGRRAVIGLLSGWRSG----AIVVSHD 193
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELNSAlgvtCVVVSHD 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
15-195 |
1.98e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.55 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLA-FGPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-VALARQILRA--------------GAD 78
Cdd:PRK11607 30 DGQHAVDDVSLTiYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdLSHVPPYQRPinmmfqsyalfphmTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 79 ETIAdvFGATQAVavLRRAEkgdasveeletadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDF 158
Cdd:PRK11607 110 QNIA--FGLKQDK--LPKAE---------------IASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 159 LLLDEPTNNLDRDGRR----AVIGLLSgwRSGA--IVVSHDRE 195
Cdd:PRK11607 171 LLLDEPMGALDKKLRDrmqlEVVDILE--RVGVtcVMVTHDQE 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-180 |
2.13e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 62.02 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALS---WSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAgA 77
Cdd:COG1135 2 IELENLSktfPTKGGPVTALDDVSLTIEKgEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVdlTALSERELRA-A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 78 DETIADVFgatQAVAVLRRAekgdaSVEE-----LETADWT---VEERIVSALARLGLEARADTLLNQLSGGQRTRAVLA 149
Cdd:COG1135 81 RRKIGMIF---QHFNLLSSR-----TVAEnvalpLEIAGVPkaeIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190
....*....|....*....|....*....|.
gi 14524463 150 AAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL 180
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLL 183
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
335-481 |
2.29e-10 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 60.77 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGYDPArPIIRDLSFSlVGPRR-VSVTGPNGSGKTSLLKVVTGELPPFKGTVsvnvpfTLLDQSVS------ 407
Cdd:COG0410 3 MLEVENLHAGYGGI-HVLHGVSLE-VEEGEiVALLGRNGAGKTTLLKAISGLLPPRSGSI------RFDGEDITglpphr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 408 ILERG-----E--------TILENfkrLNPGAsdnACRAALASFRFRADAAL-----------QRVEALSGG--QVLraG 461
Cdd:COG0410 75 IARLGigyvpEgrrifpslTVEEN---LLLGA---YARRDRAEVRADLERVYelfprlkerrrQRAGTLSGGeqQML--A 146
|
170 180
....*....|....*....|
gi 14524463 462 LACALGGSdpPSLLILDEPT 481
Cdd:COG0410 147 IGRALMSR--PKLLLLDEPS 164
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
21-207 |
2.36e-10 |
|
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: 60.31 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 21 SDLDLAFGPERTGLVGRNGIGKTSVLNIIA----GTLRPSSGtvaiqgRVALARQILRAGadETIADV---F-GATQAVA 92
Cdd:cd03240 14 ERSEIEFFSPLTLIVGQNGAGKTTIIEALKyaltGELPPNSK------GGAHDPKLIREG--EVRAQVklaFeNANGKKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 93 VLRRaekgdaSVEELETADWTVEERIVSALARLglearadtlLNQLSGGQRT------RAVLAAAIFSEPDFLLLDEPTN 166
Cdd:cd03240 86 TITR------SLAILENVIFCHQGESNWPLLDM---------RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTT 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14524463 167 NLDRDGRR-AVIGLLSGWRSGA----IVVSHDRELLEEMDAIIELT 207
Cdd:cd03240 151 NLDEENIEeSLAEIIEERKSQKnfqlIVITHDEELVDAADHIYRVE 196
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
15-165 |
2.44e-10 |
|
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: 60.62 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAGADEtiadvfgatqavav 93
Cdd:TIGR03410 11 GQSHILRGVSLEVPKgEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGE-----DITKLPPHE-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 94 lrRAEKGDASVEELET--ADWTVEERIvsalaRLGLEARAD-----------------TLLNQ----LSGGQRTRAVLAA 150
Cdd:TIGR03410 72 --RARAGIAYVPQGREifPRLTVEENL-----LTGLAALPRrsrkipdeiyelfpvlkEMLGRrggdLSGGQQQQLAIAR 144
|
170
....*....|....*
gi 14524463 151 AIFSEPDFLLLDEPT 165
Cdd:TIGR03410 145 ALVTRPKLLLLDEPT 159
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
301-515 |
2.76e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.92 E-value: 2.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 301 AGA---LDAVTAAKARIE--VLQPFSIRLPRTELPAGRQV-LAFDGVTAGY-DPARPIIRDLSFSLVGPRRVSVTGPNGS 373
Cdd:PRK11160 298 AGAfqhLGQVIASARRINeiTEQKPEVTFPTTSTAAADQVsLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGC 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 374 GKTSLLKVVTGELPPFKGTVSVN-VP------------FTLLDQSVSILerGETILENFKRLNPGASDNACRaalasfrf 440
Cdd:PRK11160 378 GKSTLLQLLTRAWDPQQGEILLNgQPiadyseaalrqaISVVSQRVHLF--SATLRDNLLLAAPNASDEALI-------- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 441 radAALQRVE--------------------ALSGGQVLRAGLACALgGSDPPsLLILDEPTNHLDIDSIEAVEAGLLSY- 499
Cdd:PRK11160 448 ---EVLQQVGleklleddkglnawlgeggrQLSGGEQRRLGIARAL-LHDAP-LLLLDEPTEGLDAETERQILELLAEHa 522
|
250
....*....|....*..
gi 14524463 500 -DGALVVVSHDETFLAN 515
Cdd:PRK11160 523 qNKTVLMITHRLTGLEQ 539
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-207 |
3.48e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 60.32 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 14 PDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR----VALA---RQILRAGAD-----ET 80
Cdd:cd03251 12 GDGPPVLRDISLDIPAgETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdYTLAslrRQIGLVSQDvflfnDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 81 IAD-----VFGATQAvAVLRRAEKGDAS--VEELETA-DWTVEERIVsalarlglearadtllnQLSGGQRTRAVLAAAI 152
Cdd:cd03251 92 VAEniaygRPGATRE-EVEEAARAANAHefIMELPEGyDTVIGERGV-----------------KLSGGQRQRIAIARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14524463 153 FSEPDFLLLDEPTNNLDRDGRRAV---IGLLSGWRSgAIVVSHDRELLEEMDAIIELT 207
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVqaaLERLMKNRT-TFVIAHRLSTIENADRIVVLE 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
34-195 |
4.26e-10 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 60.04 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTvaiqgrvalarqILRAGADET--------IADVFgatQAVA------VLRRAEK 99
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDSGK------------ILLNGKDITnlppekrdISYVP---QNYAlfphmtVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 100 GdasVEELETADWTVEERIVSALARLGLearaDTLLNQ----LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRA 175
Cdd:cd03299 95 G---LKKRKVDKKEIERKVLEIAEMLGI----DHLLNRkpetLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180
....*....|....*....|....
gi 14524463 176 VIGLLSGWRSG----AIVVSHDRE 195
Cdd:cd03299 168 LREELKKIRKEfgvtVLHVTHDFE 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
333-485 |
4.61e-10 |
|
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: 59.10 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 333 RQVLAFDGVTAGYDP-----ARPIIRDLSFSlVGPRR-VSVTGPNGSGKTSLLKVVTGELPP--FKGTVSVN-VPFTLLD 403
Cdd:cd03213 1 GVTLSFRNLTVTVKSspsksGKQLLKNVSGK-AKPGElTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINgRPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 404 -QSVSILERGETILenFKRLNPgasdnacRAALasfRFraDAALQRveaLSGGQVLRAGLACALGGSdpPSLLILDEPTN 482
Cdd:cd03213 80 fRKIIGYVPQDDIL--HPTLTV-------RETL---MF--AAKLRG---LSGGERKRVSIALELVSN--PSLLFLDEPTS 140
|
...
gi 14524463 483 HLD 485
Cdd:cd03213 141 GLD 143
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-181 |
4.72e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.97 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 18 HVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAgADETIADVFgatQAVAVL 94
Cdd:PRK11153 19 HALNNVSLHIPAgEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdlTALSEKELRK-ARRQIGMIF---QHFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 95 rraekgdAS--VEE-----LETADWT---VEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEP 164
Cdd:PRK11153 95 -------SSrtVFDnvalpLELAGTPkaeIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170
....*....|....*..
gi 14524463 165 TNNLDRDGRRAVIGLLS 181
Cdd:PRK11153 168 TSALDPATTRSILELLK 184
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-198 |
5.04e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.50 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG----RVA------LARQI------LRAGAD 78
Cdd:PRK10908 14 GRQALQGVTFHMRPgEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditRLKnrevpfLRRQIgmifqdHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 79 ETIADVFGATQAVAvlrraekgDASVEEletadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDF 158
Cdd:PRK10908 94 RTVYDNVAIPLIIA--------GASGDD-------IRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 159 LLLDEPTNNLDRDGRRAVIGLLSGW-RSGAIVV--SHDRELLE 198
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFnRVGVTVLmaTHDIGLIS 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
338-485 |
6.53e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 60.61 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV---NVPFTLLDQSVSI------ 408
Cdd:PRK13536 44 LAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvPVPARARLARARIgvvpqf 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 --LERGETILEN------FKRLNPGASDNACRAAL--ASFRFRADAalqRVEALSGGQVLRAGLACALggSDPPSLLILD 478
Cdd:PRK13536 123 dnLDLEFTVRENllvfgrYFGMSTREIEAVIPSLLefARLESKADA---RVSDLSGGMKRRLTLARAL--INDPQLLILD 197
|
....*..
gi 14524463 479 EPTNHLD 485
Cdd:PRK13536 198 EPTTGLD 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-200 |
7.33e-10 |
|
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: 61.95 E-value: 7.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 33 GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAGAD-----------ETIADVFGATQAVAVLRRAeKGD 101
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK-----SILTNISDvhqnmgycpqfDAIDDLLTGREHLYLYARL-RGV 2042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 102 ASVEELETADWTVEErivsalarLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRR----AVI 177
Cdd:TIGR01257 2043 PAEEIEKVANWSIQS--------LGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRmlwnTIV 2114
|
170 180
....*....|....*....|...
gi 14524463 178 GLLSGWRSgAIVVSHDRELLEEM 200
Cdd:TIGR01257 2115 SIIREGRA-VVLTSHSMEECEAL 2136
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
15-169 |
7.42e-10 |
|
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: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALA--RQILRAGADetIADVFgatQA- 90
Cdd:COG1126 12 GDLEVLKGISLDVEKgEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskKDINKLRRK--VGMVF---QQf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 91 ----------------VAVLRRAeKGDAsveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFS 154
Cdd:COG1126 87 nlfphltvlenvtlapIKVKKMS-KAEA------------EERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170
....*....|....*
gi 14524463 155 EPDFLLLDEPTNNLD 169
Cdd:COG1126 154 EPKVMLFDEPTSALD 168
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
32-202 |
7.49e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 59.76 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvALARQILRAgADETIADVF--------GATQAVAVLRRAEKGDAS 103
Cdd:PRK13648 38 TSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ-AITDDNFEK-LRKHIGIVFqnpdnqfvGSIVKYDVAFGLENHAVP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 104 VEELEtadwtveERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW 183
Cdd:PRK13648 116 YDEMH-------RRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKV 188
|
170 180
....*....|....*....|...
gi 14524463 184 RSGA----IVVSHDreLLEEMDA 202
Cdd:PRK13648 189 KSEHnitiISITHD--LSEAMEA 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
338-509 |
8.12e-10 |
|
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: 59.05 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLDQSVSILERGE--- 413
Cdd:cd03261 3 LRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgEDISGLSEAELYRLRRRmgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 414 -----------TILEN-------FKRLNPGASDNACRAALASFRFRaDAALQRVEALSGGQVLRAGLACALgGSDPPsLL 475
Cdd:cd03261 82 lfqsgalfdslTVFENvafplreHTRLSEEEIREIVLEKLEAVGLR-GAEDLYPAELSGGMKKRVALARAL-ALDPE-LL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 14524463 476 ILDEPTNHLDIDSIEAVEAGLLSYDGAL----VVVSHD 509
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHD 196
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
336-481 |
8.78e-10 |
|
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: 58.98 E-value: 8.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPArPIIRDLSFSlVGPRR-VSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvpftllDQSVS------I 408
Cdd:cd03224 1 LEVENLNAGYGKS-QILFGVSLT-VPEGEiVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD------GRDITglppheR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 LERG-----E--------TILENFK----RLNPGASDNACRAALASFRFRADAALQRVEALSGGQvlRAGLACALGGSDP 471
Cdd:cd03224 73 ARAGigyvpEgrrifpelTVEENLLlgayARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGE--QQMLAIARALMSR 150
|
170
....*....|
gi 14524463 472 PSLLILDEPT 481
Cdd:cd03224 151 PKLLLLDEPS 160
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-177 |
1.21e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.95 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALA-----RQI-LRAG-------------AD 78
Cdd:PRK09493 16 VLHNIDLNIDQgEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvdeRLIrQEAGmvfqqfylfphltAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 79 ETIAdvFGATQavavLRRAEKGDAsveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDF 158
Cdd:PRK09493 96 ENVM--FGPLR----VRGASKEEA------------EKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170
....*....|....*....
gi 14524463 159 LLLDEPTNNLDRDGRRAVI 177
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVL 176
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-190 |
1.45e-09 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 57.56 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPS--SGTVAIQGR----VALARQILRAG 76
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPgELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRpldkRSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 77 ADetiaDVFGATQavavlrraekgdasveeletadwTVEERI-VSALarlglearadtlLNQLSGGQRTRAVLAAAIFSE 155
Cdd:cd03213 89 QD----DILHPTL-----------------------TVRETLmFAAK------------LRGLSGGERKRVSIALELVSN 129
|
170 180 190
....*....|....*....|....*....|....*
gi 14524463 156 PDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGAIVV 190
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTI 164
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-203 |
1.47e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 60.63 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLrPSSGTVAIQGrVALaRQILRAGADETIADV------FGAT--QAVAvLRRAEKGD 101
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLGFL-PYQGSLKING-IEL-RELDPESWRKHLSWVgqnpqlPHGTlrDNVL-LGNPDASD 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 102 ASVEE-LETADwtVEErIVSALArLGLearaDTLLNQ----LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAV 176
Cdd:PRK11174 453 EQLQQaLENAW--VSE-FLPLLP-QGL----DTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180
....*....|....*....|....*....
gi 14524463 177 I-GLLSGWRS-GAIVVSHDRELLEEMDAI 203
Cdd:PRK11174 525 MqALNAASRRqTTLMVTHQLEDLAQWDQI 553
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
32-181 |
1.51e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAGADEtIADVFGATQAVAVlrraEKGDASVEELET-- 109
Cdd:PRK10253 36 TAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE-----HIQHYASKE-VARRIGLLAQNAT----TPGDITVQELVArg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 110 --------ADWTVE--ERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGL 179
Cdd:PRK10253 106 ryphqplfTRWRKEdeEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
..
gi 14524463 180 LS 181
Cdd:PRK10253 186 LS 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-169 |
1.75e-09 |
|
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: 60.08 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGpERTGLVGRNGIGKT----SVLNIIAGTLRPSSGTVAIQGR--VALARQILRA--GADetIADVF-------- 85
Cdd:COG4172 30 SFDIAAG-ETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQdlLGLSERELRRirGNR--IAMIFqepmtsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 86 -----GAtQAVAVLR--RAEKGDASveeletadwtvEERIVSALARLGL---EARADTLLNQLSGGQRTRAVLAAAIFSE 155
Cdd:COG4172 107 plhtiGK-QIAEVLRlhRGLSGAAA-----------RARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANE 174
|
170
....*....|....
gi 14524463 156 PDFLLLDEPTNNLD 169
Cdd:COG4172 175 PDLLIADEPTTALD 188
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-206 |
1.80e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.12 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 3 SITLSALSWSKPDGEHVFSDLDLAFgPER--TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAGA- 77
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSV-PSRgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRplSSLSHSVLRQGVa 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 78 ----DETI-ADVFGATqaVAVLRraekgDASveelETADWTVEERI-VSALARL---GLEARADTLLNQLSGGQRTRAVL 148
Cdd:PRK10790 419 mvqqDPVVlADTFLAN--VTLGR-----DIS----EEQVWQALETVqLAELARSlpdGLYTPLGEQGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 149 AAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA--IVVSHDRELLEEMDAIIEL 206
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTtlVVIAHRLSTIVEADTILVL 547
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
336-485 |
1.99e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.17 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYdPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV-------------------- 395
Cdd:PRK11248 2 LQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpvegpgaergvvfqneg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 396 ---------NVPFTLLDQSVSILERGETILENFKRLNpgasdnacraaLASFRFRadaalqRVEALSGGQVLRAGLACAL 466
Cdd:PRK11248 81 llpwrnvqdNVAFGLQLAGVEKMQRLEIAHQMLKKVG-----------LEGAEKR------YIWQLSGGQRQRVGIARAL 143
|
170
....*....|....*....
gi 14524463 467 GGSdpPSLLILDEPTNHLD 485
Cdd:PRK11248 144 AAN--PQLLLLDEPFGALD 160
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-206 |
2.03e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 57.88 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 13 KPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrVALArqilragadeTIADVFGATQAV 91
Cdd:cd03252 11 KPDGPVILDNISLRIKPgEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG-HDLA----------LADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 92 AVLRRAEKGDASV-EELETADWTVEERIVSALARLG--------LEARADTLLNQ----LSGGQRTRAVLAAAIFSEPDF 158
Cdd:cd03252 80 VVLQENVLFNRSIrDNIALADPGMSMERVIEAAKLAgahdfiseLPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 14524463 159 LLLDEPTNNLDRDGRRAVIGLLSGWRSG--AIVVSHDRELLEEMDAIIEL 206
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAHRLSTVKNADRIIVM 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-516 |
2.08e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGT--LRPSSGTVAIqgRVALARQILRAGADETI---------- 81
Cdd:TIGR03269 11 DGKEVLKNISFTIEEgEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIY--HVALCEKCGYVERPSKVgepcpvcggt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 82 -----ADVFGATQAV--AVLRR---------AEKGDASV-----EELETADWTVEE---RIVSALARLGLEARADTLLNQ 137
Cdd:TIGR03269 89 lepeeVDFWNLSDKLrrRIRKRiaimlqrtfALYGDDTVldnvlEALEEIGYEGKEavgRAVDLIEMVQLSHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 138 LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDG----RRAVIGLLSGWRSGAIVVSHDRELLEEMdaiieltslgtkr 213
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWPEVIEDL------------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 214 ygggwsayqAARAVELEAAQqslTLARKTADEVDRKARALAERLDKRdasgtrkaakgdmprilvgrrksnaeesrgKSV 293
Cdd:TIGR03269 236 ---------SDKAIWLENGE---IKEEGTPDEVVAVFMEGVSEVEKE------------------------------CEV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 294 ELAErrragalDAVtaakaRIEVLQPFSIRLPRTelpagrQVLAFDGVtagydparpiirdlSFSLVGPRRVSVTGPNGS 373
Cdd:TIGR03269 274 EVGE-------PII-----KVRNVSKRYISVDRG------VVKAVDNV--------------SLEVKEGEIFGIVGTSGA 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 374 GKTSLLKVVTGELPPFKGTVSVNVPFTLLDQS-VSILERGE------------------TILENF-KRLNPGASDN-ACR 432
Cdd:TIGR03269 322 GKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTkPGPDGRGRakryigilhqeydlyphrTVLDNLtEAIGLELPDElARM 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 433 AA---LASFRFRADAALQRVE----ALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAVEAGLL----SYDG 501
Cdd:TIGR03269 402 KAvitLKMVGFDEEKAEEILDkypdELSEGERHRVALAQVL--IKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQ 479
|
570
....*....|....*
gi 14524463 502 ALVVVSHDETFLANI 516
Cdd:TIGR03269 480 TFIIVSHDMDFVLDV 494
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
34-169 |
2.60e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPS---SGTVAIQGRVALARQILRAGADETIADVFGATQAV-------AVLRRAEKGDAS 103
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVrehlmfqAHLRMPRRVTKK 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14524463 104 VEEletadwtveERIVSALARLGLEARADTLLNQ------LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:TIGR00955 136 EKR---------ERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
346-485 |
2.68e-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: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 346 DPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPP---FKGTVSVN-VPFT--LLDQSVSILERGETILENF 419
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNgQPRKpdQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 420 ----------KRLNPGASDNACRAALASFRFRADAALQRV-----EALSGGQVLRAGLACALggSDPPSLLILDEPTNHL 484
Cdd:cd03234 97 tvretltytaILRLPRKSSDAIRKKRVEDVLLRDLALTRIggnlvKGISGGERRRVSIAVQL--LWDPKVLILDEPTSGL 174
|
.
gi 14524463 485 D 485
Cdd:cd03234 175 D 175
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
34-205 |
4.97e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.53 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-----------------RVALARQILRAgadetiaDVFGATqavaVLRR 96
Cdd:PRK13641 38 LVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFPEA-------QLFENT----VLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 97 AEKGDASveeLETADWTVEERIVSALARLGL-EARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRA 175
Cdd:PRK13641 107 VEFGPKN---FGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190
....*....|....*....|....*....|...
gi 14524463 176 VIGLLSGW-RSG--AIVVSHDrelleeMDAIIE 205
Cdd:PRK13641 184 MMQLFKDYqKAGhtVILVTHN------MDDVAE 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
333-509 |
5.70e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 57.33 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 333 RQVLAFDGVTAGY-DPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvPFTLLDQSVSILER 411
Cdd:PRK13635 3 EEIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-GMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 412 --------------GETILEN--FKRLNPGASdnacRAALASfrfRADAALQRV----------EALSGGQVLRAGLACA 465
Cdd:PRK13635 82 qvgmvfqnpdnqfvGATVQDDvaFGLENIGVP----REEMVE---RVDQALRQVgmedflnrepHRLSGGQKQRVAIAGV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14524463 466 LGGSdpPSLLILDEPTNHLD-IDSIEAVEA-GLLSYDGALVVVS--HD 509
Cdd:PRK13635 155 LALQ--PDIIILDEATSMLDpRGRREVLETvRQLKEQKGITVLSitHD 200
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
329-485 |
5.76e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.51 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 329 LPAGRQVLAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------------ 396
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCgepvpsrarhar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 397 -----VP-FTLLDQSVSILERgetiLENFKRLNpGASDNACRAAL------ASFRFRADAalqRVEALSGGQVLRAGLAC 464
Cdd:PRK13537 80 qrvgvVPqFDNLDPDFTVREN----LLVFGRYF-GLSAAAARALVppllefAKLENKADA---KVGELSGGMKRRLTLAR 151
|
170 180
....*....|....*....|.
gi 14524463 465 ALggSDPPSLLILDEPTNHLD 485
Cdd:PRK13537 152 AL--VNDPDVLVLDEPTTGLD 170
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-257 |
7.16e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALA-----RQILraGADETIADVFG-ATQAVAVLRRaekgdas 103
Cdd:PRK11147 346 DKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAyfdqhRAEL--DPEKTVMDNLAeGKQEVMVNGR------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 104 veeletadwtvEERIVSALAR-LGLEARADTLLNQLSGGQRTRAVLAAaIFSEPDFLL-LDEPTNNLDRDGRRAVIGLLS 181
Cdd:PRK11147 417 -----------PRHVLGYLQDfLFHPKRAMTPVKALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEELLD 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 182 GWRSGAIVVSHDRELLE---------EMDAIIEltslgtkRYGGGWSAYQAARA----VELEAAQQSLTLARKTADEVDR 248
Cdd:PRK11147 485 SYQGTVLLVSHDRQFVDntvtecwifEGNGKIG-------RYVGGYHDARQQQAqylaLKQPAVKKKEEAAAPKAETVKR 557
|
....*....
gi 14524463 249 KARALAERL 257
Cdd:PRK11147 558 SSKKLSYKL 566
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-509 |
8.13e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.18 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 19 VFSDLDLAFGPERT-GLVGRNGIGKT-SVLNIIagTLRPSSGTVAIQGRVALARQILRAGADETIADVFGATQA------ 90
Cdd:PRK15134 24 VVNDVSLQIEAGETlALVGESGSGKSvTALSIL--RLLPSPPVVYPSGDIRFHGESLLHASEQTLRGVRGNKIAmifqep 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 91 ----------------VAVLRRAEKGDASVEEletadwtveerIVSALARLGLEARADTLLN---QLSGGQRTRAVLAAA 151
Cdd:PRK15134 102 mvslnplhtlekqlyeVLSLHRGMRREAARGE-----------ILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 152 IFSEPDFLLLDEPTNNLDRDGRRAVIGLLsgwrsgaivvshdRELLEEMD-AIIELTslgtkrygggwsayqaaravele 230
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLL-------------RELQQELNmGLLFIT----------------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 231 aaqQSLTLARKTADEVD--RKARALAERldkrdasgtRKAAKGDMPRILVGRRKSNAEESrGKSVELAERrragaldavT 308
Cdd:PRK15134 215 ---HNLSIVRKLADRVAvmQNGRCVEQN---------RAATLFSAPTHPYTQKLLNSEPS-GDPVPLPEP---------A 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 309 AAKARIEVLQ-PFSIRlprtelpagRQVLAfdgVTAGYDPArpiIRDLSFSLVGPRRVSVTGPNGSGKTS----LLKVVT 383
Cdd:PRK15134 273 SPLLDVEQLQvAFPIR---------KGILK---RTVDHNVV---VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 384 GE-----------------LPPFKGTVSV--NVPFTLLDQSVSILERGETILE-NFKRLNPGASDNACRAALASFRFRAD 443
Cdd:PRK15134 338 SQgeiwfdgqplhnlnrrqLLPVRHRIQVvfQDPNSSLNPRLNVLQIIEEGLRvHQPTLSAAQREQQVIAVMEEVGLDPE 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14524463 444 AALQRVEALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDidsiEAVEAGLLS--------YDGALVVVSHD 509
Cdd:PRK15134 418 TRHRYPAEFSGGQRQRIAIARAL--ILKPSLIILDEPTSSLD----KTVQAQILAllkslqqkHQLAYLFISHD 485
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-181 |
8.75e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.13 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIqgrvalarqilrAGADETIADVfgATQAVAVLRRaekgd 101
Cdd:PRK10771 19 DLTVERG-ERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL------------NGQDHTTTPP--SRRPVSMLFQ----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 102 asvEELETADWTVEERI-----------------VSALA-RLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDE 163
Cdd:PRK10771 79 ---ENNLFSHLTVAQNIglglnpglklnaaqrekLHAIArQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDE 155
|
170
....*....|....*...
gi 14524463 164 PTNNLDRDGRRAVIGLLS 181
Cdd:PRK10771 156 PFSALDPALRQEMLTLVS 173
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-208 |
8.76e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 58.21 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 3 SITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVA--LARQILRAGADE 79
Cdd:TIGR01193 473 DIVINDVSYSYGYGSNILSDISLTIKMnSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLkdIDRHTLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TIAD--VFGATQAVAVLRRAEKGdASVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPD 157
Cdd:TIGR01193 553 LPQEpyIFSGSILENLLLGAKEN-VSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14524463 158 FLLLDEPTNNLDRDGRRAVI-GLLSGWRSGAIVVSHDRELLEEMDAIIELTS 208
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVnNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDH 683
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-169 |
1.07e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.13 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSWSKPDGEH-VFSDLDL-AFGPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-VALAR------- 70
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHeVLKGVSLqANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtINLVRdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 71 -------QILRAGAdETIADVFGATQAVAVLRRAEKGDASVEELETADwtVEERIVSALARLGLEARA-DTLLNQLSGGQ 142
Cdd:PRK10619 81 vadknqlRLLRTRL-TMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQE--ARERAVKYLAKVGIDERAqGKYPVHLSGGQ 157
|
170 180
....*....|....*....|....*..
gi 14524463 143 RTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALD 184
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
325-396 |
1.12e-08 |
|
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: 55.62 E-value: 1.12e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14524463 325 PRTELPAGRQVLAFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN 396
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
34-193 |
1.30e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.71 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLrPSSGTVAIQGR-------VALARQilRAGADETIADVFgatqAVAV-----LRRAEKGD 101
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQpleawsaAELARH--RAYLSQQQTPPF----AMPVfqyltLHQPDKTR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 102 ASVEEletadwTVEERIVSalaRLGLEARADTLLNQLSGG--QRTRavLAAAIF-----SEPD--FLLLDEPTNNLDRDG 172
Cdd:PRK03695 100 TEAVA------SALNEVAE---ALGLDDKLGRSVNQLSGGewQRVR--LAAVVLqvwpdINPAgqLLLLDEPMNSLDVAQ 168
|
170 180
....*....|....*....|....
gi 14524463 173 RRAVIGLLSGW-RSG-AIVVS-HD 193
Cdd:PRK03695 169 QAALDRLLSELcQQGiAVVMSsHD 192
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-206 |
1.40e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.96 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDlDLAFGPER---TGLVGRNGIGKTSVLNIIAGTLRP---SSGTVAIQGRVALARQI--LRa 75
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALN-DISFSIPRgswTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVwdIR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 76 gadETIADVF--------GATQAVAVLRRAEKGDASVEELEtadwtveeRIVS-ALARLGLEARADTLLNQLSGGQRTRA 146
Cdd:PRK13640 84 ---EKVGIVFqnpdnqfvGATVGDDVAFGLENRAVPRPEMI--------KIVRdVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14524463 147 VLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS----GAIVVSHDRELLEEMDAIIEL 206
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHDIDEANMADQVLVL 216
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
114-169 |
1.75e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 55.58 E-value: 1.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 114 VEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:COG4598 131 AIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-192 |
1.81e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 55.24 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 12 SKPDGEhVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIagtLR---PSSGTVAIQG-------------RVALARQ--I 72
Cdd:cd03249 12 SRPDVP-ILKGLSLTIPPgKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGvdirdlnlrwlrsQIGLVSQepV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 73 LRAGadeTIAD--VFGatqavavlrraeKGDASVEEletadwtVEERIVSALAR---LGLEARADTLL----NQLSGGQR 143
Cdd:cd03249 88 LFDG---TIAEniRYG------------KPDATDEE-------VEEAAKKANIHdfiMSLPDGYDTLVgergSQLSGGQK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 14524463 144 TRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSG--AIVVSH 192
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH 196
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
116-169 |
1.87e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 55.40 E-value: 1.87e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 14524463 116 ERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:COG4161 120 EKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-169 |
1.94e-08 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 55.89 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarQILRAGADE---------------------- 79
Cdd:COG4608 38 SFDIRRG-ETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ-----DITGLSGRElrplrrrmqmvfqdpyaslnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 -TIADVFGATQAVAvlrraekGDASVEELEtadwtveERIVSALARLGLEAR-ADTLLNQLSGGQRTRAVLAAAIFSEPD 157
Cdd:COG4608 112 mTVGDIIAEPLRIH-------GLASKAERR-------ERVAELLELVGLRPEhADRYPHEFSGGQRQRIGIARALALNPK 177
|
170
....*....|..
gi 14524463 158 FLLLDEPTNNLD 169
Cdd:COG4608 178 LIVCDEPVSALD 189
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
336-513 |
2.56e-08 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 54.01 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPAR----PIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVPFTLLDQSVSILer 411
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 412 GETILEN---FKRLNPGASDNACRA-ALasfrfRADaaLQRVEA------------LSGGQVLRAGLACAL-GGSDppsL 474
Cdd:cd03250 79 NGTIRENilfGKPFDEERYEKVIKAcAL-----EPD--LEILPDgdlteigekginLSGGQKQRISLARAVySDAD---I 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 14524463 475 LILDEPTNHLDIDS----IEAVEAGLLSYDGALVVVSHDETFL 513
Cdd:cd03250 149 YLLDDPLSAVDAHVgrhiFENCILGLLLNNKTRILVTHQLQLL 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
350-487 |
2.65e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.00 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 350 PIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN---------------VPFTLLDQSVSILERGET 414
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraasrrVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 415 ILE-----NFKRLNPGASDNacRAALASFRFRADAAL---QRVEALSGGQVLRAGLACALGGSDPpsLLILDEPTNHLDI 486
Cdd:PRK09536 97 VVEmgrtpHRSRFDTWTETD--RAAVERAMERTGVAQfadRPVTSLSGGERQRVLLARALAQATP--VLLLDEPTASLDI 172
|
.
gi 14524463 487 D 487
Cdd:PRK09536 173 N 173
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-169 |
2.74e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 55.25 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQ---ILRAGADETIadVFGAT----QAVAVLRrAEKGDA 102
Cdd:cd03291 64 EMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQfswIMPGTIKENI--IFGVSydeyRYKSVVK-ACQLEE 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 103 SVEELETADWTVeerivsaLARLGLearadtllnQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:cd03291 141 DITKFPEKDNTV-------LGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-198 |
2.80e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 54.07 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGPERT-GLVGRNGIGKTSVLNIIAG--TLRPSSGTVAIQGrvalarqilragadETIADVfgatqav 91
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVhALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKG--------------EDITDL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 92 avlrraekgdasveeletadwTVEERivsalARLGL--------EARADTLLNQL-------SGGQRTRAVLAAAIFSEP 156
Cdd:cd03217 70 ---------------------PPEER-----ARLGIflafqyppEIPGVKNADFLryvnegfSGGEKKRNEILQLLLLEP 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14524463 157 DFLLLDEPTNNLDRDGRRAVIGLLSGWRS---GAIVVSHDRELLE 198
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLD 168
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
32-190 |
3.08e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.14 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPSSGTV-----------------AIQGRVALARQILRAGA-DETI-ADVFGATQAVA 92
Cdd:PRK13649 36 TAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitstsknkdikQIRKKVGLVFQFPESQLfEETVlKDVAFGPQNFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 93 VlrraekgdaSVEELEtadwtveerivsALAR--LGLEARADTLLNQ----LSGGQRTRAVLAAAIFSEPDFLLLDEPTN 166
Cdd:PRK13649 116 V---------SQEEAE------------ALARekLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180
....*....|....*....|....*
gi 14524463 167 NLDRDGRRAVIGLLSGW-RSGAIVV 190
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLhQSGMTIV 199
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
122-169 |
3.51e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 3.51e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 14524463 122 LARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK11124 126 LERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
338-508 |
3.62e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 54.01 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYD--PARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTL-----LDQSVSIL 409
Cdd:cd03248 14 FQNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgKPISQyehkyLHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 410 ER-----GETILENFKRLNPGASDNACRAalASFRFRADAALQRVEA------------LSGGQVLRAGLACALggSDPP 472
Cdd:cd03248 94 GQepvlfARSLQDNIAYGLQSCSFECVKE--AAQKAHAHSFISELASgydtevgekgsqLSGGQKQRVAIARAL--IRNP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14524463 473 SLLILDEPTNHLDIDSIEAVEAGLlsYDG----ALVVVSH 508
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQAL--YDWperrTVLVIAH 207
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-184 |
3.79e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.89 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG---RVALaRQILRAGADET----------IADV--FGATQAVAVLRRAE 98
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLASGKISILGqptRQAL-QKNLVAYVPQSeevdwsfpvlVEDVvmMGRYGHMGWLRRAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 99 KGDasveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIG 178
Cdd:PRK15056 117 KRD-------------RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIIS 183
|
....*.
gi 14524463 179 LLSGWR 184
Cdd:PRK15056 184 LLRELR 189
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-207 |
3.87e-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: 56.49 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 5 TLSALSWSKPDGEHVfsdldlafgpertGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQ---ILRAGADETI 81
Cdd:TIGR00957 653 TLNGITFSIPEGALV-------------AVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQqawIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 82 adVFG----------ATQAVAVLrraekgdASVEELETADWT-VEERIVSalarlglearadtllnqLSGGQRTRAVLAA 150
Cdd:TIGR00957 720 --LFGkalnekyyqqVLEACALL-------PDLEILPSGDRTeIGEKGVN-----------------LSGGQKQRVSLAR 773
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14524463 151 AIFSEPDFLLLDEPTNNLDRDGRRAVI-------GLLSGwrSGAIVVSHDRELLEEMDAIIELT 207
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDAHVGKHIFehvigpeGVLKN--KTRILVTHGISYLPQVDVIIVMS 835
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-225 |
4.05e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.46 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 24 DLAFGPERTGLV---GRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQI--LRAGadeTIAD--VFGATQAVAVLRR 96
Cdd:TIGR01271 444 NISFKLEKGQLLavaGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTswIMPG---TIKDniIFGLSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 97 AEKGdASVEEletaDWTV-EERIVSALARLGLearadtllnQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDG--- 172
Cdd:TIGR01271 521 VIKA-CQLEE----DIALfPEKDKTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeke 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 14524463 173 --RRAVIGLLSGwrSGAIVVSHDRELLEEMDAIIELTSlGTKRYGGGWSAYQAAR 225
Cdd:TIGR01271 587 ifESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHE-GVCYFYGTFSELQAKR 638
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
35-193 |
4.52e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 35 VGRNGIGKTSVLNIIAGTLRPSSGTVaIQGRVALARqilragADETIADVFGAtqavAVLRRAEKGDASVEELETADWtv 114
Cdd:PRK11247 44 VGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAE------AREDTRLMFQD----ARLLPWKKVIDNVGLGLKGQW-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 115 EERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSG-WRS---GAIVV 190
Cdd:PRK11247 111 RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlWQQhgfTVLLV 190
|
...
gi 14524463 191 SHD 193
Cdd:PRK11247 191 THD 193
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-169 |
5.86e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.99 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSwSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTV-----------AIQGRVAL 68
Cdd:PRK11264 1 MSAIEVKNLV-KKFHGQTVLHGIDLEVKPgEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarSLSQQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 69 ARQiLRagadETIADVFGATQAV---AVLRRAEKGDASVEELETADwtVEERIVSALARLGLEARADTLLNQLSGGQRTR 145
Cdd:PRK11264 80 IRQ-LR----QHVGFVFQNFNLFphrTVLENIIEGPVIVKGEPKEE--ATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180
....*....|....*....|....
gi 14524463 146 AVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALD 176
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-206 |
6.06e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.65 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 1 MPSITLSALSwsKPDGEHVFS---DLDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalaRQILRAGA 77
Cdd:PRK11000 1 MASVTLRNVT--KAYGDVVISkdiNLDIHEG-EFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK----RMNDVPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 78 DETIADVFgatQAVAV---LRRAEKGD-----ASVEELEtadwtVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLA 149
Cdd:PRK11000 74 ERGVGMVF---QSYALyphLSVAENMSfglklAGAKKEE-----INQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14524463 150 AAIFSEPDFLLLDEPTNNLD---RDGRRAVIGLL-SGWRSGAIVVSHDRelLEEM---DAIIEL 206
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDaalRVQMRIEISRLhKRLGRTMIYVTHDQ--VEAMtlaDKIVVL 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
115-180 |
6.29e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.08 E-value: 6.29e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 115 EERIVSALARLGLEAraDTLL---NQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL 180
Cdd:COG4172 402 RARVAEALEEVGLDP--AARHrypHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLL 468
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
349-508 |
6.98e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 52.91 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGeLPPFKGTvsvnvpftlldqSVSILERGETILEnfkrLNPGAsd 428
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKYEVT------------EGEILFKGEDITD----LPPEE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 429 nacRAALASF-RFRADAALQRV----------EALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAVEAG-- 495
Cdd:cd03217 74 ---RARLGIFlAFQYPPEIPGVknadflryvnEGFSGGEKKRNEILQLL--LLEPDLAILDEPDSGLDIDALRLVAEVin 148
|
170
....*....|....
gi 14524463 496 -LLSYDGALVVVSH 508
Cdd:cd03217 149 kLREEGKSVLIITH 162
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-193 |
8.95e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.27 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRAGADETIADVFgatQAVAVLRRAEKGDASVEELETAD 111
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiAKISDAELREVRRKKIAMVF---QSFALMPHMTVLDNTAFGMELAG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 112 WTVEER---IVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD----RDGRRAVIGLLSGWR 184
Cdd:PRK10070 136 INAEERrekALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQ 215
|
....*....
gi 14524463 185 SGAIVVSHD 193
Cdd:PRK10070 216 RTIVFISHD 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
338-509 |
9.01e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.68 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYDPARPI----IRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV----------NVPFTLLD 403
Cdd:PRK13641 5 FENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetgNKNLKKLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 404 QSVSILER-------GETILEN--FKRLNPGASDNACR-AALASFR---FRADAALQRVEALSGGQVLRAGLACALggSD 470
Cdd:PRK13641 85 KKVSLVFQfpeaqlfENTVLKDveFGPKNFGFSEDEAKeKALKWLKkvgLSEDLISKSPFELSGGQMRRVAIAGVM--AY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 14524463 471 PPSLLILDEPTNHLDIDSIEAVEAGLLSYDGA---LVVVSHD 509
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHN 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
30-177 |
9.11e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.55 E-value: 9.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-------RVALARQilRAGAdetiadVFGA--TQAVAVLrraekg 100
Cdd:PRK13633 37 EFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeeNLWDIRN--KAGM------VFQNpdNQIVATI------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 101 dasVEE--------LETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDG 172
Cdd:PRK13633 103 ---VEEdvafgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
....*
gi 14524463 173 RRAVI 177
Cdd:PRK13633 180 RREVV 184
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
339-486 |
9.56e-08 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 52.76 E-value: 9.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 339 DGVTAGYDPARPII---RDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------VPFT------LLD 403
Cdd:cd03266 5 DALTKRFRDVKKTVqavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvkEPAEarrrlgFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 404 QSVSILER--GETILENFKRLNPGASDNACRAA--LASFRFRADAALQRVEALSGGQVLRAGLACALgGSDPPsLLILDE 479
Cdd:cd03266 85 DSTGLYDRltARENLEYFAGLYGLKGDELTARLeeLADRLGMEELLDRRVGGFSTGMRQKVAIARAL-VHDPP-VLLLDE 162
|
....*..
gi 14524463 480 PTNHLDI 486
Cdd:cd03266 163 PTTGLDV 169
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
17-207 |
1.05e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.59 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 17 EHVFSDLDLAFGPER-TGLVGRNGIGKTSVLniiagtlrpssgtvaiqgrvalaRQILragadetiadvFGATQAVAVLR 95
Cdd:cd03227 8 PSYFVPNDVTFGEGSlTIITGPNGSGKSTIL-----------------------DAIG-----------LALGGAQSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 96 RAEKGDAsveeletadwtveeRIVSALARLGLEaradTLLNQLSGGQRTRAVLAAAI----FSEPDFLLLDEPTNNLD-R 170
Cdd:cd03227 54 RRSGVKA--------------GCIVAAVSAELI----FTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDpR 115
|
170 180 190
....*....|....*....|....*....|....*....
gi 14524463 171 DGRRA--VIGLLSGWRSGAIVVSHDRELLEEMDAIIELT 207
Cdd:cd03227 116 DGQALaeAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-196 |
1.10e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 15 DGEHVFSDLDLAFGPER-TGLVGRNGIGKTSVLNIIAGTLRPS--SGTVAIQGRVALARQILRAGADETIADV------- 84
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRvTALLGRNGAGKSTLLKALAGDLTGGgaPRGARVTGDVTLNGEPLAAIDAPRLARLravlpqa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 85 ------FGATQAVAV-----LRRAekGDASVEELETADwtveerivSALARLGLEARADTLLNQLSGGQRTRAVLAAAI- 152
Cdd:PRK13547 92 aqpafaFSAREIVLLgryphARRA--GALTHRDGEIAW--------QALALAGATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 153 --------FSEPDFLLLDEPTNNLDRDGRR----AVIGLLSGWRSGAIVVSHDREL 196
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHrlldTVRRLARDWNLGVLAIVHDPNL 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
348-485 |
1.15e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.79 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 348 ARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPP------FKGTVSVNVPFTLLDQSVSILER-----GETIL 416
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPtsgtllFEGEDISTLKPEIYRQQVSYCAQtptlfGDTVY 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 417 ENFK---RLNPGASD-NACRAALASFRFRADAALQRVEALSGGQVLRAGLACALggSDPPSLLILDEPTNHLD 485
Cdd:PRK10247 99 DNLIfpwQIRNQQPDpAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNL--QFMPKVLLLDEITSALD 169
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-220 |
1.26e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 17 EHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTL--RPSSGTVAIQGrvalarqiLRAGADETIADVFGA----TQ 89
Cdd:COG2401 43 RYVLRDLNLEIEPgEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD--------NQFGREASLIDAIGRkgdfKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 90 AVAVLRRAEKGDAsveeletadwtveeriVSALARLglearadtllNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:COG2401 115 AVELLNAVGLSDA----------------VLWLRRF----------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 170 RD-GRRAVIGLLSGWRSGAI---VVSHDRELLEEM--DAIIeltslgTKRYGGGWSA 220
Cdd:COG2401 169 RQtAKRVARNLQKLARRAGItlvVATHHYDVIDDLqpDLLI------FVGYGGVPEE 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
350-510 |
1.28e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 350 PIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVPFTLLDQSVSILErgETILEN------FKRLN 423
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMP--GTIKDNiifglsYDEYR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 424 PGASDNACRAA--LASFRFRADAALQRVE-ALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDI----DSIEAVEAGL 496
Cdd:TIGR01271 518 YTSVIKACQLEedIALFPEKDKTVLGEGGiTLSGGQRARISLARAV--YKDADLYLLDSPFTHLDVvtekEIFESCLCKL 595
|
170
....*....|....
gi 14524463 497 LSYDGALVVVSHDE 510
Cdd:TIGR01271 596 MSNKTRILVTSKLE 609
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-169 |
1.41e-07 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 52.61 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRValARQILRAGADETIADVFgatQAVAVL 94
Cdd:cd03254 15 KKPVLKDINFSIKPgETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID--IRDISRKSLRSMIGVVL---QDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 95 RRAEKGDASVEELETADwtveERIVSALARLG-------LEARADTLLNQ----LSGGQRTRAVLAAAIFSEPDFLLLDE 163
Cdd:cd03254 90 SGTIMENIRLGRPNATD----EEVIEAAKEAGahdfimkLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDE 165
|
....*.
gi 14524463 164 PTNNLD 169
Cdd:cd03254 166 ATSNID 171
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
336-514 |
1.45e-07 |
|
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: 51.39 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTvsvnvpftlldqsVSILERGETI 415
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR-------------IGMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 416 lenF--KR--LNPGasdnACRAALASfrfradaALQRVeaLSGGQVLRAGLACALggSDPPSLLILDEPTNHLDIDSIEA 491
Cdd:cd03223 68 ---FlpQRpyLPLG----TLREQLIY-------PWDDV--LSGGEQQRLAFARLL--LHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|...
gi 14524463 492 VEAGLLSYDGALVVVSHDETFLA 514
Cdd:cd03223 130 LYQLLKELGITVISVGHRPSLWK 152
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-179 |
1.47e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALAR------QILRAGA------------DETIA-DV------FG 86
Cdd:PRK13634 36 VAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkklKPLRKKVgivfqfpehqlfEETVEkDIcfgpmnFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 87 ATQAVAvLRRAEKgdasveeletadwtveerivsALARLGLEaraDTLLNQ----LSGGQRTRAVLAAAIFSEPDFLLLD 162
Cdd:PRK13634 116 VSEEDA-KQKARE---------------------MIELVGLP---EELLARspfeLSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170
....*....|....*..
gi 14524463 163 EPTNNLDRDGRRAVIGL 179
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEM 187
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-191 |
1.89e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 53.73 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSS--GTVAIQGRvALARQILRAGADETIADVF------GATQAVAVLRRAEKGD 101
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNR-KPTKQILKRTGFVTQDDILyphltvRETLVFCSLLRLPKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 102 ASVEELETADwtveerivSALARLGLEARADTLLNQ-----LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR-RA 175
Cdd:PLN03211 174 TKQEKILVAE--------SVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRL 245
|
170
....*....|....*.
gi 14524463 176 VIGLLSGWRSGAIVVS 191
Cdd:PLN03211 246 VLTLGSLAQKGKTIVT 261
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
34-164 |
2.14e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.30 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvALAR----QILRAGADETIADV--FGATQAVAVL------------- 94
Cdd:PRK11300 36 LIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ-HIEGlpghQIARMGVVRTFQHVrlFREMTVIENLlvaqhqqlktglf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 95 ---------RRAEKgdasvEELE-TADWtveerivsaLARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEP 164
Cdd:PRK11300 115 sgllktpafRRAES-----EALDrAATW---------LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
328-380 |
2.17e-07 |
|
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: 53.67 E-value: 2.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 14524463 328 ELPAGRQVLAFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLK 380
Cdd:COG5265 350 PLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR 402
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-169 |
2.35e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.82 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvALARQILRAGADETIADVfgaTQAVAVL 94
Cdd:PRK10895 15 GRRVVEDVSLTVNSgEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE-DISLLPLHARARRGIGYL---PQEASIF 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 95 RRAEKGDASVEELET-ADWTVEERIVSA---LARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK10895 91 RRLSVYDNLMAVLQIrDDLSAEQREDRAnelMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
349-516 |
2.96e-07 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 51.61 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSlVGPRRVSV-TGPNGSGKTSLLKVVTG-------------------ELPP-----------------FKG 391
Cdd:COG0396 13 KEILKGVNLT-IKPGEVHAiMGPNGSGKSTLAKVLMGhpkyevtsgsilldgedilELSPderaragiflafqypveIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 392 tVSVnvpFTLLDQSVSILERGETILENFKRLnpgasdnaCRAALASFRFRADaALQR-V-EALSGGQVLRAGLA--CALg 467
Cdd:COG0396 92 -VSV---SNFLRTALNARRGEELSAREFLKL--------LKEKMKELGLDED-FLDRyVnEGFSGGEKKRNEILqmLLL- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14524463 468 gsdPPSLLILDEPTNHLDIDSIEAVEAG---LLSYDGALVVVSHDETFLANI 516
Cdd:COG0396 158 ---EPKLAILDETDSGLDIDALRIVAEGvnkLRSPDRGILIITHYQRILDYI 206
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
337-496 |
3.15e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.04 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 337 AFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------VPFTLLDQSVSIL- 409
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdirtVTRASLRRNIAVVf 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 410 -ERG---ETILENFKRLNPGASDN-----ACRAALASFRFRADAAL-----QRVEALSGGQVLRAGLACALgGSDPPsLL 475
Cdd:PRK13657 416 qDAGlfnRSIEDNIRVGRPDATDEemraaAERAQAHDFIERKPDGYdtvvgERGRQLSGGERQRLAIARAL-LKDPP-IL 493
|
170 180
....*....|....*....|.
gi 14524463 476 ILDEPTNHLDIDSIEAVEAGL 496
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAAL 514
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-172 |
3.30e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 33 GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQIlragadETIADVFGATQAVAVLrraekGDASVEE------ 106
Cdd:NF033858 296 GFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDI------ATRRRVGYMSQAFSLY-----GELTVRQnlelha 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 107 ----LETADWtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD---RDG 172
Cdd:NF033858 365 rlfhLPAAEI--AARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvaRDM 435
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
34-169 |
3.41e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.04 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrvALARQILRAGADETIADVFgatQAVAVLRRA-------EKGDASVEE 106
Cdd:PRK13657 366 IVGPTGAGKSTLINLLQRVFDPQSGRILIDG--TDIRTVTRASLRRNIAVVF---QDAGLFNRSiednirvGRPDATDEE 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 107 LETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK13657 441 MRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
364-485 |
3.44e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.12 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 364 RVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLDQS---VSILERGE------TILENFKR-LNPG----ASD 428
Cdd:PRK10771 27 RVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgQDHTTTPPSrrpVSMLFQENnlfshlTVAQNIGLgLNPGlklnAAQ 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 14524463 429 NACRAALASfRFRADAALQRVEA-LSGGQVLRAGLACALGGSDPpsLLILDEPTNHLD 485
Cdd:PRK10771 107 REKLHAIAR-QMGIEDLLARLPGqLSGGQRQRVALARCLVREQP--ILLLDEPFSALD 161
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
339-486 |
3.50e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 339 DGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTV-------------SVNVPFTLLDQS 405
Cdd:PRK10253 11 EQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaskEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 406 VS---------ILERG----ETILENFKRLNPGASDNACRAALASfrfraDAALQRVEALSGGQVLRAGLACALggSDPP 472
Cdd:PRK10253 90 ATtpgditvqeLVARGryphQPLFTRWRKEDEEAVTKAMQATGIT-----HLADQSVDTLSGGQRQRAWIAMVL--AQET 162
|
170
....*....|....
gi 14524463 473 SLLILDEPTNHLDI 486
Cdd:PRK10253 163 AIMLLDEPTTWLDI 176
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-210 |
3.56e-07 |
|
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: 50.23 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGtLRPSSgtvaiQGRVALARQilragadetiA 82
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPgDRLLITGPSGTGKSSLFRALAG-LWPWG-----SGRIGMPEG----------E 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 83 DVFGATQA----VAVLRraekgdasveeletadwtveERIVSALARlglearadtllnQLSGGQRTRAVLAAAIFSEPDF 158
Cdd:cd03223 65 DLLFLPQRpylpLGTLR--------------------EQLIYPWDD------------VLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14524463 159 LLLDEPTNNLDRDGRRAVIGLLSGWRSGAIVVSHDRELLEEMDAIIELTSLG 210
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-169 |
3.78e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.18 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRV--------ALA---RQI------------------LRAGADETIA 82
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiCLPpekRRIgyvfqdarlfphykvrgnLRYGMAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 83 DVFgatqavavlrraekgdasveeletadwtveERIVSAlarLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLD 162
Cdd:PRK11144 107 AQF------------------------------DKIVAL---LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
....*..
gi 14524463 163 EPTNNLD 169
Cdd:PRK11144 154 EPLASLD 160
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
349-480 |
4.40e-07 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 51.12 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTL-------------LDQSVSILeRGET 414
Cdd:TIGR04406 14 RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgQDITHlpmherarlgigyLPQEASIF-RKLT 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 415 ILENF-------KRLNPGASDNACRAALASFRFrADAALQRVEALSGGQVLRAGLACALGGSdpPSLLILDEP 480
Cdd:TIGR04406 93 VEENImavleirKDLDRAEREERLEALLEEFQI-SHLRDNKAMSLSGGERRRVEIARALATN--PKFILLDEP 162
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-180 |
5.30e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.17 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGpERTGLVGRNGIGKTSVL----NIIAGTLRPSS------GTVAIQGRvaLARQILRAGADE-TIADVFGATQA 90
Cdd:PRK09984 24 DLNIHHG-EMVALLGPSGSGKSTLLrhlsGLITGDKSAGShiellgRTVQREGR--LARDIRKSRANTgYIFQQFNLVNR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 91 VAVLRRAEKGDASveelETADWTV---------EERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLL 161
Cdd:PRK09984 101 LSVLENVLIGALG----STPFWRTcfswftreqKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170
....*....|....*....
gi 14524463 162 DEPTNNLDRDGRRAVIGLL 180
Cdd:PRK09984 177 DEPIASLDPESARIVMDTL 195
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
114-180 |
5.54e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.00 E-value: 5.54e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14524463 114 VEERIVSALARLGLEARADTLLN----QLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL 180
Cdd:PRK14267 122 LDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELL 192
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
354-529 |
6.04e-07 |
|
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: 50.35 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 354 DLSFSLVGPRRV-SVTGPNGSGKTSLLKVVT----GELP-------------PFKGTVSVNVPFTLLDQSVSILERGETI 415
Cdd:cd03279 19 VIDFTGLDNNGLfLICGPTGAGKSTILDAITyalyGKTPrygrqenlrsvfaPGEDTAEVSFTFQLGGKKYRVERSRGLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 416 LENFKRLnpgasdnacrAALASFRFraDAALQR-VEALSGGQVLRAGLACALGGSD--------PPSLLILDEPTNHLDI 486
Cdd:cd03279 99 YDQFTRI----------VLLPQGEF--DRFLARpVSTLSGGETFLASLSLALALSEvlqnrggaRLEALFIDEGFGTLDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 14524463 487 DSIEAVEAGL--LSYDGALV-VVSHDETFLAniGIGTRVELSTSRG 529
Cdd:cd03279 167 EALEAVATALelIRTENRMVgVISHVEELKE--RIPQRLEVIKTPG 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
338-485 |
6.86e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 50.76 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYDPA-RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV--------NVPFtlLDQSVSI 408
Cdd:PRK13632 10 VENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitiskeNLKE--IRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 LER-------GETI-------LENfKRLNPGA-----SDNACRAALASFrfradaaLQR-VEALSGGQVLRAGLACALGG 468
Cdd:PRK13632 88 IFQnpdnqfiGATVeddiafgLEN-KKVPPKKmkdiiDDLAKKVGMEDY-------LDKePQNLSGGQKQRVAIASVLAL 159
|
170
....*....|....*..
gi 14524463 469 SdpPSLLILDEPTNHLD 485
Cdd:PRK13632 160 N--PEIIIFDESTSMLD 174
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
12-190 |
6.98e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.89 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 12 SKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRV--ALARQILRAGADETIADVFGAT 88
Cdd:PRK13643 14 NSPFASRALFDIDLEVKKgSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsSTSKQKEIKPVRKKVGVVFQFP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 89 QAV----AVLRRAEKG--DASVEELETADWTVEERIVSALARLGLEARAdtllNQLSGGQRTRAVLAAAIFSEPDFLLLD 162
Cdd:PRK13643 94 ESQlfeeTVLKDVAFGpqNFGIPKEKAEKIAAEKLEMVGLADEFWEKSP----FELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180
....*....|....*....|....*....
gi 14524463 163 EPTNNLDRDGRRAVIGLL-SGWRSGAIVV 190
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFeSIHQSGQTVV 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-169 |
1.01e-06 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 49.80 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 14 PDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR--VALARQILRagadETIADV------ 84
Cdd:cd03244 14 PNLPPVLKNISFSIKPgEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiSKIGLHDLR----SRISIIpqdpvl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 85 FGATqavavLRraekgdASVEELETADwtvEERIVSALARLGLEARADTLL-----------NQLSGGQRTRAVLAAAIF 153
Cdd:cd03244 90 FSGT-----IR------SNLDPFGEYS---DEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALL 155
|
170
....*....|....*.
gi 14524463 154 SEPDFLLLDEPTNNLD 169
Cdd:cd03244 156 RKSKILVLDEATASVD 171
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-206 |
1.03e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 51.65 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 12 SKPDgEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-------------RVALARQ---ILR 74
Cdd:TIGR00958 490 NRPD-VPVLKGLTFTLHPgEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQepvLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 75 AGADETIAdvFGATQA-----VAVLRRAEKGDASVEELETADWTVEERivsalarlglearadtlLNQLSGGQRTRAVLA 149
Cdd:TIGR00958 569 GSVRENIA--YGLTDTpdeeiMAAAKAANAHDFIMEFPNGYDTEVGEK-----------------GSQLSGGQKQRIAIA 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 150 AAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGAIVVSHDRELLEEMDAIIEL 206
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQILVL 686
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
352-485 |
1.05e-06 |
|
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: 49.68 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 352 IRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV--------------NVPFTLLDQSVsilERGETILE 417
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvreprevrrRIGIVFQDLSV---DDELTGWE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14524463 418 N---FKRLN--PGAS-DNACRAALASFRFrADAALQRVEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLD 485
Cdd:cd03265 93 NlyiHARLYgvPGAErRERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHR--PEVLFLDEPTIGLD 163
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-192 |
1.12e-06 |
|
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: 49.92 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 4 ITLSALSWSKPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR-------VALARQILRA 75
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAgKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 76 GADETIadvFGATQAVAVlrRAEKGDASVEELETADWT--VEERIVSalarlgLEARADTLLNQ----LSGGQRTRAVLA 149
Cdd:cd03253 81 PQDTVL---FNDTIGYNI--RYGRPDATDEEVIEAAKAaqIHDKIMR------FPDGYDTIVGErglkLSGGEKQRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 14524463 150 AAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSG--AIVVSH 192
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAH 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
314-514 |
1.14e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 51.35 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 314 IEVLQPFSIRLPRTELPAGRQvLAFDGVTAgYDPA-RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGeLPPFkGT 392
Cdd:COG4178 342 LEAADALPEAASRIETSEDGA-LALEDLTL-RTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPY-GS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 393 VSVNVPftlldQSVSIL---ERGETILENFKRL------NPGASDNACRAALASF-------RFRADAALQRVeaLSGGQ 456
Cdd:COG4178 418 GRIARP-----AGARVLflpQRPYLPLGTLREAllypatAEAFSDAELREALEAVglghlaeRLDEEADWDQV--LSLGE 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 457 VLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAVEAGLLS--YDGALVVVSHDETFLA 514
Cdd:COG4178 491 QQRLAFARLL--LHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGHRSTLAA 548
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
367-518 |
1.26e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 367 VTGPNGSGKTSLLKVVTGELPPFKG------TVSVNVPFTLLDQSVSilergetilENFKRLNP---------------- 424
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGerqsqfSHITRLSFEQLQKLVS---------DEWQRNNTdmlspgeddtgrttae 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 425 ----GASDNACRAALASfRFRADAAL-QRVEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDIDSIE---AVEAGL 496
Cdd:PRK10938 105 iiqdEVKDPARCEQLAQ-QFGITALLdRRFKYLSTGETRKTLLCQALMSE--PDLLILDEPFDGLDVASRQqlaELLASL 181
|
170 180
....*....|....*....|....*.
gi 14524463 497 LSYDGALVVVSH--DE--TFLANIGI 518
Cdd:PRK10938 182 HQSGITLVLVLNrfDEipDFVQFAGV 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-204 |
1.42e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.99 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 6 LSALSWSKPDGEHVfsdldlafgpertGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrVALARQILRAgADETIADVF 85
Cdd:PRK13632 25 LKNVSFEINEGEYV-------------AILGHNGSGKSTISKILTGLLKPQSGEIKIDG-ITISKENLKE-IRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 86 GA--TQAVAvlrraekgdASVEE-----LETADWTVEE--RIVSALA-RLGLEARADTLLNQLSGGQRTRAVLAAAIFSE 155
Cdd:PRK13632 90 QNpdNQFIG---------ATVEDdiafgLENKKVPPKKmkDIIDDLAkKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 14524463 156 PDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA----IVVSHDrelleeMDAII 204
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkktlISITHD------MDEAI 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-203 |
1.61e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvALARQILRAGADETIADVFgatQAVAVL 94
Cdd:PRK09700 17 PVHALKSVNLTVYPgEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI-NYNKLDHKLAAQLGIGIIY---QELSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 95 rraekGDASVEE--------------LETADWTvEERIVSA--LARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDF 158
Cdd:PRK09700 93 -----DELTVLEnlyigrhltkkvcgVNIIDWR-EMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14524463 159 LLLDEPTNNL---DRDGRRAVIGLLSGWRSGAIVVSHDrelLEEMDAI 203
Cdd:PRK09700 167 IIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHK---LAEIRRI 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
350-485 |
1.67e-06 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 49.26 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 350 PIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSvnvpFTLLDQS-VSILERG-------------ETI 415
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIL----FGGEDATdVPVQERNvgfvfqhyalfrhMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 416 LENFK---RLNPGASdnacRAALASFRFRADAALQRVE----------ALSGGQVLRAGLACALggSDPPSLLILDEPTN 482
Cdd:cd03296 92 FDNVAfglRVKPRSE----RPPEAEIRAKVHELLKLVQldwladrypaQLSGGQRQRVALARAL--AVEPKVLLLDEPFG 165
|
...
gi 14524463 483 HLD 485
Cdd:cd03296 166 ALD 168
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
138-207 |
1.93e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.70 E-value: 1.93e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 138 LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSG-WRSGA--IVVSHDrelleeMDAIIELT 207
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKtiILVTHD------LDNVLEWT 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
325-486 |
1.96e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 325 PRTELPAGRQVLAFDGVTAgYDPARP---IIRDLSFSLvgpRR---VSVTGPNGSGKTSLLKVVTGELP-PFKGTV---- 393
Cdd:PRK13549 249 PREPHTIGEVILEVRNLTA-WDPVNPhikRVDDVSFSL---RRgeiLGIAGLVGAGRTELVQCLFGAYPgRWEGEIfidg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 394 ---SVNVPFTLLDQS-------------VSILERGETI-------LENFKRLNPGASDNACRAALASFRFRADAALQRVE 450
Cdd:PRK13549 325 kpvKIRNPQQAIAQGiamvpedrkrdgiVPVMGVGKNItlaaldrFTGGSRIDDAAELKTILESIQRLKVKTASPELAIA 404
|
170 180 190
....*....|....*....|....*....|....*.
gi 14524463 451 ALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDI 486
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLN--PKILILDEPTRGIDV 438
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
302-508 |
2.02e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.49 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 302 GALDAVTAAKARIEVLQpfsiRLPRTELPAG------RQVLAFDGVTAGY--DPARPIIRDLSFSLVGPRRVSVTGPNGS 373
Cdd:TIGR00958 443 GMMQAVGASEKVFEYLD----RKPNIPLTGTlaplnlEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGS 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 374 GKTSLLKVVTGELPPFKGTVSV-NVPFTLLD-----QSVSILER-----GETILENFKR-LNPGASDNACRAALASFrfr 441
Cdd:TIGR00958 519 GKSTVAALLQNLYQPTGGQVLLdGVPLVQYDhhylhRQVALVGQepvlfSGSVRENIAYgLTDTPDEEIMAAAKAAN--- 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 442 ADAALQRVEA------------LSGGQVLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAVEAGLLSYDGALVVVSH 508
Cdd:TIGR00958 596 AHDFIMEFPNgydtevgekgsqLSGGQKQRIAIARAL--VRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
349-515 |
2.05e-06 |
|
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: 47.74 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTgelppfkgtvsvnvpFTLLDQSVSILERGETilenfkrlNPGASD 428
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG---------------LALGGAQSATRRRSGV--------KAGCIV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 429 NACRAALASFRFRadaalqrveaLSGGQVLRAGLACALGGS--DPPSLLILDEPTNHLDIDSIEAVEAGLLSY--DGALV 504
Cdd:cd03227 65 AAVSAELIFTRLQ----------LSGGEKELSALALILALAslKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAQV 134
|
170
....*....|..
gi 14524463 505 -VVSHDETFLAN 515
Cdd:cd03227 135 iVITHLPELAEL 146
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
352-492 |
3.73e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.93 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 352 IRDLSFSlVGP-RRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN--VPFtllDQSVSILER-----GE--------TI 415
Cdd:COG4586 38 VDDISFT-IEPgEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyVPF---KRRKEFARRigvvfGQrsqlwwdlPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 416 LENFkRLNP---GASDNACRAALASF--RFRADAALQR-VEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDIDSI 489
Cdd:COG4586 114 IDSF-RLLKaiyRIPDAEYKKRLDELveLLDLGELLDTpVRQLSLGQRMRCELAAALLHR--PKILFLDEPTIGLDVVSK 190
|
...
gi 14524463 490 EAV 492
Cdd:COG4586 191 EAI 193
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
352-513 |
4.67e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.93 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 352 IRDLSFSLVGPRRVSVTGPNGSGKTSLL---------KVVTGELPPFKGTVSVnvpftLLDQSVSILERGETILenfkRL 422
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVneglyasgkARLISFLPKFSRNKLI-----FIDQLQFLIDVGLGYL----TL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 423 NpgasdnacraalasfrfradaalQRVEALSGGQVLRAGLACALGGSDPPSLLILDEPT---NHLDIDSIEAVEAGLLSY 499
Cdd:cd03238 82 G-----------------------QKLSTLSGGELQRVKLASELFSEPPGTLFILDEPStglHQQDINQLLEVIKGLIDL 138
|
170
....*....|....
gi 14524463 500 DGALVVVSHDETFL 513
Cdd:cd03238 139 GNTVILIEHNLDVL 152
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
7-180 |
4.83e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.55 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 7 SALSWSKP------DGehvfSDLDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGrvalarQILRAGADET 80
Cdd:PRK15079 24 KQWFWQPPktlkavDG----VTLRLYEG-ETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG------KDLLGMKDDE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 81 IADVFGATQAV-----AVLR-RAEKGDASVEELET-----ADWTVEERIVSALARLGLearADTLLN----QLSGGQRTR 145
Cdd:PRK15079 93 WRAVRSDIQMIfqdplASLNpRMTIGEIIAEPLRTyhpklSRQEVKDRVKAMMLKVGL---LPNLINryphEFSGGQCQR 169
|
170 180 190
....*....|....*....|....*....|....*
gi 14524463 146 AVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL 180
Cdd:PRK15079 170 IGIARALILEPKLIICDEPVSALDVSIQAQVVNLL 204
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
335-508 |
5.07e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNV-PFTLLDQSVSI----- 408
Cdd:PRK13543 11 LLAAHALAFSRN-EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGkTATRGDRSRFMaylgh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 ---LERGETILENFKRLNpgaSDNACRA------ALASFRFrADAALQRVEALSGGQVLRagLACALGGSDPPSLLILDE 479
Cdd:PRK13543 90 lpgLKADLSTLENLHFLC---GLHGRRAkqmpgsALAIVGL-AGYEDTLVRQLSAGQKKR--LALARLWLSPAPLWLLDE 163
|
170 180 190
....*....|....*....|....*....|..
gi 14524463 480 PTNHLDIDSIEAVE---AGLLSYDGALVVVSH 508
Cdd:PRK13543 164 PYANLDLEGITLVNrmiSAHLRGGGAALVTTH 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-387 |
5.15e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 35 VGRNGIGKTSVLNIIAGTLRPSSGTVA-------------IQGRVALARQ-----ILRAGADETiadvfGATQAvAVLRR 96
Cdd:PRK10938 35 VGANGSGKSALARALAGELPLLSGERQsqfshitrlsfeqLQKLVSDEWQrnntdMLSPGEDDT-----GRTTA-EIIQD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 97 AEKGDASVEELEtadwtveerivsalARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAV 176
Cdd:PRK10938 109 EVKDPARCEQLA--------------QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 177 igllsgwrsgaivvshdRELLEEMdaiieltslgtkrygggwsayqaaraveleaAQQSLTLArktadevdrkarALAER 256
Cdd:PRK10938 175 -----------------AELLASL-------------------------------HQSGITLV------------LVLNR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 257 LDKRDASGTRKAAKGDMPRILVGrrksnaeesrgksvelaeRRRAGALDAVTAAKARIEVLQpfSIRLPRTELPAGRQVL 336
Cdd:PRK10938 195 FDEIPDFVQFAGVLADCTLAETG------------------EREEILQQALVAQLAHSEQLE--GVQLPEPDEPSARHAL 254
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 14524463 337 AFD-------GVTAGYDPaRPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELP 387
Cdd:PRK10938 255 PANeprivlnNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP 311
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
351-509 |
5.29e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.89 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 351 IIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPP------FKG----TVSVNVPFTLLDQSVSILERGETILENFK 420
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPtsgdviFNGqpmsKLSSAAKAELRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 421 RL------------NPGASDNACRAALASFRFRADAAlQRVEALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDI-- 486
Cdd:PRK11629 104 ALenvamplligkkKPAEINSRALEMLAAVGLEHRAN-HRPSELSGGERQRVAIARAL--VNNPRLVLADEPTGNLDArn 180
|
170 180
....*....|....*....|....*
gi 14524463 487 -DSIEAVEAGLLSYDG-ALVVVSHD 509
Cdd:PRK11629 181 aDSIFQLLGELNRLQGtAFLVVTHD 205
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-509 |
6.41e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.75 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 356 SFSLVG---PRRVSVTG---PNGSGKTSLLKVVTGELPP-----------------FKGTVSVNVPFTLLDQSVSILERG 412
Cdd:cd03236 14 SFKLHRlpvPREGQVLGlvgPNGIGKSTALKILAGKLKPnlgkfddppdwdeildeFRGSELQNYFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 413 E-----------TILENFKRLNP-GASDNACRaalasfRFRADAALQR-VEALSGGQVLR-AGLACALGGSDppsLLILD 478
Cdd:cd03236 94 QyvdlipkavkgKVGELLKKKDErGKLDELVD------QLELRHVLDRnIDQLSGGELQRvAIAAALARDAD---FYFFD 164
|
170 180 190
....*....|....*....|....*....|....
gi 14524463 479 EPTNHLDID---SIEAVEAGLLSYDGALVVVSHD 509
Cdd:cd03236 165 EPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHD 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
355-509 |
6.64e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 47.53 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 355 LSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPpFKGTVSVN-VPftLLDQSVSILERgetilenfKR------------ 421
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNgRP--LSDWSAAELAR--------HRaylsqqqsppfa 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 422 ----------LNPGASDNACRAALASF--RFRADAALQR-VEALSGGQVLRAGLACAL-----GGSDPPSLLILDEPTNH 483
Cdd:COG4138 84 mpvfqylalhQPAGASSEAVEQLLAQLaeALGLEDKLSRpLTQLSGGEWQRVRLAAVLlqvwpTINPEGQLLLLDEPMNS 163
|
170 180 190
....*....|....*....|....*....|....
gi 14524463 484 LDI------DSI--EAVEAGllsydGALVVVSHD 509
Cdd:COG4138 164 LDVaqqaalDRLlrELCQQG-----ITVVMSSHD 192
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
351-396 |
6.91e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 47.38 E-value: 6.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 14524463 351 IIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN 396
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
135-216 |
7.55e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 135 LNQLSGGQRTRAVLAAAIFSEPD--FLLLDEPTNNLDRDGRRAVIGLLSGWRSGA---IVVSHDRELLEEMDAIIELTSl 209
Cdd:cd03238 85 LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGntvILIEHNLDVLSSADWIIDFGP- 163
|
....*..
gi 14524463 210 GTKRYGG 216
Cdd:cd03238 164 GSGKSGG 170
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-202 |
8.61e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 47.37 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 13 KPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAG--TLRPSSGTVAIQGRvalarQILRAGADETI-ADVFGAT 88
Cdd:COG0396 9 SVEGKEILKGVNLTIKPgEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGE-----DILELSPDERArAGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 89 QA------VAV---LRRAEKgdaSVEELETADWTVEERIVSALARLGL-EARADTLLNQ-LSGGQRTRAVLAAAIFSEPD 157
Cdd:COG0396 84 QYpveipgVSVsnfLRTALN---ARRGEELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 14524463 158 FLLLDEPTNNLDRDGRRAVIGLLSGWRS---GAIVVSHDRELLEEMDA 202
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITHYQRILDYIKP 208
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
350-486 |
8.86e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.54 E-value: 8.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 350 PIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVPFTLLDQSVSILErgETILEN------FKRLN 423
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMP--GTIKENiifgvsYDEYR 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 424 PGASDNACRAA--LASFRFRADAAL-QRVEALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDI 486
Cdd:cd03291 129 YKSVVKACQLEedITKFPEKDNTVLgEGGITLSGGQRARISLARAV--YKDADLYLLDSPFGYLDV 192
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
349-516 |
8.91e-06 |
|
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: 47.26 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGElPPFK---GTVSVNVPFTLldqSVSILERG-----------ET 414
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH-PSYEvtsGTILFKGQDLL---ELEPDERAraglflafqypEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 415 I----LENFKRlnpgASDNACRAA-------LASFRFRADAALQRV------------EALSGGQ----------VLRag 461
Cdd:TIGR01978 89 IpgvsNLEFLR----SALNARRSArgeepldLLDFEKLLKEKLALLdmdeeflnrsvnEGFSGGEkkrneilqmaLLE-- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 14524463 462 lacalggsdpPSLLILDEPTNHLDIDSIEAVEAGLLSY---DGALVVVSHDETFLANI 516
Cdd:TIGR01978 163 ----------PKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYI 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
3-193 |
1.12e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.08 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 3 SITLSALSWSKPDG---EHV-FSDLDLAFGPERT-GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALAR---QILR 74
Cdd:PRK13646 2 TIRFDNVSYTYQKGtpyEHQaIHDVNTEFEQGKYyAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 75 AgADETIADVFGATQAV----AVLRRAEKG----DASVEEletadwtVEERIVSALARLGLEARADTLLN-QLSGGQRTR 145
Cdd:PRK13646 82 P-VRKRIGMVFQFPESQlfedTVEREIIFGpknfKMNLDE-------VKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRK 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 14524463 146 AVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWR----SGAIVVSHD 193
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD 205
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-68 |
1.13e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 1.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 2 PSITLSALSWSKPDGEHVFSDLDLAF---GPERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVAL 68
Cdd:PRK13545 20 PFDKLKDLFFRSKDGEYHYALNNISFevpEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL 89
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
122-206 |
1.36e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.15 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 122 LARLGLEaraDTLLN----QLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGL-LSGWRSG--AIVVSHDR 194
Cdd:PRK13631 160 LNKMGLD---DSYLErspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLiLDAKANNktVFVITHTM 236
|
90
....*....|...
gi 14524463 195 E-LLEEMDAIIEL 206
Cdd:PRK13631 237 EhVLEVADEVIVM 249
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
33-193 |
1.39e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.84 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 33 GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRvalarqilragaDETIADVFGATQA-----------------VAVLR 95
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPDAGEVHYRMR------------DGQLRDLYALSEAerrrllrtewgfvhqhpRDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 96 RAEKGDASV-EELETADW----TVEERIVSALARLGLEA-RADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK11701 104 MQVSAGGNIgERLMAVGArhygDIRATAGDWLERVEIDAaRIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
170 180
....*....|....*....|....*...
gi 14524463 170 RDGRRAVIGLLSGWRS----GAIVVSHD 193
Cdd:PRK11701 184 VSVQARLLDLLRGLVRelglAVVIVTHD 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
345-524 |
1.57e-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: 48.09 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 345 YDP-ARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTV-----SVNVPFTLLDQSV------SILERG 412
Cdd:TIGR01257 938 FEPsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkDIETNLDAVRQSLgmcpqhNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 413 ETILEN---FKRLNPGASDnacRAALASFRFRADAAL-----QRVEALSGGQVLRAGLACALGGSdpPSLLILDEPTNHL 484
Cdd:TIGR01257 1018 LTVAEHilfYAQLKGRSWE---EAQLEMEAMLEDTGLhhkrnEEAQDLSGGMQRKLSVAIAFVGD--AKVVVLDEPTSGV 1092
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14524463 485 DIDSIEAVEAGLLSY-DGALVVVSHDETFLANIgIGTRVEL 524
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYrSGRTIIMSTHHMDEADL-LGDRIAI 1132
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
349-480 |
2.08e-05 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 46.00 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------VPF--------TLLDQSVSILeRGET 414
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditkLPMhkrarlgiGYLPQEASIF-RKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 415 ILENFkrlnpgasdnacRAALASFRFRADAALQRVE-----------------ALSGGQVLRAGLACALGGSdpPSLLIL 477
Cdd:cd03218 92 VEENI------------LAVLEIRGLSKKEREEKLEelleefhithlrkskasSLSGGERRRVEIARALATN--PKFLLL 157
|
...
gi 14524463 478 DEP 480
Cdd:cd03218 158 DEP 160
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-168 |
2.33e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 33 GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG---RVALARQILRAGadetIADVFGATQAVAVLRRAEK-------GDA 102
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemRFASTTAALAAG----VAIIYQELHLVPEMTVAENlylgqlpHKG 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 103 SVEELETADWTVEERivsaLARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNL 168
Cdd:PRK11288 110 GIVNRRLLNYEAREQ----LEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
338-508 |
2.40e-05 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 44.73 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAgydparpiIRDLSFSLvgpRRVSVT---GPNGSGKTSLLKVVTGELPPFKGTVSVNvpftllDQSVSIlerget 414
Cdd:cd03216 10 FGGVKA--------LDGVSLSV---RRGEVHallGENGAGKSTLMKILSGLYKPDSGEILVD------GKEVSF------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 415 ilenfkrLNPgasdnacRAALAsfrfradAALQRVEALSGGQvlRAGLACALGGSDPPSLLILDEPTNHLDIDSIEAVEA 494
Cdd:cd03216 67 -------ASP-------RDARR-------AGIAMVYQLSVGE--RQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170
....*....|....*..
gi 14524463 495 --GLLSYDG-ALVVVSH 508
Cdd:cd03216 124 viRRLRAQGvAVIFISH 140
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
338-497 |
2.56e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.64 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTV-----------SVNVPFtLLDQSV 406
Cdd:PRK10908 4 FEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlkNREVPF-LRRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 407 SILERGETILENFKRLNPGASDNACRAALASFRFRADAALQRVE----------ALSGGQVLRAGLACALggSDPPSLLI 476
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGlldkaknfpiQLSGGEQQRVGIARAV--VNKPAVLL 160
|
170 180
....*....|....*....|.
gi 14524463 477 LDEPTNHLDidsiEAVEAGLL 497
Cdd:PRK10908 161 ADEPTGNLD----DALSEGIL 177
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
344-509 |
2.89e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 45.83 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 344 GYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLDQSVSILERGETIL---ENF 419
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgEPLAKLNRAQRKAFRRDIQMvfqDSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 420 KRLNPGAS---------------DNACRAALASFRFRA----DAALQRVEA-LSGGQVLRAGLACALGGSdpPSLLILDE 479
Cdd:PRK10419 100 SAVNPRKTvreiireplrhllslDKAERLARASEMLRAvdldDSVLDKRPPqLSGGQLQRVCLARALAVE--PKLLILDE 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 14524463 480 PTNHLDIdsieAVEAGLLS--------YDGALVVVSHD 509
Cdd:PRK10419 178 AVSNLDL----VLQAGVIRllkklqqqFGTACLFITHD 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
34-196 |
3.10e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 44.94 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG------RVALARQILRAGADETIadvfgatQAVAVLRraekgDASVEEL 107
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTYQKQLCFVGHRSGI-------NPYLTLR-----ENCLYDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 108 ETADWTVEeriVSALARL-GLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS- 185
Cdd:PRK13540 100 HFSPGAVG---ITELCRLfSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAk 176
|
170
....*....|..
gi 14524463 186 -GAIVVSHDREL 196
Cdd:PRK13540 177 gGAVLLTSHQDL 188
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-272 |
3.17e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQ---ILRAGADETIadVFGATQAVAVLRRAEKgdasVEELE 108
Cdd:PTZ00243 689 TVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQqawIMNATVRGNI--LFFDEEDAARLADAVR----VSQLE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 109 tADwtveerivsaLARL--GLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRD-GRRAVIGLLSGWRS 185
Cdd:PTZ00243 763 -AD----------LAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALA 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 186 GA--IVVSHDRELLEEMDAIIELTSlGTKRYGGGW------SAYQAARAVELEAAQQSLTLARKTADEVDRkARALAERL 257
Cdd:PTZ00243 832 GKtrVLATHQVHVVPRADYVVALGD-GRVEFSGSSadfmrtSLYATLAAELKENKDSKEGDADAEVAEVDA-APGGAVDH 909
|
250
....*....|....*
gi 14524463 258 DKRDASGTRKAAKGD 272
Cdd:PTZ00243 910 EPPVAKQEGNAEGGD 924
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
138-169 |
3.33e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 45.41 E-value: 3.33e-05
10 20 30
....*....|....*....|....*....|..
gi 14524463 138 LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
349-509 |
3.51e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.53 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV---NVP-------------FTLLDQS------V 406
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdgeNIPamsrsrlytvrkrMSMLFQSgalftdM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 407 SILERGETILENFKRLNPGASDNACRAALASFRFRADAALQRVEaLSGGQVLRAGLACALGGSdpPSLLILDEPTNHLDI 486
Cdd:PRK11831 100 NVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSE-LSGGMARRAALARAIALE--PDLIMFDEPFVGQDP 176
|
170 180
....*....|....*....|....*..
gi 14524463 487 DSIEAVEAGLLSYDGAL----VVVSHD 509
Cdd:PRK11831 177 ITMGVLVKLISELNSALgvtcVVVSHD 203
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
441-523 |
3.84e-05 |
|
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: 46.58 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 441 RADAALQRVEALSGGQ------VLRAGLACALGGSdpPSLLILDEPTNHLDIDSIEAVEAGLLSY--------DGALVVV 506
Cdd:TIGR00606 1189 KGDTALDMRGRCSAGQkvlaslIIRLALAETFCLN--CGIIALDEPTTNLDRENIESLAHALVEIiksrsqqrNFQLLVI 1266
|
90
....*....|....*..
gi 14524463 507 SHDETFLANIGIGTRVE 523
Cdd:TIGR00606 1267 THDEDFVELLGRSEYVE 1283
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
114-169 |
3.94e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 45.29 E-value: 3.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 114 VEERIVSALARLGL----EARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK14247 119 LQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
349-517 |
3.97e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.42 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVPFTLLDQSV----SILERGETILEnFKRLNP 424
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfqidAIKLRKEVGMV-FQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 425 -----------------GASDN--------ACRAALASFRFRADAALQRVEALSGGQVLRAGLACALggSDPPSLLILDE 479
Cdd:PRK14246 102 fphlsiydniayplkshGIKEKreikkiveECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARAL--ALKPKVLLMDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 14524463 480 PTNHLDIDSIEAVEAGL--LSYDGALVVVSHDETFLANIG 517
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLIteLKNEIAIVIVSHNPQQVARVA 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
325-522 |
4.06e-05 |
|
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: 46.36 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 325 PRTELPAGRQVLAFDGVTAgYDPARPIIR---DLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELP-PFKGTVSVN---- 396
Cdd:TIGR02633 247 PHEPHEIGDVILEARNLTC-WDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINgkpv 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 397 ---------------VPFTLLDQS-VSILERGETI----LENF---KRLNPGASDNACRAALASFRFRADAALQRVEALS 453
Cdd:TIGR02633 326 dirnpaqairagiamVPEDRKRHGiVPILGVGKNItlsvLKSFcfkMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLS 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 454 GGQVLRAGLACALggSDPPSLLILDEPTNHLDIDSIEAVE--AGLLSYDG-ALVVVSHDetfLANI-GIGTRV 522
Cdd:TIGR02633 406 GGNQQKAVLAKML--LTNPRVLILDEPTRGVDVGAKYEIYklINQLAQEGvAIIVVSSE---LAEVlGLSDRV 473
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
32-180 |
4.37e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.54 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGtlRPSSGTvaIQGRVALARQILragaDETIADVFGatqavavlrRAEKGDASVEELetad 111
Cdd:cd03232 36 TALMGESGAGKTTLLDVLAG--RKTAGV--ITGEILINGRPL----DKNFQRSTG---------YVEQQDVHSPNL---- 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14524463 112 wTVEERI-VSALAR-LGLEaradtllnqlsggQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL 180
Cdd:cd03232 95 -TVREALrFSALLRgLSVE-------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
30-204 |
4.96e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.08 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 30 ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQI--LRagadETIADVF--------GATQAVAVLRRAEK 99
Cdd:PRK13642 34 EWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnLR----RKIGMVFqnpdnqfvGATVEDDVAFGMEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 100 GDASVEELETadwTVEERIVsALARLGLEARADTllnQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGL 179
Cdd:PRK13642 110 QGIPREEMIK---RVDEALL-AVNMLDFKTREPA---RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180
....*....|....*....|....*....
gi 14524463 180 L----SGWRSGAIVVSHDRELLEEMDAII 204
Cdd:PRK13642 183 IheikEKYQLTVLSITHDLDEAASSDRIL 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-206 |
5.50e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 43.96 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 16 GEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR---VALARQILRAGadetiadvfgatqaV 91
Cdd:cd03215 12 VKGAVRDVSFEVRAgEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtRRSPRDAIRAG--------------I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 92 AVLRRAEKGDASVeeletADWTVEERIvsalarlglearadTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRD 171
Cdd:cd03215 78 AYVPEDRKREGLV-----LDLSVAENI--------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190
....*....|....*....|....*....|....*...
gi 14524463 172 GRRAVIGLLSGWRS---GAIVVShdrellEEMDAIIEL 206
Cdd:cd03215 139 AKAEIYRLIRELADagkAVLLIS------SELDELLGL 170
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-480 |
6.36e-05 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 45.09 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 354 DLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvPFTLLDQSVSI---LERG--------------ETIL 416
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLG-GEVLQDSARGIflpPHRRrigyvfqearlfphLSVR 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14524463 417 ENfkrLNPGASdnACRAALASFRFRADAAL--------QRVEALSGGQVLRAGLACALGGSdpPSLLILDEP 480
Cdd:COG4148 96 GN---LLYGRK--RAPRAERRISFDEVVELlgighlldRRPATLSGGERQRVAIGRALLSS--PRLLLMDEP 160
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
20-201 |
7.30e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.99 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 20 FSDLDLAFGPERTGLVGRNGIGKTSVLNIIAGTLRPSSG-------------TVAIQGRV-----ALARQILRAGADETI 81
Cdd:COG3593 14 IKDLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddPDLPEIEIeltfgSLLSRLLRLLLKEED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 82 ADVF-------------GATQAVAVLRRAEKGDASVEELETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVL 148
Cdd:COG3593 94 KEELeealeelneelkeALKALNELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGKELPLDRLGSGFQRLILL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 149 AAAIF-------SEPDFLLLDEPTNNLDRDGRRAVIGLL---SGWRSGAIVVSHDRELLEEMD 201
Cdd:COG3593 174 ALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLkelSEKPNQVIITTHSPHLLSEVP 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
336-488 |
7.35e-05 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 43.94 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPARP-IIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------VPFTLLDQSVSI 408
Cdd:cd03369 7 IEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgidistIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 LERGETILENFKRLNPGA----SDNACRAALasfrfradaalqRV----EALSGGQVLRAGLACALGGSdpPSLLILDEP 480
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPfdeySDEEIYGAL------------RVseggLNLSQGQRQLLCLARALLKR--PRVLVLDEA 152
|
....*...
gi 14524463 481 TNHLDIDS 488
Cdd:cd03369 153 TASIDYAT 160
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-193 |
8.25e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 44.27 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 33 GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVA-LARQILRAGA---DETIADVFGATQAVAVLRRAEKGDASVEELE 108
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyFGKDIFQIDAiklRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 109 TADWTVEERIVS-ALARLGLEARADTLLN----QLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGW 183
Cdd:PRK14246 120 IKEKREIKKIVEeCLRKVGLWKEVYDRLNspasQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL 199
|
170
....*....|..
gi 14524463 184 RS--GAIVVSHD 193
Cdd:PRK14246 200 KNeiAIVIVSHN 211
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
113-199 |
8.70e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.73 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 113 TVEERIVSALARLGL---EARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS---- 185
Cdd:PRK11022 126 TRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenm 205
|
90
....*....|....
gi 14524463 186 GAIVVSHDRELLEE 199
Cdd:PRK11022 206 ALVLITHDLALVAE 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
348-486 |
9.11e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 348 ARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELP--------PFKGTVSVN-VPFTLLDQSVsiLERGETILEN 418
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNgEPLAAIDAPR--LARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 419 FKR----------LNPGASDNACRAALASFRFR--ADAALQRVEA----------LSGGQVLRAGLACAL-------GGS 469
Cdd:PRK13547 91 AAQpafafsareiVLLGRYPHARRAGALTHRDGeiAWQALALAGAtalvgrdvttLSGGELARVQFARVLaqlwpphDAA 170
|
170
....*....|....*..
gi 14524463 470 DPPSLLILDEPTNHLDI 486
Cdd:PRK13547 171 QPPRYLLLDEPTAALDL 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
355-509 |
9.20e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 355 LSFSLVGPRRVSVTGPNGSGKTSLLKVVTGeLPPFKGTVSVNVPfTLLDQSVSILERGETILENFKR------------- 421
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQ-PLEAWSAAELARHRAYLSQQQTppfampvfqyltl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 422 -LNPGASDNACRAALASF--RFRADAALQR-VEALSGGQVLRAGLACALGGSDPPS-----LLILDEPTNHLDI------ 486
Cdd:PRK03695 93 hQPDKTRTEAVASALNEVaeALGLDDKLGRsVNQLSGGEWQRVRLAAVVLQVWPDInpagqLLLLDEPMNSLDVaqqaal 172
|
170 180
....*....|....*....|....*
gi 14524463 487 DSI--EAVEAGllsydGALVVVSHD 509
Cdd:PRK03695 173 DRLlsELCQQG-----IAVVMSSHD 192
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
122-255 |
9.51e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 122 LARLGLEARADTLLNQLS-------------GGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIG-LLSGWRSGA 187
Cdd:NF000106 116 LSRKDARARADELLERFSlteaagraaakysGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDeVRSMVRDGA 195
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14524463 188 IVVSHDRELLEEMDAIIELTSLGTKRYgggwSAYQAARAVELEAAQQSLTLARKTADEVDRKARALAE 255
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRV----IADGKVDELKTKVGGRTLQIRPAHAAELDRMVGAIAQ 259
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
336-509 |
1.12e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 43.90 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDpARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTvsvnvpftLLDQSVSILERGETI 415
Cdd:PRK11247 13 LLLNAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE--------LLAGTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 416 LENFK--RLNPGAS--DNACRAALASFRFRADAALQRV----------EALSGGQVLRAGLACALggSDPPSLLILDEPT 481
Cdd:PRK11247 84 RLMFQdaRLLPWKKviDNVGLGLKGQWRDAALQALAAVgladranewpAALSGGQKQRVALARAL--IHRPGLLLLDEPL 161
|
170 180 190
....*....|....*....|....*....|..
gi 14524463 482 NHLD----IDSIEAVEAGLLSYDGALVVVSHD 509
Cdd:PRK11247 162 GALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
122-216 |
1.17e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 122 LARLGLEARADTLlnqlSGGQRTRAVLAAAIFSEPDFLL--LDEPTNNL-DRDGRRaVIGLLSGWR---SGAIVVSHDRE 195
Cdd:TIGR00630 477 LDYLSLSRAAGTL----SGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLhQRDNRR-LINTLKRLRdlgNTLIVVEHDED 551
|
90 100
....*....|....*....|.
gi 14524463 196 LLEEMDAIIELTSlGTKRYGG 216
Cdd:TIGR00630 552 TIRAADYVIDIGP-GAGEHGG 571
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
135-210 |
1.73e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 135 LNQLSGGQRT------RAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL------SGWRSGAIVVSHDRELLEEMDA 202
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIeyslkdSSDIPQVIMISHHRELLSVADV 878
|
....*...
gi 14524463 203 IIELTSLG 210
Cdd:PRK01156 879 AYEVKKSS 886
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
303-396 |
1.96e-04 |
|
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: 44.02 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 303 ALDAVTAAKARIEVLQPFSIRLPRTELPAGRQVLAFDGVTAGYDPARPiirDLSFSlVGP-----RR---VSVTGPNGSG 374
Cdd:COG4615 295 ALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDG---DEGFT-LGPidltiRRgelVFIVGGNGSG 370
|
90 100
....*....|....*....|..
gi 14524463 375 KTSLLKVVTGELPPFKGTVSVN 396
Cdd:COG4615 371 KSTLAKLLTGLYRPESGEILLD 392
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
352-486 |
2.01e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 352 IRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN---------------VPFTLLDQSVSI--LERGET 414
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfgdysyrsqrIRMIFQDPSTSLnpRQRISQ 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 415 ILENFKRLN----PGASDNACRAALASFRFRADAALQRVEALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDI 486
Cdd:PRK15112 109 ILDFPLRLNtdlePEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARAL--ILRPKVIIADEALASLDM 182
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
338-488 |
2.04e-04 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 42.87 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAGYDP-ARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVN------VPFTLLDQSVSI-- 408
Cdd:cd03244 5 FKNVSLRYRPnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDgvdiskIGLHDLRSRISIip 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 ----LERGeTILENfkrLNP--GASDNACRAALasfrfrADAAL-QRVEALS---------GGQVLRAG------LACAL 466
Cdd:cd03244 85 qdpvLFSG-TIRSN---LDPfgEYSDEELWQAL------ERVGLkEFVESLPggldtvveeGGENLSVGqrqllcLARAL 154
|
170 180
....*....|....*....|..
gi 14524463 467 ggSDPPSLLILDEPTNHLDIDS 488
Cdd:cd03244 155 --LRKSKILVLDEATASVDPET 174
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
349-485 |
2.11e-04 |
|
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: 42.63 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFsLVGP-RRVSVTGPNGSGKTSLLKVVTGELPpfkGTVSVNvpftlldqsVSILERGETILENFKRlnpgas 427
Cdd:cd03233 20 IPILKDFSG-VVKPgEMVLVLGRPGSGCSTLLKALANRTE---GNVSVE---------GDIHYNGIPYKEFAEK------ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14524463 428 dnaCRAALA----------------SFRFRADA-ALQRVEALSGGQVLRAGLACALGGsdPPSLLILDEPTNHLD 485
Cdd:cd03233 81 ---YPGEIIyvseedvhfptltvreTLDFALRCkGNEFVRGISGGERKRVSIAEALVS--RASVLCWDNSTRGLD 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-176 |
2.57e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 2.57e-04
10 20 30
....*....|....*....|....*....|....*....
gi 14524463 138 LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAV 176
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-169 |
2.61e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 13 KPDGEHVFSDLDLAFGP-ERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG----RVALA--RQILRAGADETIadVF 85
Cdd:PLN03232 1245 RPGLPPVLHGLSFFVSPsEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvaKFGLTdlRRVLSIIPQSPV--LF 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 86 GATQAVAVLRRAEKGDASVeeletadWTVEER--IVSALAR--LGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLL 161
Cdd:PLN03232 1323 SGTVRFNIDPFSEHNDADL-------WEALERahIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVL 1395
|
....*...
gi 14524463 162 DEPTNNLD 169
Cdd:PLN03232 1396 DEATASVD 1403
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
34-193 |
2.68e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.76 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKT----SVLNIIAGTLRPSSGTVAIQGrVALARQILRAgadETIADVFGATQAVAVLRRAEKGDASVEELET 109
Cdd:PRK10418 34 LVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG-KPVAPCALRG---RKIATIMQNPRSAFNPLHTMHTHARETCLAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 110 ADWTVEERIVSALARLGLEARADTLLN---QLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRS- 185
Cdd:PRK10418 110 GKPADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQk 189
|
170
....*....|.
gi 14524463 186 ---GAIVVSHD 193
Cdd:PRK10418 190 ralGMLLVTHD 200
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
135-210 |
2.81e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 135 LNQLSGGQRT------RAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWR---SGAIVVSHDRELLEEMDAIIE 205
Cdd:PRK03918 786 LTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLrkiPQVIIVSHDEELKDAADYVIR 865
|
....*
gi 14524463 206 LTSLG 210
Cdd:PRK03918 866 VSLEG 870
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
334-488 |
2.81e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.95 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 334 QVLAFDGVTAGYDPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSV---NVPFTLLDQSVSILE 410
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqPTRQALQKNLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 411 RGETI-------LENFKRLNPGASDNACRAALASFRFRADAALQRVE----------ALSGGQVLRAGLACALggSDPPS 473
Cdd:PRK15056 85 QSEEVdwsfpvlVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDmvefrhrqigELSGGQKKRVFLARAI--AQQGQ 162
|
170
....*....|....*
gi 14524463 474 LLILDEPTNHLDIDS 488
Cdd:PRK15056 163 VILLDEPFTGVDVKT 177
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-165 |
2.84e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGpERTGLVGRNGIGKTSVLNIIAGTLRPSSGTV--------------AIQGRVALARQILraGAD--------E 79
Cdd:NF033858 21 SLDIPAG-CMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevlggdmadarhrrAVCPRIAYMPQGL--GKNlyptlsvfE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 80 TI---ADVFGatqavavLRRAEKgdasveeletadwtvEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEP 156
Cdd:NF033858 98 NLdffGRLFG-------QDAAER---------------RRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
....*....
gi 14524463 157 DFLLLDEPT 165
Cdd:NF033858 156 DLLILDEPT 164
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
410-518 |
3.44e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.00 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 410 ERGETILENFKRLNPGASD---NACRAALASFRFRADAALQRVEA--LSGGQvLRA-GLACALGGSDPPSLLILDEPTNH 483
Cdd:COG4637 212 ERFERILEALRDAFPGFEDievEPDEDGRVLLEFREKGLDRPFPAreLSDGT-LRFlALLAALLSPRPPPLLCIEEPENG 290
|
90 100 110
....*....|....*....|....*....|....*...
gi 14524463 484 LDIDSIEAVeAGLL---SYDGALVVVSHDETFLANIGI 518
Cdd:COG4637 291 LHPDLLPAL-AELLreaSERTQVIVTTHSPALLDALEP 327
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
351-508 |
3.78e-04 |
|
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: 43.20 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 351 IIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNVP---F-----------TLLDQSVSilerGETIL 416
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKgklFyvpqrpymtlgTLRDQIIY----PDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 417 ENFKRlnpGASDNACRAALASFRFraDAALQR----------VEALSGGQVLRAGLACALggSDPPSLLILDEPTNHLDI 486
Cdd:TIGR00954 543 DMKRR---GLSDKDLEQILDNVQL--THILEReggwsavqdwMDVLSGGEKQRIAMARLF--YHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|..
gi 14524463 487 DSIEAVEAGLLSYDGALVVVSH 508
Cdd:TIGR00954 616 DVEGYMYRLCREFGITLFSVSH 637
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
335-485 |
3.82e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.48 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 335 VLAFDGVTAGY-DPARPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVS-VNVPFTLLDQSV--SILE 410
Cdd:PRK13640 5 IVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkITVDGITLTAKTvwDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 411 RGETILEN---------------FKRLNPGASDNA----CRAALASFRFrADAALQRVEALSGGQVLRAGLACALGGSdp 471
Cdd:PRK13640 85 KVGIVFQNpdnqfvgatvgddvaFGLENRAVPRPEmikiVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVE-- 161
|
170
....*....|....
gi 14524463 472 PSLLILDEPTNHLD 485
Cdd:PRK13640 162 PKIIILDESTSMLD 175
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
137-204 |
4.10e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 42.30 E-value: 4.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14524463 137 QLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL----SGWRSGAIVVSHDR-ELLEEMDAII 204
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMdQVLRIADEVI 222
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
367-509 |
4.21e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 367 VTGPNGSGKTSLLKVVT----GE-----------LPPFKGTVSVNVPFTLLDQSVSI----------------------- 408
Cdd:COG0419 28 IVGPNGAGKSTILEAIRyalyGKarsrsklrsdlINVGSEEASVELEFEHGGKRYRIerrqgefaefleakpserkealk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 409 ----LERGETILENFKRLNPGASDNACRAA----LASFRFRADAALQRVEALSGGQVLRAGLACALGgsdppslLILDep 480
Cdd:COG0419 108 rllgLEIYEELKERLKELEEALESALEELAelqkLKQEILAQLSGLDPIETLSGGERLRLALADLLS-------LILD-- 178
|
170 180
....*....|....*....|....*....
gi 14524463 481 TNHLDIDSIEAVEAGLLSydgaLVVVSHD 509
Cdd:COG0419 179 FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
34-204 |
4.28e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.08 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQG-------------RVALARQILRAGADeTIADvfgatqAVAVlrrAEKG 100
Cdd:PRK11176 374 LVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFND-TIAN------NIAY---ARTE 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 101 DASVEELETAdwtveERIVSALARL-GLEARADTLLNQ----LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRA 175
Cdd:PRK11176 444 QYSREQIEEA-----ARMAYAMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERA 518
|
170 180 190
....*....|....*....|....*....|.
gi 14524463 176 VIGLLSGWRSG--AIVVSHDRELLEEMDAII 204
Cdd:PRK11176 519 IQAALDELQKNrtSLVIAHRLSTIEKADEIL 549
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
116-180 |
4.38e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 42.64 E-value: 4.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 116 ERIVSALARLGLEAR-ADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLL 180
Cdd:PRK11308 132 EKALAMMAKVGLRPEhYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
328-485 |
4.44e-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: 43.36 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 328 ELPAGRQVLAfDGVTAGYDPA-RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTgELPPFKGTVSVN---------- 396
Cdd:TIGR01271 1211 CWPSGGQMDV-QGLTAKYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDgvswnsvtlq 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 397 ---VPFTLLDQSVSILErgETILENfkrLNPGA--SDN---------ACRAALASFRFRADAALqrveaLSGGQVLRAG- 461
Cdd:TIGR01271 1289 twrKAFGVIPQKVFIFS--GTFRKN---LDPYEqwSDEeiwkvaeevGLKSVIEQFPDKLDFVL-----VDGGYVLSNGh 1358
|
170 180
....*....|....*....|....*..
gi 14524463 462 --LAC-ALGGSDPPSLLILDEPTNHLD 485
Cdd:TIGR01271 1359 kqLMClARSILSKAKILLLDEPSAHLD 1385
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-169 |
4.52e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 32 TGLVGRNGIGKTSVLNIIAGtlRPSSGTVAIQGRVALARQIlragaDETIA---------DVFGATQAV-------AVLR 95
Cdd:TIGR00956 792 TALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPL-----DSSFQrsigyvqqqDLHLPTSTVreslrfsAYLR 864
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 96 RAekgdASVEELETADWtVEERIvsalARLGLEARADTLLNQ----LSGGQRTRAVLAAAIFSEPDFLL-LDEPTNNLD 169
Cdd:TIGR00956 865 QP----KSVSKSEKMEY-VEEVI----KLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
349-480 |
4.85e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 41.94 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSL-----VGprrvsVTGPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLD-------------QSVSIL 409
Cdd:COG1137 16 RTVVKDVSLEVnqgeiVG-----LLGPNGAGKTTTFYMIVGLVKPDSGRIFLDgEDITHLPmhkrarlgigylpQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 410 eRGETILENFkrlnpgasdnacRAALASFRFRADAALQRVE-----------------ALSGGQVLRAGLACALGGSdpP 472
Cdd:COG1137 91 -RKLTVEDNI------------LAVLELRKLSKKEREERLEelleefgithlrkskaySLSGGERRRVEIARALATN--P 155
|
....*...
gi 14524463 473 SLLILDEP 480
Cdd:COG1137 156 KFILLDEP 163
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
356-509 |
5.11e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.85 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 356 SFSLVG---PRRVSVT---GPNGSGKTSLLKVVTGELPPfkgtvsvNvpFTLLDQSVS---ILE--RGETILENFKRLnp 424
Cdd:COG1245 87 GFRLYGlpvPKKGKVTgilGPNGIGKSTALKILSGELKP-------N--LGDYDEEPSwdeVLKrfRGTELQDYFKKL-- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 425 gaSDNACRAAL----------------------ASFRFRADAALQR----------VEALSGGQVLR-AGLACALGGSDp 471
Cdd:COG1245 156 --ANGEIKVAHkpqyvdlipkvfkgtvrellekVDERGKLDELAEKlglenildrdISELSGGELQRvAIAAALLRDAD- 232
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14524463 472 psLLILDEPTNHLDIDS-IEAVEA--GLLSYDGALVVVSHD 509
Cdd:COG1245 233 --FYFFDEPSSYLDIYQrLNVARLirELAEEGKYVLVVEHD 271
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
22-192 |
5.22e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 22 DLDLAFGPER-TGLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVALARQILRAGadeTIADVFGAtqavavlrraeKG 100
Cdd:PRK13541 18 DLSITFLPSAiTYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCT---YIGHNLGL-----------KL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 101 DASVEE---LETADWTVEERIVSALARLGLEARADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVI 177
Cdd:PRK13541 84 EMTVFEnlkFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170
....*....|....*...
gi 14524463 178 GLLS-GWRSGAIVV--SH 192
Cdd:PRK13541 164 NLIVmKANSGGIVLlsSH 181
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
336-509 |
5.45e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.84 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 336 LAFDGVTAGYDPaRPIIRDLSFSLVgPRRV-SVTGPNGSGKTSLLKVVTGELPPFKGTVSvnvpFTLLDQS-VSILERGE 413
Cdd:PRK11701 7 LSVRGLTKLYGP-RKGCRDVSFDLY-PGEVlGIVGESGSGKTTLLNALSARLAPDAGEVH----YRMRDGQlRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 414 TILE-------NFKRLNP--------GASDNACRAALAS-----FRFRADAA--LQRVE-----------ALSGGQVLRA 460
Cdd:PRK11701 81 AERRrllrtewGFVHQHPrdglrmqvSAGGNIGERLMAVgarhyGDIRATAGdwLERVEidaariddlptTFSGGMQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 14524463 461 GLACALGGSdpPSLLILDEPTNHLDIdsieAVEAGLL--------SYDGALVVVSHD 509
Cdd:PRK11701 161 QIARNLVTH--PRLVFMDEPTGGLDV----SVQARLLdllrglvrELGLAVVIVTHD 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
338-484 |
6.51e-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: 42.50 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 338 FDGVTAgydparpiIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELP-------------PFK----------GTVS 394
Cdd:TIGR02633 11 FGGVKA--------LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiywsgsPLKasnirdteraGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 395 VNVPFTLLdQSVSILER---GETILENFKRLNPGASDNACRAALASFRFRADAALQRVEALSGGQVLRAGLACALggSDP 471
Cdd:TIGR02633 83 IHQELTLV-PELSVAENiflGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKAL--NKQ 159
|
170
....*....|...
gi 14524463 472 PSLLILDEPTNHL 484
Cdd:TIGR02633 160 ARLLILDEPSSSL 172
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
369-508 |
6.78e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.68 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 369 GPNGSGKTSLLK------------VVTGELP----------------------------PFKGTVSVNVPFTL------- 401
Cdd:PRK14239 38 GPSGSGKSTLLRsinrmndlnpevTITGSIVynghniysprtdtvdlrkeigmvfqqpnPFPMSIYENVVYGLrlkgikd 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 402 ---LDQSVSILERGETILENFK-RLNpgasdnacraalasfrfraDAALqrveALSGGQVLRAGLACALGGSdpPSLLIL 477
Cdd:PRK14239 118 kqvLDEAVEKSLKGASIWDEVKdRLH-------------------DSAL----GLSGGQQQRVCIARVLATS--PKIILL 172
|
170 180 190
....*....|....*....|....*....|...
gi 14524463 478 DEPTNHLDIDSIEAVEAGL--LSYDGALVVVSH 508
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLlgLKDDYTMLLVTR 205
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
315-513 |
7.83e-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: 42.63 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 315 EVLQPFSIRlPRTELPAGRQVLAFDGVT---AGYDParPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKG 391
Cdd:TIGR00957 617 EELEPDSIE-RRTIKPGEGNSITVHNATftwARDLP--PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 392 TVSVNVPFTLLDQSVSIleRGETILENF---KRLNPgasdNACRAALASFRFRADAAL----QRVEA------LSGGQVL 458
Cdd:TIGR00957 694 HVHMKGSVAYVPQQAWI--QNDSLRENIlfgKALNE----KYYQQVLEACALLPDLEIlpsgDRTEIgekgvnLSGGQKQ 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14524463 459 RAGLACAL-GGSDppsLLILDEPTNHLDIDSIEAVEAGLLSYDGAL-----VVVSHDETFL 513
Cdd:TIGR00957 768 RVSLARAVySNAD---IYLFDDPLSAVDAHVGKHIFEHVIGPEGVLknktrILVTHGISYL 825
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-169 |
8.27e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 8.27e-04
10 20 30
....*....|....*....|....*....|..
gi 14524463 138 LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
138-193 |
8.76e-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: 40.25 E-value: 8.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 138 LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR----RAVIGLLSGWRSGAIVVSHD 193
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEEGKKTALVVEHD 131
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-195 |
1.02e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 6 LSALSWSKPDGEHVFsdldlafgpertgLVGRNGIGKTSVLNIIAGTlRPS--SGTVAIQGRvalarqilRAGADETIAD 83
Cdd:PRK10938 276 LHNLSWQVNPGEHWQ-------------IVGPNGAGKSTLLSLITGD-HPQgySNDLTLFGR--------RRGSGETIWD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 84 V--------------------------------FGATQAVAvlrraekgDAsvEELETADWtveerivsaLARLGLEAR- 130
Cdd:PRK10938 334 IkkhigyvssslhldyrvstsvrnvilsgffdsIGIYQAVS--------DR--QQKLAQQW---------LDILGIDKRt 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 131 ADTLLNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGR----RAVIGLLSGWRSGAIVVSHDRE 195
Cdd:PRK10938 395 ADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRqlvrRFVDVLISEGETQLLFVSHHAE 463
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
138-169 |
1.06e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.91 E-value: 1.06e-03
10 20 30
....*....|....*....|....*....|..
gi 14524463 138 LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
352-380 |
1.20e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 1.20e-03
10 20 30
....*....|....*....|....*....|
gi 14524463 352 IRDLSFSLVGPRRVSV-TGPNGSGKTSLLK 380
Cdd:COG3950 14 FEDLEIDFDNPPRLTVlVGENGSGKTTLLE 43
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
25-193 |
1.46e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 25 LAFGPERTGLVGRNGIGKTSVLNIIAGTLrpssgTVAIQGRVALARQILRAGADETIADV-FGATQAVAVLRRA------ 97
Cdd:COG0419 19 IDFDDGLNLIVGPNGAGKSTILEAIRYAL-----YGKARSRSKLRSDLINVGSEEASVELeFEHGGKRYRIERRqgefae 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 98 -------------------EKGDASVEELETADWTVEERIVSALARLGLEARADTLL------NQLSGGQRTRAVLAAAI 152
Cdd:COG0419 94 fleakpserkealkrllglEIYEELKERLKELEEALESALEELAELQKLKQEILAQLsgldpiETLSGGERLRLALADLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 14524463 153 fsepdFLLLDepTNNLDRDGRRAVIGLLsgwrSGAIVVSHD 193
Cdd:COG0419 174 -----SLILD--FGSLDEERLERLLDAL----EELAIITHV 203
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
135-204 |
1.75e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 1.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 135 LNQLSGGQRTRAVLAA--AIFS-EPD-FLLLDEPTNNLDRDGRRAVIGLLSGWRSGA--IVVSHDRELLEEMDAII 204
Cdd:pfam02463 1075 LDLLSGGEKTLVALALifAIQKyKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAqfIVISLREEMLEKADKLV 1150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
69-169 |
1.88e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 69 ARQILRAGADETIADVFGATQAVAVLRrAEKGDASVEELETADwtVEERIVSALARLGLEARADTLL----NQLSGGQRT 144
Cdd:PTZ00265 510 KRNSCRAKCAGDLNDMSNTTDSNELIE-MRKNYQTIKDSEVVD--VSKKVLIHDFVSALPDKYETLVgsnaSKLSGGQKQ 586
|
90 100
....*....|....*....|....*
gi 14524463 145 RAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PTZ00265 587 RISIARAIIRNPKILILDEATSSLD 611
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
115-169 |
2.06e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 40.58 E-value: 2.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 115 EERIVSALARLGLEARADTL-LNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:TIGR02633 380 LQIIGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
33-68 |
2.13e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 2.13e-03
10 20 30
....*....|....*....|....*....|....*.
gi 14524463 33 GLVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGRVAL 68
Cdd:PRK13546 54 GLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV 89
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
451-506 |
2.25e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 14524463 451 ALSGGQVLRAGLACAL-GGSDPPSLLILDEPTNHLDIDSIEAVEAGLLS--YDGALVVV 506
Cdd:PRK00635 809 SLSGGEIQRLKLAYELlAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSltHQGHTVVI 867
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-104 |
2.39e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.51 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 29 PERTGLVGRNGIGKTSVLNIIAGTLRPSSGTVAI----QGRVALARQILRAGADETIADVFGATQAVAVLRRAEKGDASV 104
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYidgeDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
453-528 |
2.72e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 40.07 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 453 SGGQVLRAGLACALggSDPPSLLILDEPTNHLDIdSIEA----------VEAGLlsydgALVVVSHDETFLANIG----- 517
Cdd:PRK15079 163 SGGQCQRIGIARAL--ILEPKLIICDEPVSALDV-SIQAqvvnllqqlqREMGL-----SLIFIAHDLAVVKHISdrvlv 234
|
90
....*....|...
gi 14524463 518 --IGTRVELSTSR 528
Cdd:PRK15079 235 myLGHAVELGTYD 247
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
349-489 |
3.26e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 39.49 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTVSVNvpftllDQSVSIL------ERGETILEN---- 418
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID------DEDISLLplharaRRGIGYLPQeasi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 419 FKRLNpgASDN-----ACRAALASFRfRADAALQRVE-------------ALSGGQVLRAGLACALGGSdpPSLLILDEP 480
Cdd:PRK10895 90 FRRLS--VYDNlmavlQIRDDLSAEQ-REDRANELMEefhiehlrdsmgqSLSGGERRRVEIARALAAN--PKFILLDEP 164
|
....*....
gi 14524463 481 TNHLDIDSI 489
Cdd:PRK10895 165 FAGVDPISV 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
337-481 |
3.37e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.00 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 337 AFDGVTAgydparpiIRDLSFSLvgpRRVSVT---GPNGSGKTSLLKVVTGELPPFKGTVSVN-VPFTLLD--------- 403
Cdd:COG1129 13 SFGGVKA--------LDGVSLEL---RPGEVHallGENGAGKSTLMKILSGVYQPDSGEILLDgEPVRFRSprdaqaagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 404 ----QSVSILErGETILEN---------FKRLNPGASDNACRAALASFRFRADAAlQRVEALSGGQ---VLragLACALg 467
Cdd:COG1129 82 aiihQELNLVP-NLSVAENiflgreprrGGLIDWRAMRRRARELLARLGLDIDPD-TPVGDLSVAQqqlVE---IARAL- 155
|
170
....*....|....
gi 14524463 468 gSDPPSLLILDEPT 481
Cdd:COG1129 156 -SRDARVLILDEPT 168
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
123-206 |
3.40e-03 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.16 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 123 ARLGLEARADTLLN-------------QLSGGQRTRAVLAAAIFSEPDFLL--LDEPTNNL-DRDGRRaVIGLLSGWR-- 184
Cdd:cd03270 110 ARVGIRERLGFLVDvglgyltlsrsapTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLhPRDNDR-LIETLKRLRdl 188
|
90 100
....*....|....*....|...
gi 14524463 185 -SGAIVVSHDRELLEEMDAIIEL 206
Cdd:cd03270 189 gNTVLVVEHDEDTIRAADHVIDI 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
137-193 |
3.40e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 39.25 E-value: 3.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14524463 137 QLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLSGWRSGA----IVVSHD 193
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeltmVIVSHN 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
349-393 |
3.69e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 38.78 E-value: 3.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 14524463 349 RPIIRDLSFSLVGPRRVSVTGPNGSGKTSLLKVVTGELPPFKGTV 393
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEI 58
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
33-169 |
4.81e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14524463 33 GLVGRngiGKTSVLNIIAGTLR-PSSGTVAIQGRVALAR---QILRAGadetIADV--------------FGATQAVAVL 94
Cdd:PRK13549 295 GLVGA---GRTELVQCLFGAYPgRWEGEIFIDGKPVKIRnpqQAIAQG----IAMVpedrkrdgivpvmgVGKNITLAAL 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14524463 95 RRAEKGDASVEELEtadwtvEERIVSALARLGLEARADTL-LNQLSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLD 169
Cdd:PRK13549 368 DRFTGGSRIDDAAE------LKTILESIQRLKVKTASPELaIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
138-193 |
6.08e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 38.61 E-value: 6.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 14524463 138 LSGGQRTRAVLAAAIFSEPDFLLLDEPTNNLDRDGRRAVIGLLS--GWRSGAIVVSHD 193
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHelKEQYTIIIVTHN 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-65 |
9.09e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 38.49 E-value: 9.09e-03
10 20 30
....*....|....*....|....*....|..
gi 14524463 34 LVGRNGIGKTSVLNIIAGTLRPSSGTVAIQGR 65
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN 73
|
|
| |
