|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-492 |
2.77e-128 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 385.57 E-value: 2.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHlPDELHQQTLLD----------AL 89
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQE-PPLDDDLTVLDtvldgdaelrAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 LARLPEAERESS--------------------AW----RAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPD 145
Cdd:COG0488 93 EAELEELEAKLAepdedlerlaelqeefealgGWeaeaRAEEILSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 146 LLLLDEPGNHLDLPTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLPCT------QARAALAARDE 219
Cdd:COG0488 173 LLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSayleqrAERLEQEAAAY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 220 SDALRHKAEQKE-IDRVTASAKRlatwgqvydnedlARKAKQMEKQVARLKEEQTELAQGSRwRLTLSGDALAADRLLEL 298
Cdd:COG0488 253 AKQQKKIAKEEEfIRRFRAKARK-------------AKQAQSRIKALEKLEREEPPRRDKTV-EIRFPPPERLGKKVLEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 299 ENLAVSaAPDTPTL--FTLplaRLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP--G-VTFHPRVSLGYYDQSLHQ 373
Cdd:COG0488 319 EGLSKS-YGDKTLLddLSL---RIDRGDRIGLIGPNGAGKSTLLKLL-----AGELEPdsGtVKLGETVKIGYFDQHQEE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 374 LPDNATLLEALEPFAPELQQRKLA--LISAGFPWARHGQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKE 451
Cdd:COG0488 390 LDPDKTVLDELRDGAPGGTEQEVRgyLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLE 469
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 495164891 452 ALAQTLQTFEGGLLLVTHDRTLMEASCNRFWLVEDGGLSEW 492
Cdd:COG0488 470 ALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-487 |
3.21e-55 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 197.31 E-value: 3.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLP--DELHQQTLLD------ALLA 91
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPalPQPALEYVIDgdreyrQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 92 RLPEAERES---------------SAW----RAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:PRK10636 97 QLHDANERNdghaiatihgkldaiDAWtirsRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 153 GNHLDLPTMLWLEQFLARWNGSFILVSHDSALLDSVTNRtwILRDGQLQAFDLPCT-----QARAALAARDESdALRHKA 227
Cdd:PRK10636 177 TNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDK--IIHIEQQSLFEYTGNyssfeVQRATRLAQQQA-MYESQQ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 228 E-----QKEIDRVTASAKrlatwgqvydnedlarKAKQMEKQVARLkeEQTELAQGSR----WRLTLSGDALAADRLLEL 298
Cdd:PRK10636 254 ErvahlQSYIDRFRAKAT----------------KAKQAQSRIKML--ERMELIAPAHvdnpFHFSFRAPESLPNPLLKM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 299 ENlaVSAAPDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP---GVTFHPRVSLGYYDQslHQLP 375
Cdd:PRK10636 316 EK--VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL-----AGELAPvsgEIGLAKGIKLGYFAQ--HQLE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 376 ---DNATLLEALEPFAPELQQRKLALISAGFPWarHGQRV----DTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDME 448
Cdd:PRK10636 387 flrADESPLQHLARLAPQELEQKLRDYLGGFGF--QGDKVteetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
490 500 510
....*....|....*....|....*....|....*....
gi 495164891 449 GKEALAQTLQTFEGGLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:PRK10636 465 MRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDG 503
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
30-500 |
8.49e-52 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 185.48 E-value: 8.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 30 GDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQhlpDEL--HQQTLLDALLA---------------- 91
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQ---DQFafEEFTVLDTVIMghtelwevkqerdriy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 92 RLPEAERE------------------SSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPG 153
Cdd:PRK15064 104 ALPEMSEEdgmkvadlevkfaemdgyTAEARAGELLLGVGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 154 NHLDLPTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFD-------LPCTQARAALAArdesDALRHK 226
Cdd:PRK15064 184 NNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPgnydeymTAATQARERLLA----DNAKKK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 227 AEQKE----IDRVTASAK--RLATwgqvydnedlaRKAKQMEKqvarLKEEqtELAQGSRWR--LTLSGDALAADRLLEL 298
Cdd:PRK15064 260 AQIAElqsfVSRFSANASkaKQAT-----------SRAKQIDK----IKLE--EVKPSSRQNpfIRFEQDKKLHRNALEV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 299 ENLavSAAPDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP---GVTFHPRVSLGYYDQ-SLHQL 374
Cdd:PRK15064 323 ENL--TKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-----VGELEPdsgTVKWSENANIGYYAQdHAYDF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 375 PDNATLLEALEPFAPEL---QQRKLALISAGFPWARHGQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKE 451
Cdd:PRK15064 396 ENDLTLFDWMSQWRQEGddeQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIE 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 495164891 452 ALAQTLQTFEGGLLLVTHDRTLMEASCNRFWLVEDGGLSEWH-NMEALLA 500
Cdd:PRK15064 476 SLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSgTYEEYLR 525
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-492 |
3.04e-50 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 183.23 E-value: 3.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLP-------------------- 77
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPrnvegtvydfvaegieeqae 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 78 --DELHQQTLLDAL---------LARLPEAERESSAW----RAQALLANMGF-AEAAWSltagSLSGGQHTRLLLARALI 141
Cdd:PRK11147 97 ylKRYHDISHLVETdpseknlneLAKLQEQLDHHNLWqlenRINEVLAQLGLdPDAALS----SLSGGWLRKAALGRALV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 142 ISPDLLLLDEPGNHLDLPTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFdlPCTQArAALAARDEsd 221
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSY--PGNYD-QYLLEKEE-- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 222 ALRHKAEQK-EIDRVTAS----------AKRLATWGQVYdnedlARKAKQMEKQvARLKEEQT---ELAQGSRwrltlSG 287
Cdd:PRK11147 248 ALRVEELQNaEFDRKLAQeevwirqgikARRTRNEGRVR-----ALKALRRERS-ERREVMGTakmQVEEASR-----SG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 288 DALaadrlLELENlaVSAAPDTPTL---FTLPLARlksGDRVALLGHNGCGKSSLLRLLWRQWQ--TGETVPGVtfhpRV 362
Cdd:PRK11147 317 KIV-----FEMEN--VNYQIDGKQLvkdFSAQVQR---GDKIALIGPNGCGKTTLLKLMLGQLQadSGRIHCGT----KL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 363 SLGYYDQSLHQLPDNATLLEALEPFAPEL----QQRKLA--LISAGFPWARHGQRVDTLSGGERSRLLFVGLSLARYSLL 436
Cdd:PRK11147 383 EVAYFDQHRAELDPEKTVMDNLAEGKQEVmvngRPRHVLgyLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLL 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 495164891 437 MLDEPTNHLDMEGKEALAQTLQTFEGGLLLVTHDRTLMEASCNRFWLVE-DGGLSEW 492
Cdd:PRK11147 463 ILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRY 519
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-471 |
1.04e-49 |
|
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: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTlkKGDRIGLIGHNGCGKSTLLKAL-------DGTLAPAEGV---------VTRAARCLLARVEQHLPDELHQQTLL 86
Cdd:TIGR03719 26 LSFF--PGAKIGVLGLNGAGKSTLLRIMagvdkdfNGEARPQPGIkvgylpqepQLDPTKTVRENVEEGVAEIKDALDRF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 DALLARL--PEAERESSAWRaQALLANMGFAEAAWSL------------------TAGSLSGGQHTRLLLARALIISPDL 146
Cdd:TIGR03719 104 NEISAKYaePDADFDKLAAE-QAELQEIIDAADAWDLdsqleiamdalrcppwdaDVTKLSGGERRRVALCRLLLSKPDM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 147 LLLDEPGNHLDLPTMLWLEQFLARWNGSFILVSHDSALLDSVTNrtWILR--DGQLQAFD------LPCTQARAALAARD 218
Cdd:TIGR03719 183 LLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILEldRGRGIPWEgnysswLEQKQKRLEQEEKE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 219 ESDalRHKAEQKEIDRVTASAKrlatwgqvydnedlARKAK---------QMEKQVARLKEEQTEL--AQGSRwrltLSG 287
Cdd:TIGR03719 261 ESA--RQKTLKRELEWVRQSPK--------------GRQAKskarlaryeELLSQEFQKRNETAEIyiPPGPR----LGD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 288 DALAA--------DRLLeLENLAvsaapdtptlFTLPlarlkSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP---GV 356
Cdd:TIGR03719 321 KVIEAenltkafgDKLL-IDDLS----------FKLP-----PGGIVGVIGPNGAGKSTLFRMI-----TGQEQPdsgTI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 357 TFHPRVSLGYYDQSLHQLPDNATLLEALEPFAPELQQRKL-----ALISA-GFPWARHGQRVDTLSGGERSRLLFVGLSL 430
Cdd:TIGR03719 380 EIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKLGKReipsrAYVGRfNFKGSDQQKKVGQLSGGERNRVHLAKTLK 459
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 495164891 431 ARYSLLMLDEPTNHLDMEGKEALAQTLQTFEGGLLLVTHDR 471
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDR 500
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-493 |
1.37e-48 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 180.06 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLK-----ALDG------TLAPAEGVV---TRAARCLL-ARVE--QHLPDELH- 81
Cdd:PLN03073 193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGipkncqILHVEQEVVgddTTALQCVLnTDIErtQLLEEEAQl 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 82 --QQTLL-------------------DALLARLPEAERE-------SSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTR 133
Cdd:PLN03073 273 vaQQRELefetetgkgkgankdgvdkDAVSQRLEEIYKRlelidayTAEARAASILAGLSFTPEMQVKATKTFSGGWRMR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 134 LLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFdlpctqaraa 213
Cdd:PLN03073 353 IALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTY---------- 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 214 laardesdalrhKAEQKEIDRVtaSAKRLATWGQVYDNEDLARKAKQMEKQVARLKEEQTELAQGSRWRLTLSG--DALA 291
Cdd:PLN03073 423 ------------KGDYDTFERT--REEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGhvDAVV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 292 ADRLLELEN-----------LAVSAA----PDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP-- 354
Cdd:PLN03073 489 NDPDYKFEFptpddrpgppiISFSDAsfgyPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI-----SGELQPss 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 355 GVTFH-PRVSLGYYDQslHQ-----LPDNATL-LEALEPFAPElQQRKLALISAGFPWARHGQRVDTLSGGERSRLLFVG 427
Cdd:PLN03073 564 GTVFRsAKVRMAVFSQ--HHvdgldLSSNPLLyMMRCFPGVPE-QKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAK 640
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 428 LSLARYSLLMLDEPTNHLDMEGKEALAQTLQTFEGGLLLVTHDRTLMEASCNRFWLVEDGGLSEWH 493
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFH 706
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-204 |
1.45e-48 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 176.41 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLpDELH-QQTLLDALLARLPEAERESs 101
Cdd:COG0488 334 LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDpDKTVLDELRDGAPGGTEQE- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 102 awrAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNGSFILVSHD 181
Cdd:COG0488 412 ---VRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHD 488
|
170 180
....*....|....*....|...
gi 495164891 182 SALLDSVTNRTWILRDGQLQAFD 204
Cdd:COG0488 489 RYFLDRVATRILEFEDGGVREYP 511
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
20-199 |
3.33e-47 |
|
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: 161.85 E-value: 3.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQhlpdelhqqtlldallarlpeaere 99
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 100 ssawraqallanmgfaeaawsltagsLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNGSFILVS 179
Cdd:cd03221 71 --------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVS 124
|
170 180
....*....|....*....|
gi 495164891 180 HDSALLDSVTNRTWILRDGQ 199
Cdd:cd03221 125 HDRYFLDQVATKIIELEDGK 144
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-471 |
2.78e-43 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 162.60 E-value: 2.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 30 GDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRA----------------ARCLLARVEQHLPDELHQQTLLDALLARL 93
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApgikvgylpqepqldpEKTVRENVEEGVAEVKAALDRFNEIYAAY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 94 PEAERESsawraQALLANMGFAEA------AWSLTA------------------GSLSGGQHTRLLLARALIISPDLLLL 149
Cdd:PRK11819 113 AEPDADF-----DALAAEQGELQEiidaadAWDLDSqleiamdalrcppwdakvTKLSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 150 DEPGNHLDLPTMLWLEQFLARWNGSFILVSHDSALLDSVTNrtWIL---RdGQLQAFD------LPCTQARAALAARDES 220
Cdd:PRK11819 188 DEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILeldR-GRGIPWEgnysswLEQKAKRLAQEEKQEA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 221 DalRHKAEQKEIDRVTASAKrlatwgqvydnedlARKAK---------QMEKQVARLKEEQTEL--AQGSRwrltLSGDA 289
Cdd:PRK11819 265 A--RQKALKRELEWVRQSPK--------------ARQAKskarlaryeELLSEEYQKRNETNEIfiPPGPR----LGDKV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 290 LAA--------DRLLeLENLAvsaapdtptlFTLPlarlkSGDRVALLGHNGCGKSSLLRLLWRQWQ--TGETVPGVTfh 359
Cdd:PRK11819 325 IEAenlsksfgDRLL-IDDLS----------FSLP-----PGGIVGIIGPNGAGKSTLFKMITGQEQpdSGTIKIGET-- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 360 prVSLGYYDQSLHQLPDNATLLEALEPFAPELQ--QRKL---ALISA-GFPWARHGQRVDTLSGGERSRllfvgLSLARY 433
Cdd:PRK11819 387 --VKLAYVDQSRDALDPNKTVWEEISGGLDIIKvgNREIpsrAYVGRfNFKGGDQQKKVGVLSGGERNR-----LHLAKT 459
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 495164891 434 -----SLLMLDEPTNHLDMEGKEALAQTLQTFEGGLLLVTHDR 471
Cdd:PRK11819 460 lkqggNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDR 502
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
319-488 |
5.64e-38 |
|
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: 136.81 E-value: 5.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVPG---VTFHPRVSLGYYDQslhqlpdnatllealepfapelqqrk 395
Cdd:cd03221 22 TINPGDRIGLVGRNGAGKSTLLKLI-----AGELEPDegiVTWGSTVKIGYFEQ-------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 396 lalisagfpwarhgqrvdtLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQTFEGGLLLVTHDRTLME 475
Cdd:cd03221 71 -------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLD 131
|
170
....*....|...
gi 495164891 476 ASCNRFWLVEDGG 488
Cdd:cd03221 132 QVATKIIELEDGK 144
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-219 |
1.55e-29 |
|
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: 116.28 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQHlPDelHQ---QTL 85
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdgkditkknlRELRRKVGLVFQN-PD--DQlfaPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LD----ALLAR-LPEAERESsawRAQALLANMG---FAEAAWSltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:COG1122 94 EEdvafGPENLgLPREEIRE---RVEEALELVGlehLADRPPH----ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495164891 158 LPTMLWLEQFLARWNG---SFILVSHDSALLDSVTNRTWILRDGQLQAFDLPctqaRAALAARDE 219
Cdd:COG1122 167 PRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP----REVFSDYEL 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-200 |
5.99e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.14 E-value: 5.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 5 LTAHSLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLlarvEQHLPDELHQQ- 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL----SAMPPPEWRRQv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 ------------TLLDALLARLPEAERESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDE 151
Cdd:COG4619 77 ayvpqepalwggTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495164891 152 PGNHLDLPTMLWLEQFLARW----NGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:COG4619 157 PTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-203 |
3.57e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 110.99 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarcllarveqhlpdelhqqTLLDALLARLPEAER- 98
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI----------------------LLDGKDLASLSPKELa 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 99 ESSAWRAQAL-LANM-GFAEAAWSltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNGSF- 175
Cdd:cd03214 73 RKIAYVPQALeLLGLaHLADRPFN----ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERg 148
|
170 180 190
....*....|....*....|....*....|.
gi 495164891 176 ---ILVSHDSALLDSVTNRTWILRDGQLQAF 203
Cdd:cd03214 149 ktvVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-199 |
4.37e-28 |
|
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: 111.79 E-value: 4.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLAR-----------VEQHlPDelHQ---QTL 85
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLslkelrrkvglVFQN-PD--DQffgPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LD----ALLAR-LPEAERESsawRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:cd03225 94 EEevafGLENLgLPEEEIEE---RVEEALELVGLEGLRDRSPF-TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495164891 161 MLWLEQFLARWNG---SFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:cd03225 170 RRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-152 |
5.99e-28 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 109.27 E-value: 5.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDE---LHQQTLLD--------- 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEigyVFQDPQLFprltvrenl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 88 ---ALLARLPEAERESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:pfam00005 81 rlgLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-225 |
3.05e-27 |
|
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: 110.28 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQHLPDELH-QQTLLD 87
Cdd:COG1124 21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpvtrrrrKAFRRRVQMVFQDPYASLHpRHTVDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 AL-----LARLPEAERessawRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT-- 160
Cdd:COG1124 101 ILaeplrIHGLPDREE-----RIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqa 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495164891 161 -ML-WLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAfdlpcTQARAALAARDESDALRH 225
Cdd:COG1124 176 eILnLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVE-----ELTVADLLAGPKHPYTRE 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-204 |
6.52e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.00 E-value: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------RAARCLLARV-----EQHLPDELhqqTLLD 87
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvaRDPAEVRRRIgyvpqEPALYPDL---TVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 AL-----LARLPEAERESsawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTML 162
Cdd:COG1131 93 NLrffarLYGLPRKEARE---RIDELLELFGLTDAA-DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495164891 163 WLEQFLARWNG---SFILVSHDSALLDSVTNRTWILRDGQLQAFD 204
Cdd:COG1131 169 ELWELLRELAAegkTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-206 |
1.35e-26 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 108.59 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 4 LLTAHSLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARV 72
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslsrRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 73 EQHLPDELHqQTLLDA-LLARLPEA---ERESSAWRAQAL--LANMG---FAEAAWSltagSLSGGQHTRLLLARALIIS 143
Cdd:COG1120 81 PQEPPAPFG-LTVRELvALGRYPHLglfGRPSAEDREAVEeaLERTGlehLADRPVD----ELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495164891 144 PDLLLLDEPGNHLDLP----TMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:COG1120 156 PPLLLLDEPTSHLDLAhqleVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-279 |
1.42e-26 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 114.50 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDELHQQTLLDALLARLPEAERE 99
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLARLAPQELE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 100 SsawRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNGSFILVS 179
Cdd:PRK10636 408 Q---KLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVS 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 180 HDSALLDSVTNRTWILRDGQLQAF--DLPCTQARAALAARDESDAlrhKAEQKEIDRVTASAKR--------LATWGQVY 249
Cdd:PRK10636 485 HDRHLLRSTTDDLYLVHDGKVEPFdgDLEDYQQWLSDVQKQENQT---DEAPKENNANSAQARKdqkrreaeLRTQTQPL 561
|
250 260 270
....*....|....*....|....*....|
gi 495164891 250 DNEdLARKAKQMEKQVARLKEEQTELAQGS 279
Cdd:PRK10636 562 RKE-IARLEKEMEKLNAQLAQAEEKLGDSE 590
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-200 |
1.53e-26 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 105.94 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTraarcllarveqhlpdelhqqtLLDALLARLPEAERE 99
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK----------------------VLGKDIKKEPEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 100 SSAWraqaLLANMGFAeaaWSLTAG---SLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQF---LARWNG 173
Cdd:cd03230 74 RIGY----LPEEPSLY---ENLTVRenlKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELlreLKKEGK 146
|
170 180
....*....|....*....|....*..
gi 495164891 174 SFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:cd03230 147 TILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-200 |
1.66e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQ--HLPdelhQQTLLDA--------- 88
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigYVP----QRAEVDWdfpitvrdv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 ----------LLARLPEAEREssawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL 158
Cdd:COG1121 98 vlmgrygrrgLFRRPSRADRE----AVDEALERVGLEDLA-DRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495164891 159 PTMLWLEQFLARWNG---SFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:COG1121 173 ATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-199 |
3.84e-26 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 104.63 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 6 TAHSLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcllarveqhlpdelhqqtl 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 ldALLARLPEAERESSAWRAQallanmgfaeaawsltagsLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLE 165
Cdd:cd00267 62 --DIAKLPLEELRRRIGYVPQ-------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLL 120
|
170 180 190
....*....|....*....|....*....|....*..
gi 495164891 166 QFLARWNG---SFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:cd00267 121 ELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-508 |
1.11e-25 |
|
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: 110.76 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRIDSPFGPE--LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGtLAPAEGVVT---------------- 62
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVpaVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISgevlldgrdllelsea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 63 -RAARCllARVEQHLPDELHQQTLLD--ALLARLPEAERESSAWRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARA 139
Cdd:COG1123 80 lRGRRI--GMVFQDPMTQLNPVTVGDqiAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-QLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 140 LIISPDLLLLDEPGNHLDLPT----MLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQafdlpctqaraala 215
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV-------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 216 ardesdalrhkaEQKEIDRVTASAKRLATWGQVYDNEDLARKAKQmekqvarlkeeqtelaqgsrwrltlsgdalAADRL 295
Cdd:COG1123 223 ------------EDGPPEEILAAPQALAAVPRLGAARGRAAPAAA------------------------------AAEPL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTLFTlplA------RLKSGDRVALLGHNGCGKSSLLRLLWR--QWQTGEtvpgVTFHPRVSLGYY 367
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVR---AvddvslTLRRGETLGLVGESGSGKSTLARLLLGllRPTSGS----ILFDGKDLTKLS 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 368 DQSLHQL----------PDNA-----TLLEAL-EPF-------APELQQRKLALISA-GFPwARHGQR-VDTLSGGERSR 422
Cdd:COG1123 334 RRSLRELrrrvqmvfqdPYSSlnprmTVGDIIaEPLrlhgllsRAERRERVAELLERvGLP-PDLADRyPHELSGGQRQR 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 423 llfvgLSLARY-----SLLMLDEPTNHLDMEGKEALAQTL----QTFEGGLLLVTHDRTLMEASCNRFWLVEDGGLSEWH 493
Cdd:COG1123 413 -----VAIARAlalepKLLILDEPTSALDVSVQAQILNLLrdlqRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
570
....*....|....*
gi 495164891 494 NMEALLARLRAAPTQ 508
Cdd:COG1123 488 PTEEVFANPQHPYTR 502
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
20-202 |
1.02e-24 |
|
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: 103.01 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT----------RAARCLLARV--EQHLPDELhqqTLLD 87
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepREARRQIGVLpdERGLYDRL---TVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 --ALLARLPEAERESSAWRAQALLANMGFAEAAWSLTAGsLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLE 165
Cdd:COG4555 94 niRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGE-LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495164891 166 QFLARW---NGSFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:COG4555 173 EILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-271 |
1.24e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 108.50 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDELHQQTLLDALLARLPEAERESSAW 103
Cdd:PRK11147 339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNLAEGKQEVMVNGRPR 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 104 RAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNGSFILVSHDSA 183
Cdd:PRK11147 419 HVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQ 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 184 LLDSVTNRTWILR-DGQLQAF-----DLPCTQARaALAARDESDALRHKAEQKEIDRVTASAKRLaTWGQVYDNEDLARK 257
Cdd:PRK11147 499 FVDNTVTECWIFEgNGKIGRYvggyhDARQQQAQ-YLALKQPAVKKKEEAAAPKAETVKRSSKKL-SYKLQRELEQLPQL 576
|
250
....*....|....
gi 495164891 258 AKQMEKQVARLKEE 271
Cdd:PRK11147 577 LEDLEAEIEALQAQ 590
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
23-188 |
4.25e-24 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 100.25 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQH------------LPDELhqqTLLDAL- 89
Cdd:COG4133 21 LSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrrlaylghadgLKPEL---TVRENLr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 -LARLpeAERESSAWRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFL 168
Cdd:COG4133 98 fWAAL--YGLRADREAIDEALEAVGLAGLA-DLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
170 180
....*....|....*....|...
gi 495164891 169 ARWN---GSFILVSHDSALLDSV 188
Cdd:COG4133 175 AAHLargGAVLLTTHQPLELAAA 197
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-200 |
1.90e-23 |
|
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: 98.48 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV----------TRAARCLLarVEQHLPDELHQQTLLDAL 89
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikakERRKSIGY--VMQDVDYQLFTDSVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 LARLPEAEResSAWRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTM-----LWL 164
Cdd:cd03226 94 LLGLKELDA--GNEQAETVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMervgeLIR 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 495164891 165 EqfLARWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:cd03226 171 E--LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-200 |
2.08e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 95.36 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT----------RAARCLLARVEQH-LPDEL--HQQTLL 86
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqkniEALRRIGALIEAPgFYPNLtaRENLRL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 DALLARLPEAeressawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQ 166
Cdd:cd03268 96 LARLLGIRKK-------RIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRE 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 495164891 167 FLARWN---GSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:cd03268 168 LILSLRdqgITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-203 |
2.67e-22 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 101.48 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 15 PFGPEL-NALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDELHQQTLLDALLAR- 92
Cdd:PLN03073 519 PGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRc 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 93 ---LPEaeressawraQALLANMGFAEAAWSLTAGS---LSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQ 166
Cdd:PLN03073 599 fpgVPE----------QKLRAHLGSFGVTGNLALQPmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ 668
|
170 180 190
....*....|....*....|....*....|....*..
gi 495164891 167 FLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAF 203
Cdd:PLN03073 669 GLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPF 705
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-202 |
3.73e-22 |
|
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: 95.05 E-value: 3.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLK-----KGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLL-ARVEQHLPDE------LHQQ-TLLDALL 90
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdSRKKINLPPQqrkiglVFQQyALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 91 AR------LPEAERESSAWRAQALLANMGFAEAAWSLTAGsLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWL 164
Cdd:cd03297 92 VRenlafgLKRKRNREDRISVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495164891 165 EQFL----ARWNGSFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:cd03297 171 LPELkqikKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-202 |
6.39e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 95.15 E-value: 6.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEG-VVT----RAARCLLARVEQHL----PdELHQQ-----TL 85
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgeRRGGEDVWELRKRIglvsP-ALQLRfprdeTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LDALL----------ARLPEAEREssawRAQALLANMG---FAEAAWsltaGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:COG1119 98 LDVVLsgffdsiglyREPTDEQRE----RARELLELLGlahLADRPF----GTLSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495164891 153 GNHLDLPTMLWLEQFLARWNGS----FILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEgaptLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
20-207 |
7.22e-22 |
|
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: 94.94 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT--------------RAARCLLARVEQH--LPDE---- 79
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklkgkalRQLRRQIGMIFQQfnLIERlsvl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 80 -------LHQQTLLDALLARLPEAEREssawRAQALLANMGFAEAAWSlTAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:cd03256 97 envlsgrLGRRSTWRSLFGLFPKEEKQ----RALAALERVGLLDKAYQ-RADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 153 GNHLDLPT----MLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLqAFDLPC 207
Cdd:cd03256 172 VASLDPASsrqvMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI-VFDGPP 229
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-200 |
7.40e-22 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 94.49 E-value: 7.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDELHQ----------------- 82
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRKEiqmvfqdpmsslnprmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 83 --QTLLDALLARLPEAERESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:cd03257 101 igEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 161 ----MLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:cd03257 181 qaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-202 |
7.83e-22 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 94.34 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRIDSPFGPE----LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT----------RAAR 66
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidgqdisslsEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 67 CLLAR-----VEQ--HLPDELhqqTLLD-----ALLARLPEAERESsawRAQALLANMGFAEAAwSLTAGSLSGGQHTRL 134
Cdd:COG1136 81 ARLRRrhigfVFQffNLLPEL---TALEnvalpLLLAGVSRKERRE---RARELLERVGLGDRL-DHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164891 135 LLARALIISPDLLLLDEP-GNhLDLPT----MLWLEQFLARWNGSFILVSHDSALLdSVTNRTWILRDGQLQA 202
Cdd:COG1136 154 AIARALVNRPKLILADEPtGN-LDSKTgeevLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-181 |
8.06e-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: 94.43 E-value: 8.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV------------TRAARCLLARVEQH--LPDEL----- 80
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditglppHEIARLGIGRTFQIprLFPELtvlen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 81 -----HQQTLLDALLARLPEAERESSAwRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPG-- 153
Cdd:cd03219 96 vmvaaQARTGSGLLLARARREEREARE-RAEELLERVGLADLA-DRPAGELSYGQQRRLEIARALATDPKLLLLDEPAag 173
|
170 180
....*....|....*....|....*....
gi 495164891 154 -NHLDLPTMLWLEQFLARWNGSFILVSHD 181
Cdd:cd03219 174 lNPEETEELAELIRELRERGITVLLVEHD 202
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
20-217 |
1.00e-21 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 94.74 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT--------------RAARCLLARVEQH--LPDE---- 79
Cdd:COG3638 19 LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvdgqdvtalrgralRRLRRRIGMIFQQfnLVPRlsvl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 80 -------LHQQTLLDALLARLPEAEREssawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:COG3638 99 tnvlagrLGRTSTWRSLLGLFPPEDRE----RALEALERVGLADKAYQR-ADQLSGGQQQRVAIARALVQEPKLILADEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 153 GNHLDLPT----MLWLEQfLARWNGSFILVS-HDSALLDSVTNRTWILRDGQLqAFDLPCTQARAALAAR 217
Cdd:COG3638 174 VASLDPKTarqvMDLLRR-IAREDGITVVVNlHQVDLARRYADRIIGLRDGRV-VFDGPPAELTDAVLRE 241
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-181 |
2.47e-21 |
|
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: 92.60 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQ--HLPdelhQQTLLDA--------- 88
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVP----QRRSIDRdfpisvrdv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 ----------LLARLPEAEREssawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL 158
Cdd:cd03235 91 vlmglyghkgLFRRLSKADKA----KVDEALERVGLSELA-DRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180
....*....|....*....|....*.
gi 495164891 159 PTMLWLEQFLARWNG---SFILVSHD 181
Cdd:cd03235 166 KTQEDIYELLRELRRegmTILVVTHD 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-185 |
5.58e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQH--LPDELhQQTLLDA------- 88
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRseVPDSL-PLTVRDLvamgrwa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 ---LLARLPEAEREssawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLE 165
Cdd:NF040873 85 rrgLWRRLTRDDRA----AVDDALERVGLADLA-GRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180
....*....|....*....|...
gi 495164891 166 QFLARWNG---SFILVSHDSALL 185
Cdd:NF040873 160 ALLAEEHArgaTVVVVTHDLELV 182
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-181 |
8.40e-21 |
|
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: 92.02 E-value: 8.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRIDspFG--PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT------------RAAR 66
Cdd:COG0411 1 SDPLLEVRGLTKR--FGglVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 67 CLLARVEQH--LPDEL------------HQQTLLDALLARLPEAERESSAWRAQA--LLANMGFAEAAwSLTAGSLSGGQ 130
Cdd:COG0411 79 LGIARTFQNprLFPELtvlenvlvaahaRLGRGLLAALLRLPRARREEREARERAeeLLERVGLADRA-DEPAGNLSYGQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495164891 131 HTRLLLARALIISPDLLLLDEPG---NHLDLPTMLWLEQFLARWNG-SFILVSHD 181
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHD 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-181 |
8.41e-21 |
|
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: 90.99 E-value: 8.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcllaRVEQHLPDE--LHQQ-------TLLD--A 88
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE----PVTGPGPDRgyVFQQdallpwlTVLDnvA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 L---LARLPEAERESsawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLE 165
Cdd:cd03293 96 LgleLQGVPKAEARE---RAEELLELVGLSGFE-NAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQ 171
|
170 180
....*....|....*....|
gi 495164891 166 QFLAR-WNG---SFILVSHD 181
Cdd:cd03293 172 EELLDiWREtgkTVLLVTHD 191
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
20-181 |
8.76e-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: 92.07 E-value: 8.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcllaRVEQHLPDE--LHQQ-------TLLD--A 88
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGK----PVTGPGPDRgvVFQEpallpwlTVLDnvA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 L---LARLPEAERESsawRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLE 165
Cdd:COG1116 103 LgleLRGVPKAERRE---RARELLELVGLAGFEDAYPH-QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQ 178
|
170 180
....*....|....*....|
gi 495164891 166 QFLAR-WNG---SFILVSHD 181
Cdd:COG1116 179 DELLRlWQEtgkTVLFVTHD 198
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-200 |
1.07e-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: 89.58 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarcllarveqhlpdelhqqtLLDAllarlpeae 97
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-----------------------RLDG--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 98 RESSAWRAQALLANMGFAEAAWSLTAGS-----LSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLAR-- 170
Cdd:cd03246 64 ADISQWDPNELGDHVGYLPQDDELFSGSiaeniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlk 143
|
170 180 190
....*....|....*....|....*....|.
gi 495164891 171 -WNGSFILVSHDSALLDSVtNRTWILRDGQL 200
Cdd:cd03246 144 aAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-202 |
1.69e-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: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT----------RAARCLLARVEQH--LPDEL--HQQTL 85
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYingysirtdrKAARQSLGYCPQFdaLFDELtvREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LDALLARLPEAERESSawrAQALLANMGFaEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDlPTM---L 162
Cdd:cd03263 98 FYARLKGLPKSEIKEE---VELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PASrraI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495164891 163 W-LEQFLARwNGSFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:cd03263 173 WdLILEVRK-GRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-202 |
6.71e-20 |
|
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: 93.29 E-value: 6.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQHlpDELHQQTLLDA 88
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdldeDDLRRRIAVVPQR--PHLFDTTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 L-LARlPEAEREssawRAQALLANMGFAEAAWSLTAG----------SLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:COG4987 429 LrLAR-PDATDE----ELWAALERVGLGDWLAALPDGldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLD 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495164891 158 LPTMLWLEQFLARW--NGSFILVSHDSALLDSVtNRTWILRDGQLQA 202
Cdd:COG4987 504 AATEQALLADLLEAlaGRTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-202 |
8.60e-20 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 88.03 E-value: 8.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarcLLARVE--QHLPDELHQQ------------ 83
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV------LLDGTDirQLDPADLRRNigyvpqdvtlfy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 -TLLDALLARLPEAEREssawraqALLANMGFAEAAwSLTAG--------------SLSGGQHTRLLLARALIISPDLLL 148
Cdd:cd03245 92 gTLRDNITLGAPLADDE-------RILRAAELAGVT-DFVNKhpngldlqigergrGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 149 LDEPGNHLDLPTMLWLEQFLARWNG--SFILVSHDSALLDSVtNRTWILRDGQLQA 202
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLV-DRIIVMDSGRIVA 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-200 |
1.15e-19 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 87.93 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT----------RAARCLLAR-----VEQH---LPDelh 81
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdisklsEKELAAFRRrhigfVFQSfnlLPD--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 82 qQTLLD-----ALLARLPEAERESsawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEP-GNh 155
Cdd:cd03255 97 -LTALEnvelpLLLAGVPKKERRE---RAEELLERVGLGDRL-NHYPSELSGGQQQRVAIARALANDPKIILADEPtGN- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495164891 156 LDLPT---MLWLEQFLARWNG-SFILVSHDsALLDSVTNRTWILRDGQL 200
Cdd:cd03255 171 LDSETgkeVMELLRELNKEAGtTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
320-487 |
1.20e-19 |
|
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: 85.76 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVPgvtfhPRVSLGYYDQSLHQLPdnatllealepfaPELQQRKLALi 399
Cdd:cd00267 22 LKAGEIVALVGPNGSGKSTLLRAI-----AGLLKP-----TSGEILIDGKDIAKLP-------------LEELRRRIGY- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 400 sagfpwarhgqrVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQTF-EGG--LLLVTHDRTLMEA 476
Cdd:cd00267 78 ------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaEEGrtVIIVTHDPELAEL 145
|
170
....*....|.
gi 495164891 477 SCNRFWLVEDG 487
Cdd:cd00267 146 AADRVIVLKDG 156
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-204 |
1.58e-19 |
|
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: 87.19 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQ---------------HLpdelhqqT 84
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPErrnigmvfqdyalfpHL-------T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 85 LLDAL-----LARLPEAERESsawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP 159
Cdd:cd03259 89 VAENIafglkLRGVPKAEIRA---RVRELLELVGLEGLL-NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495164891 160 TMLWLEQFLARWNGSF----ILVSHDSALLDSVTNRTWILRDGQLQAFD 204
Cdd:cd03259 165 LREELREELKELQRELgittIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
34-202 |
1.60e-19 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 88.33 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 34 GLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQHLPDELHQQTLLDALLARLPE-----AE 97
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrRARARRVALVEQDSDTAVPLTVRDVVALGRIPHrslwaGD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 98 RESSAWRAQALLANMG---FAEAAWSltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNG- 173
Cdd:TIGR03873 111 SPHDAAVVDRALARTElshLADRDMS----TLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAt 186
|
170 180 190
....*....|....*....|....*....|.
gi 495164891 174 --SFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:TIGR03873 187 gvTVVAALHDLNLAASYCDHVVVLDGGRVVA 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-200 |
2.24e-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: 92.20 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQHlpDELHQQTLLDA 88
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqidpASLRRQIGVVLQD--VFLFSGTIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 LLARLPEAEREssawRAQALLANMGFAEAAWSLTAG----------SLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL 158
Cdd:COG2274 569 ITLGDPDATDE----EIIEAARLAGLHDFIEALPMGydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 159 PTMLWLEQFLARWNG--SFILVSHDSALLDSVtNRTWILRDGQL 200
Cdd:COG2274 645 ETEAIILENLRRLLKgrTVIIIAHRLSTIRLA-DRIIVLDKGRI 687
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
20-199 |
2.69e-19 |
|
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: 85.70 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarcllarveqhlpdELHQQTLldALLARLPEAERE 99
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-----------------LIDGEDL--TDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 100 SSAWRAQ--ALLANMgfaeAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT----MLWLEQFLARWNG 173
Cdd:cd03229 77 RIGMVFQdfALFPHL----TVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITrrevRALLKSLQAQLGI 152
|
170 180
....*....|....*....|....*.
gi 495164891 174 SFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:cd03229 153 TVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-200 |
2.91e-19 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 91.36 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 5 LTAHSLRIDSPFGPE-LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARV 72
Cdd:COG4988 337 IELEDVSFSYPGGRPaLDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdldpASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 73 EQHlpDELHQQTLLDALLARLPEAEREssawRAQALLANMGFAEAAWSLTAG----------SLSGGQHTRLLLARALII 142
Cdd:COG4988 417 PQN--PYLFAGTIRENLRLGRPDASDE----ELEAALEAAGLDEFVAALPDGldtplgeggrGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 143 SPDLLLLDEPGNHLDLPTMLWLEQFLARWNGS--FILVSHDSALLDSVtNRTWILRDGQL 200
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQA-DRILVLDDGRI 549
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-206 |
3.63e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.06 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARC--LLarveqhlpdEL----HQQ------TLLD 87
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsaLL---------ELgagfHPEltgrenIYLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ALLARLPEAERESsawRAQALLAnmgFAEaawsLTA------GSLSGGQHTRLLLARALIISPDLLLLDEpgnhldlptm 161
Cdd:COG1134 113 GRLLGLSRKEIDE---KFDEIVE---FAE----LGDfidqpvKTYSSGMRARLAFAVATAVDPDILLVDE---------- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 162 lWL---------------EQFLARwNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:COG1134 173 -VLavgdaafqkkclariRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-200 |
4.76e-19 |
|
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: 87.17 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT--------------RAARCLLARVEQHLPDELHQQ 83
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqldrkqrRAFRRDVQLVFQDSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLDALLA-------RLPEAERESsawRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHL 156
Cdd:TIGR02769 105 MTVRQIIGeplrhltSLDESEQKA---RIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495164891 157 DLPTML----WLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:TIGR02769 182 DMVLQAvileLLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-202 |
2.00e-18 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 89.15 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarcLLARVEQHL--PDELHQQ------------ 83
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSV------LLDGVDIRQidPADLRRNigyvpqdprlfy 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 -TLLDALLARLPEAEREssawRAQALLANMGFAEAAWSLTAG----------SLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:TIGR03375 553 gTLRDNIALGAPYADDE----EILRAAELAGVTEFVRRHPDGldmqigergrSLSGGQRQAVALARALLRDPPILLLDEP 628
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495164891 153 GNHLDLPTMLWLEQFLARWNG--SFILVSHDSALLDSVTnRTWILRDGQLQA 202
Cdd:TIGR03375 629 TSAMDNRSEERFKDRLKRWLAgkTLVLVTHRTSLLDLVD-RIIVMDNGRIVA 679
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-199 |
3.42e-18 |
|
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: 83.64 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEG------------VVTRAARCLLA-R------VEQHLpD 78
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsilvrhdggwvdLAQASPREILAlRrrtigyVSQFL-R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 79 ELHQQTLLD----ALLARlpEAERESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGN 154
Cdd:COG4778 104 VIPRVSALDvvaePLLER--GVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495164891 155 HLD---------LptmlwLEQFLARwnGSFIL-VSHDSALLDSVTNRTWILRDGQ 199
Cdd:COG4778 182 SLDaanravvveL-----IEEAKAR--GTAIIgIFHDEEVREAVADRVVDVTPFS 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-200 |
4.96e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.35 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 8 HSLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL--LARVEQHLPDELHQQTL 85
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLakLNRAQRKAFRRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LDAL-------------------LARLPEAERESsawRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDL 146
Cdd:PRK10419 96 QDSIsavnprktvreiireplrhLLSLDKAERLA---RASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 147 LLLDEPGNHLDLPTMLWLEQFLA----RWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:PRK10419 173 LILDEAVSNLDLVLQAGVIRLLKklqqQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
319-487 |
6.18e-18 |
|
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: 82.51 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLL--WRQWQTGE-TVPGVtfhPRVSLGYYDQSLH-----QLPD----NATLLEALEp 386
Cdd:cd03225 23 TIKKGEFVLIVGPNGSGKSTLLRLLngLLGPTSGEvLVDGK---DLTKLSLKELRRKvglvfQNPDdqffGPTVEEEVA- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 387 FAP--------ELQQRKLALISAGFPWARHGQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQ 458
Cdd:cd03225 99 FGLenlglpeeEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK 178
|
170 180 190
....*....|....*....|....*....|..
gi 495164891 459 TF--EG-GLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:cd03225 179 KLkaEGkTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
20-200 |
7.23e-18 |
|
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: 83.01 E-value: 7.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT--------------RAARCLLARVEQHLpDELHQQTL 85
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKARRRIGMIFQHF-NLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LD--AL---LARLPEAERESsawRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:cd03258 100 FEnvALpleIAGVPKAEIEE---RVLELLELVGLEDKADAYPA-QLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 161 MLWLEQFLARWNGSF----ILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:cd03258 176 TQSILALLRDINRELgltiVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-203 |
8.32e-18 |
|
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: 82.61 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTL-----APAEGVVT-------------RAARCLLARVEQHlPDELH 81
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLldgkdiydldvdvLELRRRVGMVFQK-PNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 82 QqTLLD--ALLARLP-EAERESSAWRAQALLANMG-FAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:cd03260 95 G-SIYDnvAYGLRLHgIKLKEELDERVEEALRKAAlWDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495164891 158 LPTMLWLEQFLARWNGSF--ILVSHDSALLDSVTNRTWILRDGQLQAF 203
Cdd:cd03260 174 PISTAKIEELIAELKKEYtiVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-201 |
8.77e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 82.41 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT----------RAARCLLAR----VEQ--HLpdeLHQQ 83
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlkRREIPYLRRrigvVFQdfRL---LPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLD--AL---LARLPEAERESsawRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDl 158
Cdd:COG2884 95 TVYEnvALplrVTGKSRKEIRR---RVREVLDLVGLSDKAKALPH-ELSGGEQQRVAIARALVNRPELLLADEPTGNLD- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495164891 159 PTMLW-----LEQFLARwnG-SFILVSHDSALLDSVTNRTWILRDGQLQ 201
Cdd:COG2884 170 PETSWeimelLEEINRR--GtTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
20-203 |
9.03e-18 |
|
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: 82.72 E-value: 9.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLpDELHQQT--------LLDAL-- 89
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL-YELRRRIgmlfqggaLFDSLtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 ----------LARLPEAERESsawRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEP--GnhLD 157
Cdd:COG1127 100 fenvafplreHTDLSEAEIRE---LVLEKLELVGLPGAADKMPS-ELSGGMRKRVALARALALDPEILLYDEPtaG--LD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495164891 158 LPTMLWLEQFLARWNGSF----ILVSHDSALLDSVTNRTWILRDGQLQAF 203
Cdd:COG1127 174 PITSAVIDELIRELRDELgltsVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-206 |
1.00e-17 |
|
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: 82.73 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcllaRVEQHLPDELH-------QQTLL---- 86
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE----DIREQDPVELRrkigyviQQIGLfphm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 -----DALLARLPEAERESSAWRAQALLANMGFAEAAWS-LTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:cd03295 91 tveenIALVPKLLKWPKEKIRERADELLALVGLDPAEFAdRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPIT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495164891 161 MLWLEQFLARWN----GSFILVSHD--SALLdsVTNRTWILRDGQLQAFDLP 206
Cdd:cd03295 171 RDQLQEEFKRLQqelgKTIVFVTHDidEAFR--LADRIAIMKNGEIVQVGTP 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
20-199 |
1.04e-17 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 80.89 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarcllarveqhlpdelhqqTLLDALLARLPEAE-R 98
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI----------------------LIDGVDLRDLDLESlR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 99 ESSAWRAQ-ALLANMGFAEaawSLtagsLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNG--SF 175
Cdd:cd03228 76 KNIAYVPQdPFLFSGTIRE---NI----LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTV 148
|
170 180
....*....|....*....|....
gi 495164891 176 ILVSHDSALLDSVtNRTWILRDGQ 199
Cdd:cd03228 149 IVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-181 |
1.19e-17 |
|
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: 83.27 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 14 SPFgpELNAL---SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPD------------ 78
Cdd:TIGR04521 14 TPF--EKKALddvSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDlrkkvglvfqfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 79 --ELHQQTLLD--ALLAR---LPEAERESsawRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDE 151
Cdd:TIGR04521 92 ehQLFEETVYKdiAFGPKnlgLSEEEAEE---RVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDE 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 495164891 152 PGNHLDlP----TMLwleQFLARWNG----SFILVSHD 181
Cdd:TIGR04521 169 PTAGLD-PkgrkEIL---DLFKRLHKekglTVILVTHS 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
17-203 |
1.34e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 86.10 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 17 GPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQ-HLPDELHQQTLLDALlarlpe 95
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdHAYDFENDLTLFDWM------ 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 96 aeresSAWRAQ--------ALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQF 167
Cdd:PRK15064 406 -----SQWRQEgddeqavrGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMA 480
|
170 180 190
....*....|....*....|....*....|....*.
gi 495164891 168 LARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAF 203
Cdd:PRK15064 481 LEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDF 516
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-206 |
1.50e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 84.38 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLarveqHLPDE------LHQQtllDAL---- 89
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLPPEkrnvgmVFQD---YALfphl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 -----------LARLPEAERESsawRAQALLA--NM-GFAEAAwsltAGSLSGGQHTRLLLARALIISPDLLLLDEPGNH 155
Cdd:COG3842 93 tvaenvafglrMRGVPKAEIRA---RVAELLElvGLeGLADRY----PHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495164891 156 LDLP----TMLWLEQFLARWNGSFILVSHDS--ALldSVTNRTWILRDGQLQAFDLP 206
Cdd:COG3842 166 LDAKlreeMREELRRLQRELGITFIYVTHDQeeAL--ALADRIAVMNDGRIEQVGTP 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
16-200 |
2.10e-17 |
|
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: 81.04 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 16 FGPE--LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARvEQHLpDELHQQ---------- 83
Cdd:cd03262 10 FGDFhvLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDD-KKNI-NELRQKvgmvfqqfnl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 ----TLLDAL-LA-----RLPEAERESsawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEPG 153
Cdd:cd03262 88 fphlTVLENItLApikvkGMSKAEAEE---RALELLEKVGLADKADAY-PAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 154 NHLDlPTM----LWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:cd03262 164 SALD-PELvgevLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-200 |
2.49e-17 |
|
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: 80.91 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-------TRAARCLLARVEQHLPDELHQQTLLD--- 87
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvSDLRGRAIPYLRRKIGVVFQDFRLLPdrn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 -----ALLARLPEAERESSAWRAQALLANMGFAEAAWSLTAGsLSGGQHTRLLLARALIISPDLLLLDEPGNHLDlPTML 162
Cdd:cd03292 95 vyenvAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTGNLD-PDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 163 W-----LEQFLARwnGSFILVS-HDSALLDSVTNRTWILRDGQL 200
Cdd:cd03292 173 WeimnlLKKINKA--GTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-199 |
2.70e-17 |
|
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: 80.79 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQH---LPDE--LHQ-QTLLDAL--LA 91
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigyLPEErgLYPkMKVIDQLvyLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 92 RLPEAERESSAWRAQALLANMGFAEaAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD-LPTMLWLEQF--L 168
Cdd:cd03269 96 QLKGLKKEEARRRIDEWLERLELSE-YANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpVNVELLKDVIreL 174
|
170 180 190
....*....|....*....|....*....|.
gi 495164891 169 ARWNGSFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:cd03269 175 ARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
18-217 |
3.04e-17 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 84.80 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraaRCLLARVEQHLPDELHQQ--------TLLDAL 89
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV----RLDGADLSQWDREELGRHigylpqdvELFDGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 L----ARLPEAERES--SAwraqALLAnmGFAEAAWSLTAG----------SLSGGQHTRLLLARALIISPDLLLLDEPG 153
Cdd:COG4618 422 IaeniARFGDADPEKvvAA----AKLA--GVHEMILRLPDGydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495164891 154 NHLDLPTMLWLEQFLARW---NGSFILVSHDSALLdSVTNRTWILRDGQLQAFDlPCTQARAALAAR 217
Cdd:COG4618 496 SNLDDEGEAALAAAIRALkarGATVVVITHRPSLL-AAVDKLLVLRDGRVQAFG-PRDEVLARLARP 560
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-204 |
3.58e-17 |
|
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: 80.65 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAAR--CLL---ARVEQHLPDElhQQTLLDALLARLP 94
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLglgGGFNPELTGR--ENIYLNGRLLGLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 95 EAERESsawRAQALLAnmgFAE--AAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARW- 171
Cdd:cd03220 116 RKEIDE---KIDEIIE---FSElgDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELl 189
|
170 180 190
....*....|....*....|....*....|....*
gi 495164891 172 --NGSFILVSHDSALLDSVTNRTWILRDGQLQAFD 204
Cdd:cd03220 190 kqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
20-157 |
3.67e-17 |
|
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: 81.19 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT--------------RAARCLLARVEQH---------- 75
Cdd:TIGR02315 18 LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtditklrgkklRKLRRRIGMIFQHynlierltvl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 76 ---LPDELHQQTLLDALLARLPEAEREssawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:TIGR02315 98 envLHGRLGYKPTWRSLLGRFSEEDKE----RALSALERVGLADKA-YQRADQLSGGQQQRVAIARALAQQPDLILADEP 172
|
....*
gi 495164891 153 GNHLD 157
Cdd:TIGR02315 173 IASLD 177
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-206 |
4.19e-17 |
|
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: 80.49 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGV-------VTRAARCLLARV-----EQHLPDEL--HQQTL 85
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdVVREPREVRRRIgivfqDLSVDDELtgWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LDALLARLPEAERESsawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTM--LW 163
Cdd:cd03265 96 IHARLYGVPGAERRE---RIDELLDFVGLLEAADRL-VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRahVW 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495164891 164 --LEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:cd03265 172 eyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-195 |
5.03e-17 |
|
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: 84.22 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQ---HL-PDELHQQTLLDAL-LARLPEAE 97
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQsrdALdPNKTVWEEISGGLdIIKLGKRE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 98 RESSAWraqalLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNGSFIL 177
Cdd:TIGR03719 421 IPSRAY-----VGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVV 495
|
170
....*....|....*...
gi 495164891 178 VSHDSALLDSVTnrTWIL 195
Cdd:TIGR03719 496 ISHDRWFLDRIA--THIL 511
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-181 |
6.74e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.68 E-value: 6.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAH-SLRIDSPFGPE--LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTR---------AARcl 68
Cdd:COG4525 1 MSMLTVRHvSVRYPGGGQPQpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtgpgADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 69 lARVEQH---LPdelhQQTLLD--AL---LARLPEAERESsawRAQALLANMGFAEAA----WSLtagslSGGQHTRLLL 136
Cdd:COG4525 79 -GVVFQKdalLP----WLNVLDnvAFglrLRGVPKAERRA---RAEELLALVGLADFArrriWQL-----SGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495164891 137 ARALIISPDLLLLDEPGNHLDLPTMLWLEQFLAR-WNGS---FILVSHD 181
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDvWQRTgkgVFLITHS 194
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
296-487 |
9.50e-17 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 79.68 E-value: 9.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLL--WRQWQTGE-TVPGVT--------FHPRVSL 364
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSL-SIEKGEFVAIIGPNGSGKSTLLRLLngLLKPTSGEvLVDGKDitkknlreLRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 365 gyydqsLHQLPDN----ATLLEALEpFAP--------ELQQR-KLALISAGFpWARHGQRVDTLSGGERSRLLFVGLsLA 431
Cdd:COG1122 80 ------VFQNPDDqlfaPTVEEDVA-FGPenlglpreEIRERvEEALELVGL-EHLADRPPHELSGGQKQRVAIAGV-LA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 432 -RYSLLMLDEPTNHLDMEGKEALAQTLQTF--EG-GLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:COG1122 151 mEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-198 |
1.06e-16 |
|
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: 79.43 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcllaRVEQHLPDEL---HQQTLL---------- 86
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK----QITEPGPDRMvvfQNYSLLpwltvrenia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 ---DALLARLPEAERESSAWRAQALLanmGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLW 163
Cdd:TIGR01184 77 lavDRVLPDLSKSERRAIVEEHIALV---GLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495164891 164 L-EQFLARWNGS---FILVSH--DSALLdsVTNRTWILRDG 198
Cdd:TIGR01184 153 LqEELMQIWEEHrvtVLMVTHdvDEALL--LSDRVVMLTNG 191
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-160 |
1.41e-16 |
|
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: 82.79 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------RAARCLLARVEQHLPDELH--QQTLLDA 88
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTldgvpvsSLDQDEVRRRVSVCAQDAHlfDTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 LLARLPEAERESsAWRAqalLANMGFAEAAWSLTAG----------SLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL 158
Cdd:TIGR02868 429 LRLARPDATDEE-LWAA---LERVGLADWLRALPDGldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
..
gi 495164891 159 PT 160
Cdd:TIGR02868 505 ET 506
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
319-489 |
2.99e-16 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 76.71 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLWR--QWQTGEtvpgvtfhprVSLGyyDQSLHQLP------DNATLLEALEpfapE 390
Cdd:cd03214 21 SIEAGEIVGILGPNGAGKSTLLKTLAGllKPSSGE----------ILLD--GKDLASLSpkelarKIAYVPQALE----L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 391 LQQRKLAlisagfpwarhGQRVDTLSGGERSRLLfvglsLARY-----SLLMLDEPTNHLDMEGKEALAQTLQTF--EGG 463
Cdd:cd03214 85 LGLAHLA-----------DRPFNELSGGERQRVL-----LARAlaqepPILLLDEPTSHLDIAHQIELLELLRRLarERG 148
|
170 180
....*....|....*....|....*...
gi 495164891 464 L--LLVTHDRTLMEASCNRFWLVEDGGL 489
Cdd:cd03214 149 KtvVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-186 |
4.26e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 5 LTAHSLRIDSPFG-PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGtLAP-AEGVVTR--AARCLLarveqhLPDE- 79
Cdd:COG4178 363 LALEDLTLRTPDGrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIARpaGARVLF------LPQRp 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 80 -LHQQTLLDALLarLPEAERESSAWRAQALLANMGFA--------EAAWSLTagsLSGGQHTRLLLARALIISPDLLLLD 150
Cdd:COG4178 436 yLPLGTLREALL--YPATAEAFSDAELREALEAVGLGhlaerldeEADWDQV---LSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190
....*....|....*....|....*....|....*...
gi 495164891 151 EPGNHLDLPTMLWLEQFLAR--WNGSFILVSHDSALLD 186
Cdd:COG4178 511 EATSALDEENEAALYQLLREelPGTTVISVGHRSTLAA 548
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-183 |
4.37e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.14 E-value: 4.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 5 LTAHSLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAegvVTRAARCLLARVE-QHLPDELHQQ 83
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPA---FSASGEVLLNGRRlTALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLL--DALL---------------ARLPEAERESsawRAQALLANMG---FAEAawslTAGSLSGGQHTRLLLARALIIS 143
Cdd:COG4136 79 GILfqDDLLfphlsvgenlafalpPTIGRAQRRA---RVEQALEEAGlagFADR----DPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 144 PDLLLLDEPGNHLDLPTMLWLEQF----LARWNGSFILVSHDSA 183
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEE 195
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-202 |
9.56e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 76.99 E-value: 9.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPD---ELHQQTLL--D----- 87
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRigvVFGQKTQLwwDlpvid 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 --ALLA---RLPEAEressAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTML 162
Cdd:cd03267 115 sfYLLAaiyDLPPAR----FKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 163 WLEQFLARWN----GSFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:cd03267 191 NIRNFLKEYNrergTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-217 |
9.91e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.41 E-value: 9.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtRAARCLLArveqhlpdELHQQTLLDALLARLPEAERE 99
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLA--------EAREDTRLMFQDARLLPWKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 100 --------SSAWRAQAL--LANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLA 169
Cdd:PRK11247 99 idnvglglKGQWRDAALqaLAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 170 R-W---NGSFILVSHDSALLDSVTNRTWILRDGQLQ---AFDLPCTQAR-----AALAAR 217
Cdd:PRK11247 178 SlWqqhGFTVLLVTHDVSEAVAMADRVLLIEEGKIGldlTVDLPRPRRRgsarlAELEAE 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-181 |
9.99e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 9.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRIDspFGPE--LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVeqhlPD 78
Cdd:PRK09544 1 MTSLVSLENVSVS--FGQRrvLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYV----PQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 79 ELHQQTLLDALLARLpeaERESSAWRAQALLANMGFAEAAWSLTA--GSLSGGQHTRLLLARALIISPDLLLLDEPGNHL 156
Cdd:PRK09544 75 KLYLDTTLPLTVNRF---LRLRPGTKKEDILPALKRVQAGHLIDApmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180
....*....|....*....|....*....
gi 495164891 157 DLPTMLWL----EQFLARWNGSFILVSHD 181
Cdd:PRK09544 152 DVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-469 |
1.21e-15 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 76.66 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLWRQ-WQT--------GETVPGVT-FHPRVSLGYYDQSLHQ-LPDNATLLEALE-- 385
Cdd:COG1119 25 TVKPGEHWAILGPNGAGKSTLLSLITGDlPPTygndvrlfGERRGGEDvWELRKRIGLVSPALQLrFPRDETVLDVVLsg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 386 -------PFAPELQQRKLA---LISAGFpWARHGQRVDTLSGGERSRLLfvglsLARY-----SLLMLDEPTNHLDMEGK 450
Cdd:COG1119 105 ffdsiglYREPTDEQRERArelLELLGL-AHLADRPFGTLSQGEQRRVL-----IARAlvkdpELLILDEPTAGLDLGAR 178
|
170 180
....*....|....*....|...
gi 495164891 451 EALAQTLQTF--EGG--LLLVTH 469
Cdd:COG1119 179 ELLLALLDKLaaEGAptLVLVTH 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-206 |
1.28e-15 |
|
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: 76.51 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcllaRVEQHLPDELHQQTLLD--AL-------- 89
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK----DITNLPPHKRPVNTVFQnyALfphltvfe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 -------LARLPEAERESSAWRAQALLANMGFAEAAWSltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTML 162
Cdd:cd03300 92 niafglrLKKLPKAEIKERVAEALDLVQLEGYANRKPS----QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495164891 163 WLEQFLARWNGS----FILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:cd03300 168 DMQLELKRLQKElgitFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
319-489 |
1.73e-15 |
|
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: 75.70 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLWRQWQTGE------TVPGVTFHP---RVSLGYYDQSLH----QLPDNATL----- 380
Cdd:cd03245 26 TIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSgsvlldGTDIRQLDPadlRRNIGYVPQDVTlfygTLRDNITLgapla 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 381 -----LEALE-----PFAPeLQQRKLALisagfpwaRHGQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGK 450
Cdd:cd03245 106 dderiLRAAElagvtDFVN-KHPNGLDL--------QIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495164891 451 EALAQTLQTFEGG--LLLVTHdRTLMEASCNRFWLVEDGGL 489
Cdd:cd03245 177 ERLKERLRQLLGDktLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-152 |
1.73e-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: 75.55 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-------TRAA---------------RCLLAR--VEQH 75
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIrfdgrdiTGLPpheraragigyvpegRRIFPEltVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 76 L-------PDELHQQTlLDALLARLPE-AERessawRAQAllanmgfaeaawsltAGSLSGGQHTRLLLARALIISPDLL 147
Cdd:cd03224 96 LllgayarRRAKRKAR-LERVYELFPRlKER-----RKQL---------------AGTLSGGEQQMLAIARALMSRPKLL 154
|
....*
gi 495164891 148 LLDEP 152
Cdd:cd03224 155 LLDEP 159
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
8-206 |
2.57e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 8 HSLRIDSPFGPE-LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV---------------TRAARCLLAR 71
Cdd:PRK13643 9 YTYQPNSPFASRaLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvsstskqkeIKPVRKKVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 72 VEQHLPDELHQQTLLDAlLARLPE---AERESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLL 148
Cdd:PRK13643 89 VFQFPESQLFEETVLKD-VAFGPQnfgIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495164891 149 LDEPGNHLDLPT---MLWLEQFLARWNGSFILVSHdsaLLDSV---TNRTWILRDGQLQAFDLP 206
Cdd:PRK13643 168 LDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH---LMDDVadyADYVYLLEKGHIISCGTP 228
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-203 |
2.76e-15 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 77.46 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLL-ARVEQHLPDE-------LHQQTLLDALLARlp 94
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdSRKGIFLPPEkrrigyvFQEARLFPHLSVR-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 95 eAERESSAWRAQALLANMGFAEAAWSLT--------AGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT----ML 162
Cdd:TIGR02142 94 -GNLRYGMKRARPSERRISFERVIELLGighllgrlPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeiLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495164891 163 WLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAF 203
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAA 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
17-185 |
2.82e-15 |
|
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: 78.48 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 17 GPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDE---------LHQQTLLD 87
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQiawvpqhpfLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ALLARLPEAERESSAwRAQALLANMGFAEAA---WSLTAGS----LSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:TIGR02857 415 NIRLARPDASDAEIR-EALERAGLDEFVAALpqgLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180
....*....|....*....|....*..
gi 495164891 161 -MLWLEQFLARWNG-SFILVSHDSALL 185
Cdd:TIGR02857 494 eAEVLEALRALAQGrTVLLVTHRLALA 520
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
20-206 |
3.43e-15 |
|
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: 75.23 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL--LARVE-QHLPDE---LHQQ-TLLDAL--- 89
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsgLSEAElYRLRRRmgmLFQSgALFDSLtvf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 --LA-------RLPEAERESsawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:cd03261 96 enVAfplrehtRLSEEEIRE---IVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495164891 161 MLWLEQFLARWNGSF----ILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:cd03261 172 SGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-203 |
3.56e-15 |
|
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: 78.54 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraaRCLLARVEQ-----------HLPD--ELHQQT 84
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV----RLDGADLKQwdretfgkhigYLPQdvELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 85 LLD--ALLARLPEAERESSAWR---AQALLAN--MGFaEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:TIGR01842 408 VAEniARFGENADPEKIIEAAKlagVHELILRlpDGY-DTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495164891 158 ----LPTMLWLEQFLARwNGSFILVSHDSALLDSVtNRTWILRDGQLQAF 203
Cdd:TIGR01842 487 eegeQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRIARF 534
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
320-443 |
4.02e-15 |
|
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: 72.68 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLWRQ---------WQTGETVPGVTFHPRVSLGYYDQSLHQLPdNATLLEAL------ 384
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLlsptegtilLDGQDLTDDERKSLRKEIGYVFQDPQLFP-RLTVRENLrlglll 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495164891 385 -EPFAPELQQR-KLALISAGFPWARH---GQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTN 443
Cdd:pfam00005 87 kGLSKREKDARaEEALEKLGLGDLADrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
296-487 |
5.69e-15 |
|
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: 72.80 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLLwrqwqtgetvpgvtfhprvsLGYYDqslhqlP 375
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLL--------------------LRLYD------P 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 376 DNATLL---EALEPFAPELQQRKLALISagfpwarhgQRV----DT-----LSGGERSRllfvgLSLARY-----SLLML 438
Cdd:cd03228 55 TSGEILidgVDLRDLDLESLRKNIAYVP---------QDPflfsGTireniLSGGQRQR-----IAIARAllrdpPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 439 DEPTNHLDMEGKEALAQTLQTFEGG--LLLVTHDRTLMEaSCNRFWLVEDG 487
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGktVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-201 |
6.64e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.01 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT------------------------RAARCLLARVEQH 75
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVvngqtinlvrdkdgqlkvadknqlRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 76 LPDELHQQTL---LDALLARLPEAERESSAwRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:PRK10619 101 FNLWSHMTVLenvMEAPIQVLGLSKQEARE-RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495164891 153 GNHLD---LPTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQ 201
Cdd:PRK10619 180 TSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-200 |
9.23e-15 |
|
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: 77.15 E-value: 9.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 5 LTAHSLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-----------TRAARCLLARVE 73
Cdd:TIGR03269 285 VSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGPDGRGRAK 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 74 QHLpDELHQQ-----------TLLDALLARLPEaerESSAWRAQALLANMGF----AEAAWSLTAGSLSGGQHTRLLLAR 138
Cdd:TIGR03269 365 RYI-GILHQEydlyphrtvldNLTEAIGLELPD---ELARMKAVITLKMVGFdeekAEEILDKYPDELSEGERHRVALAQ 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 139 ALIISPDLLLLDEPGNHLDLPTMLWLEQFL--AR--WNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAReeMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
296-489 |
1.06e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 72.25 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLLWRQWQ--TGE-TVPGVTFHpRVSLGYYDQSLH 372
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRptSGRvRLDGADIS-QWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 373 QLPDNATLLEalepfapelqqrklalisagfpwarhGQRVDT-LSGGERSRllfVGLSLARY---SLLMLDEPTNHLDME 448
Cdd:cd03246 80 YLPQDDELFS--------------------------GSIAENiLSGGQRQR---LGLARALYgnpRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 449 GKEALAQTLQTFEGG---LLLVTHDRTLMeASCNRFWLVEDGGL 489
Cdd:cd03246 131 GERALNQAIAALKAAgatRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-158 |
1.13e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.28 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT------------RAARCLLARVEQHL-PDELHQQTLL 86
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpismlssrQLARRLALLPQHHLtPEGITVRELV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 87 D-------ALLARLPEAERESSAWRAQAllanMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL 158
Cdd:PRK11231 98 AygrspwlSLWGRLSAEDNARVNQAMEQ----TRINHLADRRLT-DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
296-473 |
1.56e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.42 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLWRQWQtgetvpgvtfhprvslgYYDQSLHQLP 375
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSF-EIKPGDRLLITGPSGTGKSSLFRALAGLWP-----------------WGSGRIGMPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 376 DNATLLEALEPFAPELQQRKlALIsagFPWArhgqrvDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQ 455
Cdd:cd03223 63 GEDLLFLPQRPYLPLGTLRE-QLI---YPWD------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ 132
|
170
....*....|....*...
gi 495164891 456 TLQTFEGGLLLVTHDRTL 473
Cdd:cd03223 133 LLKELGITVISVGHRPSL 150
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
23-195 |
2.12e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.93 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQ---HLPDElhqQTL-------LDALlaR 92
Cdd:PRK11819 343 LSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQsrdALDPN---KTVweeisggLDII--K 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 93 LPEAERESSAWraqalLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWN 172
Cdd:PRK11819 418 VGNREIPSRAY-----VGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFP 492
|
170 180
....*....|....*....|...
gi 495164891 173 GSFILVSHDSALLDSVTnrTWIL 195
Cdd:PRK11819 493 GCAVVISHDRWFLDRIA--THIL 513
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
295-489 |
3.05e-14 |
|
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: 72.77 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 295 LLELENLAVSAaPDTPTL----FTLPlarlkSGDRVALLGHNGCGKSSLLRLLWRQ--WQTGE-TVPGV---TFHPRV-- 362
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLddvsLSLP-----PGEVTALLGPNGSGKSTLLRALAGLlkPSSGEvLLDGRdlaSLSRREla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 363 -SLGYYDQSlHQLPDNATLLE-----------ALEPFAPELQQR-KLALISAGfpwARH--GQRVDTLSGGERSRLLfvg 427
Cdd:COG1120 75 rRIAYVPQE-PPAPFGLTVRElvalgryphlgLFGRPSAEDREAvEEALERTG---LEHlaDRPVDELSGGERQRVL--- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495164891 428 lsLARY-----SLLMLDEPTNHLDMEGKEALAQTLQTF--EGGL--LLVTHDRTLMEASCNRFWLVEDGGL 489
Cdd:COG1120 148 --IARAlaqepPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRtvVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-202 |
3.06e-14 |
|
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: 70.54 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarcllarveqhlpdelhqqtLLDAllarlpEAERE 99
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI-----------------------LVDG------KEVSF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 100 SSAWRAQALLANMGFaeaawsltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARW--NG-SFI 176
Cdd:cd03216 67 ASPRDARRAGIAMVY----------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVI 136
|
170 180 190
....*....|....*....|....*....|
gi 495164891 177 LVSH----DSALLDSVTnrtwILRDGQLQA 202
Cdd:cd03216 137 FISHrldeVFEIADRVT----VLRDGRVVG 162
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
286-501 |
3.45e-14 |
|
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: 75.19 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 286 SGDALAADRLLELENLAVSAAPDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLLWRQW--QTGEtvpgvtfhprVS 363
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLdpQSGS----------IT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 364 LGyyDQSLHQLPD-----------------NATLLEALEPFAPELQQRKL--ALISAGF-PWARH---------GQRVDT 414
Cdd:COG4987 394 LG--GVDLRDLDEddlrrriavvpqrphlfDTTLRENLRLARPDATDEELwaALERVGLgDWLAAlpdgldtwlGEGGRR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 415 LSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQTFEGG--LLLVTHDRTLMEAsCNRFWLVEDGGLSEW 492
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLER-MDRILVLEDGRIVEQ 550
|
....*....
gi 495164891 493 HNMEALLAR 501
Cdd:COG4987 551 GTHEELLAQ 559
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-206 |
3.47e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.32 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT---------------RAARCLLARVEQHLPDELHQQT 84
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpetgnknlKKLRKKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 85 LL-DALLARLPEAERESSAwRAQAL--LANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDlPT- 160
Cdd:PRK13641 103 VLkDVEFGPKNFGFSEDEA-KEKALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD-PEg 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495164891 161 ---MLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:PRK13641 181 rkeMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
16-206 |
4.63e-14 |
|
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: 71.99 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 16 FG--PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT---RAARCLLAR------VEQHLPDELHQqT 84
Cdd:cd03296 12 FGdfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggEDATDVPVQernvgfVFQHYALFRHM-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 85 LLDAL---LARLPEAERESSAW---RAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD- 157
Cdd:cd03296 91 VFDNVafgLRVKPRSERPPEAEiraKVHELLKLVQLDWLADRYPA-QLSGGQRQRVALARALAVEPKVLLLDEPFGALDa 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495164891 158 -----LPTmlWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:cd03296 170 kvrkeLRR--WLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-206 |
4.96e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-------TRAARCLLARVEQ-----HLPDELHQQTL 85
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkplDYSKRGLLALRQQvatvfQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LDALLA------RLPEAERESSAWRAQALLANMGFAEAAWSltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD-- 157
Cdd:PRK13638 95 IDSDIAfslrnlGVPEAEITRRVDEALTLVDAQHFRHQPIQ----CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpa 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495164891 158 -LPTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:PRK13638 171 gRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-200 |
5.16e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.42 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 4 LLTAHSLRIDSPFGPE-LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------------RAARCLL 69
Cdd:PRK13639 1 ILETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLikgepikydkkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 70 ARVEQHLPDELHQQTLLD-----ALLARLPEAERESSAWRAQALLANMGFAEAAwsltAGSLSGGQHTRLLLARALIISP 144
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEdvafgPLNLGLSKEEVEKRVKEALKAVGMEGFENKP----PHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 145 DLLLLDEPGNHLDLPTMLWLEQFLARWN--GSFILVS-HDSALLDSVTNRTWILRDGQL 200
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNkeGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-206 |
5.46e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 72.07 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL-------LARVEQHLPdelhQQTLLD----- 87
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawspweLARRRAVLP----QHSSLAfpftv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ---ALLARLP-EAERESSAWRAQALLANMG---FAEAAWSltagSLSGGQHTRLLLARALI-------ISPDLLLLDEPG 153
Cdd:COG4559 93 eevVALGRAPhGSSAAQDRQIVREALALVGlahLAGRSYQ----TLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 154 NHLDLP---TMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:COG4559 169 SALDLAhqhAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTP 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-152 |
6.36e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 71.55 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-------TRAARCLLAR-----------------VEQH 75
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIrfdgediTGLPPHRIARlgigyvpegrrifpsltVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 76 L-------PDELHQQTLLDALLARLPE-AERessawRAQAllanmgfaeaawsltAGSLSGGQHTRLLLARALIISPDLL 147
Cdd:COG0410 99 LllgayarRDRAEVRADLERVYELFPRlKER-----RRQR---------------AGTLSGGEQQMLAIGRALMSRPKLL 158
|
....*
gi 495164891 148 LLDEP 152
Cdd:COG0410 159 LLDEP 163
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-202 |
7.41e-14 |
|
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: 71.31 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL-------LARV-----------EQHLPdelh 81
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedaRARLrarhvgfvfqsFQLLP---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 82 qqTL-------LDALLARLPEAERessawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEP-G 153
Cdd:COG4181 104 --TLtalenvmLPLELAGRRDARA-----RARALLERVGLGHRL-DHYPAQLSGGEQQRVALARAFATEPAILFADEPtG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495164891 154 NhLDLPT---MLWLEQFLARWNGS-FILVSHDSALLDSvTNRTWILRDGQLQA 202
Cdd:COG4181 176 N-LDAATgeqIIDLLFELNRERGTtLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-200 |
7.55e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.50 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 5 LTAHSLRIDSPFGPEL-NALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLaPAEGVVT-----------RAARCLLARV 72
Cdd:PRK11174 350 IEAEDLEILSPDGKTLaGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKingielreldpESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 73 EQ--HLPdelhQQTLLDALLARLPEAEREssawRAQALLANMGFAEAAWSLT----------AGSLSGGQHTRLLLARAL 140
Cdd:PRK11174 429 GQnpQLP----HGTLRDNVLLGNPDASDE----QLQQALENAWVSEFLPLLPqgldtpigdqAAGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495164891 141 IISPDLLLLDEPGNHLDLPT----MLWLEQflARWNGSFILVSHDSALLDSVtNRTWILRDGQL 200
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSeqlvMQALNA--ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-217 |
7.75e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 4 LLTAHSLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLapAEGVVTRAARCL--------------- 68
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDL--TGGGAPRGARVTgdvtlngeplaaida 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 69 --LARVEQHLPDELHQQTLLDA----LLARLPEAERESSAWRAQALLANMGFAEAAWSLTAG----SLSGGQHTRLLLAR 138
Cdd:PRK13547 79 prLARLRAVLPQAAQPAFAFSAreivLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGrdvtTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 139 AL---------IISPDLLLLDEPGNHLDLP---TMLWLEQFLAR-WNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDL 205
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAhqhRLLDTVRRLARdWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
250
....*....|..
gi 495164891 206 PCTQARAALAAR 217
Cdd:PRK13547 239 PADVLTPAHIAR 250
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-203 |
9.90e-14 |
|
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: 70.30 E-value: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGdRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARveqhlPDELHQ------QT--------- 84
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-----PQKLRRrigylpQEfgvypnftv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 85 --LLD--ALLARLPEAERESsawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:cd03264 90 reFLDyiAWLKGIPSKEVKA---RVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495164891 161 MLWLEQFLARW--NGSFILVSHDSALLDSVTNRTWILRDGQLQAF 203
Cdd:cd03264 166 RIRFRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-200 |
1.16e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.70 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 14 SPF-GPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT---------------RAARCLLARVEQHLP 77
Cdd:PRK13649 16 TPFeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitstsknkdiKQIRKKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 78 DELHQQTLLDAlLARLPE---AERESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGN 154
Cdd:PRK13649 96 SQLFEETVLKD-VAFGPQnfgVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495164891 155 HLDlPT----MLWLEQFLARWNGSFILVSHdsaLLDSVTN---RTWILRDGQL 200
Cdd:PRK13649 175 GLD-PKgrkeLMTLFKKLHQSGMTIVLVTH---LMDDVANyadFVYVLEKGKL 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
232-501 |
1.42e-13 |
|
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: 73.71 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 232 IDRVTASAKRLA-TWGQVYDnedlARKAKQMEKQVARLKEEQTELAQGSRwRLTLSGDalaadrlLELENLAVSAAPDTP 310
Cdd:COG2274 421 SGRFLAPVAQLIgLLQRFQD----AKIALERLDDILDLPPEREEGRSKLS-LPRLKGD-------IELENVSFRYPGDSP 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 311 TL---FTLplaRLKSGDRVALLGHNGCGKSSLLRLLWRQW--QTGE-TVPGV---TFHPRV---SLGYYDQSLHQLpdNA 378
Cdd:COG2274 489 PVldnISL---TIKPGERVAIVGRSGSGKSTLLKLLLGLYepTSGRiLIDGIdlrQIDPASlrrQIGVVLQDVFLF--SG 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 379 TLLEALEPFAPELQQRKL--ALISAGFpwarH--------------GQRVDTLSGGERSRLLfvglsLAR--Y---SLLM 437
Cdd:COG2274 564 TIRENITLGDPDATDEEIieAARLAGL----HdfiealpmgydtvvGEGGSNLSGGQRQRLA-----IARalLrnpRILI 634
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 438 LDEPTNHLDMEGKEALAQTLQTFEGG--LLLVTHDRTLMeASCNRFWLVEDGGLSEWHNMEALLAR 501
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-202 |
1.46e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 70.26 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-------------TRAARCLlarveQHLPDE---LHQQ 83
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmhKRARLGI-----GYLPQEasiFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLDALLA-----RLPEAERESsawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL 158
Cdd:cd03218 91 TVEENILAvleirGLSKKEREE---KLEELLEEFHITHLRKSK-ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495164891 159 PTMLWLE---QFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:cd03218 167 IAVQDIQkiiKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLA 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-502 |
1.51e-13 |
|
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: 73.30 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGT--LAPAEG-VVTRAARC----------------------------- 67
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGrIIYHVALCekcgyverpskvgepcpvcggtlepeevd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 68 -------LLARVEQHLPDELHQ-------QTLLDALLARLPEA--ERESSAWRAQALLaNMGFAEAAWSLTAGSLSGGQH 131
Cdd:TIGR03269 96 fwnlsdkLRRRIRKRIAIMLQRtfalygdDTVLDNVLEALEEIgyEGKEAVGRAVDLI-EMVQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 132 TRLLLARALIISPDLLLLDEPGNHLDLPTMLW----LEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLqafdlpc 207
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEI------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 208 tqaraalaardesdalrhkaeQKEIDRVTASAKRLATWGQVydnedlaRKAKQME--KQVARLKEeqtelaqgsrwrltL 285
Cdd:TIGR03269 248 ---------------------KEEGTPDEVVAVFMEGVSEV-------EKECEVEvgEPIIKVRN--------------V 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 286 SGDALAADRllelenlAVSAAPDTPTLftlplaRLKSGDRVALLGHNGCGKSSLLRLLW--RQWQTGE------------ 351
Cdd:TIGR03269 286 SKRYISVDR-------GVVKAVDNVSL------EVKEGEIFGIVGTSGAGKTTLSKIIAgvLEPTSGEvnvrvgdewvdm 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 352 TVPGVTFHPRVS--LGYYDQSLHQLP-----DNATLLEALEpFAPELQQRK--LALISAGF--PWARH--GQRVDTLSGG 418
Cdd:TIGR03269 353 TKPGPDGRGRAKryIGILHQEYDLYPhrtvlDNLTEAIGLE-LPDELARMKavITLKMVGFdeEKAEEilDKYPDELSEG 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 419 ERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTL--------QTFegglLLVTHDRTLMEASCNRFWLVEDGGLS 490
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkareemeQTF----IIVSHDMDFVLDVCDRAALMRDGKIV 507
|
570
....*....|..
gi 495164891 491 EWHNMEALLARL 502
Cdd:TIGR03269 508 KIGDPEEIVEEL 519
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
320-489 |
1.57e-13 |
|
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: 68.96 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP--------GVTFHP-----RVSLGYYDQSLhQLPDNATLLEALEp 386
Cdd:cd03230 23 VEKGEIYGLLGPNGAGKTTLIKII-----LGLLKPdsgeikvlGKDIKKepeevKRRIGYLPEEP-SLYENLTVRENLK- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 387 fapelqqrklalisagfpwarhgqrvdtLSGGERSRLLFVgLSLARY-SLLMLDEPTNHLDMEGKEALAQTLQTF--EGG 463
Cdd:cd03230 96 ----------------------------LSGGMKQRLALA-QALLHDpELLILDEPTSGLDPESRREFWELLRELkkEGK 146
|
170 180
....*....|....*....|....*..
gi 495164891 464 L-LLVTHDRTLMEASCNRFWLVEDGGL 489
Cdd:cd03230 147 TiLLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-200 |
1.62e-13 |
|
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: 70.75 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV----------TRAA-----RCLLARVEQH---LPdelh 81
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVlidgqdiaamSRKElrelrRKKISMVFQSfalLP---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 82 QQTLLDAL-----LARLPEAERESsawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHL 156
Cdd:cd03294 116 HRTVLENVafgleVQGVPRAEREE---RAAEALELVGLEGWEHKY-PDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495164891 157 DlPT--------MLWLEQFLARwngSFILVSHDsalLDS---VTNRTWILRDGQL 200
Cdd:cd03294 192 D-PLirremqdeLLRLQAELQK---TIVFITHD---LDEalrLGDRIAIMKDGRL 239
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-202 |
1.70e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.64 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGtLAPAEGVVTRAARCL-------LARVEQHLPdelHQQTLLDAL--- 89
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLsdwsaaeLARHRAYLS---QQQSPPFAMpvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 ----LARLPEAERESSAWRAQALLANMGFAEA-AWSLTAgsLSGGQHTRLLLARALI-----ISPD--LLLLDEPGNHLD 157
Cdd:COG4138 88 qylaLHQPAGASSEAVEQLLAQLAEALGLEDKlSRPLTQ--LSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495164891 158 ----LPTMLWLEQFlARWNGSFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:COG4138 166 vaqqAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVA 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-202 |
1.77e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.23 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV----------TRAARCLLARVE-------QHL-PDELH 81
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsklSSAAKAELRNQKlgfiyqfHHLlPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 82 QQTLLDALLarLPEAERESSAWRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTM 161
Cdd:PRK11629 105 LENVAMPLL--IGKKKPAEINSRALEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495164891 162 LWLEQFLARWN----GSFILVSHDSALLDSVtNRTWILRDGQLQA 202
Cdd:PRK11629 182 DSIFQLLGELNrlqgTAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-181 |
1.95e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.50 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 4 LLTAHSLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT---------RAARCLLARVEQ 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpvegpGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 75 HLPdelhQQTLLDAL-----LARLPEAERESsawRAQALLANMGFAEAA----WSLtagslSGGQHTRLLLARALIISPD 145
Cdd:PRK11248 81 LLP----WRNVQDNVafglqLAGVEKMQRLE---IAHQMLKKVGLEGAEkryiWQL-----SGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495164891 146 LLLLDEPGNHLDLPTMLWLEQFLAR-WNGS---FILVSHD 181
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKlWQETgkqVLLITHD 188
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
265-475 |
2.29e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.92 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 265 VARLKEEQTELAQGSRWRLTLSGDALAADRLLELENLAVsAAPDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRL-- 342
Cdd:COG4178 332 VDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAia 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 343 -LWrQWQTGE-TVP---GVTF---HPRVSLG------YYDQSLHQLPDnATLLEALE-----PFAPELQQRKlalisagf 403
Cdd:COG4178 411 gLW-PYGSGRiARPagaRVLFlpqRPYLPLGtlrealLYPATAEAFSD-AELREALEavglgHLAERLDEEA-------- 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495164891 404 PWARhgqrvdTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQT--FEGGLLLVTHDRTLME 475
Cdd:COG4178 481 DWDQ------VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGHRSTLAA 548
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-158 |
2.72e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQH--LPDELHQQTLL 86
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLvagddvealsaRAASRRVASVPQDtsLSFEFDVRQVV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 87 DalLARLPEAERESSAWRA------QALLANMGFAEAAWSLTagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL 158
Cdd:PRK09536 99 E--MGRTPHRSRFDTWTETdraaveRAMERTGVAQFADRPVT--SLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-198 |
3.09e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.02 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 21 NALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT------------RAARCLLARVEQH--LPDEL------ 80
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhieglpghQIARMGVVRTFQHvrLFREMtvienl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 81 ----HQQ---TLLDALLA--RLPEAERESSAwRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDE 151
Cdd:PRK11300 102 lvaqHQQlktGLFSGLLKtpAFRRAESEALD-RAATWLERVGLLEHA-NRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 152 PGNHLDLPTMLWLEQFLAR----WNGSFILVSHDSALLDSVTNRTWILRDG 198
Cdd:PRK11300 180 PAAGLNPKETKELDELIAElrneHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-157 |
3.64e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.04 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL-----------LARVEQHLPDELHQQTLL 86
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLseetvwdvrrqVGMVFQNPDNQFVGATVQ 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164891 87 DALLARLPE--AERESSAWRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PRK13635 101 DDVAFGLENigVPREEMVERVDQALRQVGMEDFLNREPH-RLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
17-202 |
4.03e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 17 GPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLaPAEGVVTRAARCL-------LAR----------------VE 73
Cdd:PRK03695 9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLeawsaaeLARhraylsqqqtppfampVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 74 QHLPDELHQQTLLDALLARLPEAereSSAWRAQALLANMgfaeaawsltAGSLSGGQHTRLLLARA-LIISPD------L 146
Cdd:PRK03695 88 QYLTLHQPDKTRTEAVASALNEV---AEALGLDDKLGRS----------VNQLSGGEWQRVRLAAVvLQVWPDinpagqL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 147 LLLDEPGNHLDLPTMLWLEQFL---ARWNGSFILVSHDsalldsvTNRT-------WILRDGQLQA 202
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLselCQQGIAVVMSSHD-------LNHTlrhadrvWLLKQGKLLA 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
320-502 |
4.19e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 68.94 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP--G--------VTFHP---RVSLGYYDQSLHqLPDNATLLEALEP 386
Cdd:COG1131 23 VEPGEIFGLLGPNGAGKTTTIRML-----LGLLRPtsGevrvlgedVARDPaevRRRIGYVPQEPA-LYPDLTVRENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 387 FA-------PELQQRKLALISA-GFPWARHgQRVDTLSGGERSRLlfvGLSLA---RYSLLMLDEPTNHLDMEGKEALAQ 455
Cdd:COG1131 97 FArlyglprKEARERIDELLELfGLTDAAD-RKVGTLSGGMKQRL---GLALAllhDPELLILDEPTSGLDPEARRELWE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495164891 456 TLQTF--EG-GLLLVTHDRTLMEASCNRFWLVEDGGLSEWHNMEALLARL 502
Cdd:COG1131 173 LLRELaaEGkTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-152 |
5.47e-13 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 68.71 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------------RAARCL------------------ 68
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRldgeditklppheRARAGIayvpqgreifprltveen 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 69 -------LARVEQHLPDELHQQ-TLLDALLARLpeaeressawraqallanmgfaeaawsltAGSLSGGQHTRLLLARAL 140
Cdd:TIGR03410 96 lltglaaLPRRSRKIPDEIYELfPVLKEMLGRR-----------------------------GGDLSGGQQQQLAIARAL 146
|
170
....*....|..
gi 495164891 141 IISPDLLLLDEP 152
Cdd:TIGR03410 147 VTRPKLLLLDEP 158
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-192 |
6.21e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 22 ALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarCLLARVEQHLPDELHQQTLldaLLARLPEAERESS 101
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-----LWQGEPIRRQRDEYHQDLL---YLGHQPGIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 102 AW---RAQALLANMGFAEAAWS------------LTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQ 166
Cdd:PRK13538 91 ALenlRFYQRLHGPGDDEALWEalaqvglagfedVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170 180
....*....|....*....|....*....
gi 495164891 167 FLARW---NGSFILVSHDSALLDSVTNRT 192
Cdd:PRK13538 171 LLAQHaeqGGMVILTTHQDLPVASDKVRK 199
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
319-503 |
6.47e-13 |
|
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: 68.73 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVPGV-------------TFHPRVSLGYYDQSLHqLPDNATLLEALE 385
Cdd:COG4555 23 TAKDGEITGLLGPNGAGKTTLLRML-----AGLLKPDSgsilidgedvrkePREARRQIGVLPDERG-LYDRLTVRENIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 386 PFAP-------ELQQRKLALISA-GFPWARHgQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTL 457
Cdd:COG4555 97 YFAElyglfdeELKKRIEELIELlGLEEFLD-RRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREIL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495164891 458 QTF---EGGLLLVTHDRTLMEASCNRFWLVEDGGLSEWHNMEALLARLR 503
Cdd:COG4555 176 RALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-181 |
7.38e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.61 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRIDSP-----FGPE-----LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------- 62
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvkrglFKPErlvkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdllk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 63 --RAARCLLAR------------------VEQHLPDELHQQTLLDAllarlpeAERESsawRAQALLANMGFAEAAWSLT 122
Cdd:PRK11308 82 adPEAQKLLRQkiqivfqnpygslnprkkVGQILEEPLLINTSLSA-------AERRE---KALAMMAKVGLRPEHYDRY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 123 AGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD-------LPTMLWLEQFLarwNGSFILVSHD 181
Cdd:PRK11308 152 PHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvsvqaqvLNLMMDLQQEL---GLSYVFISHD 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-181 |
7.89e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 69.79 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVE----------QHLpdelhqqtlldAL 89
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPprerrvgfvfQHY-----------AL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 -------------LARLPEAERESSAwRAQALLANM---GFAEAawslTAGSLSGGQHTRLLLARALIISPDLLLLDEPG 153
Cdd:COG1118 87 fphmtvaeniafgLRVRPPSKAEIRA-RVEELLELVqleGLADR----YPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190
....*....|....*....|....*....|....
gi 495164891 154 NHLD------LptMLWLEQFLARWNGSFILVSHD 181
Cdd:COG1118 162 GALDakvrkeL--RRWLRRLHDELGGTTVFVTHD 193
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
326-489 |
7.97e-13 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 67.92 E-value: 7.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 326 VALLGHNGCGKSSLLRLLwrqwqTGETVP--GVTF-----------HPRVSLGYYDQSLhQLPDNATLLEALEPFA---- 388
Cdd:cd03263 31 FGLLGHNGAGKTTTLKML-----TGELRPtsGTAYingysirtdrkAARQSLGYCPQFD-ALFDELTVREHLRFYArlkg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 389 -PELQQRKLA---LISAGFPWARHgQRVDTLSGGERsRLLFVGLSLARYS-LLMLDEPTNHLDMEGKEALAQTLQTFEGG 463
Cdd:cd03263 105 lPKSEIKEEVellLRVLGLTDKAN-KRARTLSGGMK-RKLSLAIALIGGPsVLLLDEPTSGLDPASRRAIWDLILEVRKG 182
|
170 180
....*....|....*....|....*...
gi 495164891 464 --LLLVTHDRTLMEASCNRFWLVEDGGL 489
Cdd:cd03263 183 rsIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-198 |
9.58e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.47 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT----------RAARCLLARVEQHlpDELHQQ-TLL 86
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpvparaRLARARIGVVPQF--DNLDLEfTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 DALLA-----RLPEAERESsawraqALLANMGFA--EAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP 159
Cdd:PRK13536 133 ENLLVfgryfGMSTREIEA------VIPSLLEFArlESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495164891 160 T--MLW--LEQFLARwNGSFILVSHDSALLDSVTNRTWILRDG 198
Cdd:PRK13536 207 ArhLIWerLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
23-199 |
1.12e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.86 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------------RAARCLLAR--------VEQHLPDELH 81
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMldgvdlshvppyqRPINMMFQSyalfphmtVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 82 QQtlldallaRLPEAERESsawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD--LP 159
Cdd:PRK11607 118 QD--------KLPKAEIAS---RVNEMLGLVHMQEFA-KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495164891 160 TMLWLE--QFLARWNGSFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:PRK11607 186 DRMQLEvvDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-152 |
1.54e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTR-----AARCLLAR-----------------VEQHLpdELH 81
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIATRrrvgymsqafslygeltVRQNL--ELH 363
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495164891 82 qqtlldALLARLPEAERESsawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:NF033858 364 ------ARLFHLPAAEIAA---RVAEMLERFDLADVADAL-PDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
295-483 |
1.64e-12 |
|
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: 66.73 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 295 LLELENLAVSaaPDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLL------------WRqwqtGETVPGVTFHPRV 362
Cdd:COG4133 2 MLEAENLSCR--RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILagllppsagevlWN----GEPIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 363 SLGYydqSLHQ--LPDNATLLEALE------PFAPELQQRKLALISAGFPWARHgQRVDTLSGGERSRLLFVGLSLARYS 434
Cdd:COG4133 76 RLAY---LGHAdgLKPELTVRENLRfwaalyGLRADREAIDEALEAVGLAGLAD-LPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 435 LLMLDEPTNHLDMEGKEALAQTLQTF--EGGLLLVTHDRTLMEASCNRFWL 483
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHlaRGGAVLLTTHQPLELAAARVLDL 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-201 |
2.05e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.73 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARClLARVEQHLPDELHQQTL------------LD 87
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEARAKLRAKHVgfvfqsfmliptLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ALL-ARLP-----EAERESSAwRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTM 161
Cdd:PRK10584 105 ALEnVELPallrgESSRQSRN-GAKALLEQLGLGKRLDHLPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 162 LWLEQFLARWNGSF----ILVSHDSALLdSVTNRTWILRDGQLQ 201
Cdd:PRK10584 183 DKIADLLFSLNREHgttlILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
16-152 |
2.32e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 66.94 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 16 FGPE--LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------------RAARCLLARVEQ------ 74
Cdd:COG1126 11 FGDLevLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITvdgedltdskkdiNKLRRKVGMVFQqfnlfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 75 HLpdelhqqTLLD-ALLA-----RLPEAERESsawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLL 148
Cdd:COG1126 91 HL-------TVLEnVTLApikvkKMSKAEAEE---RAMELLERVGLADKADAY-PAQLSGGQQQRVAIARALAMEPKVML 159
|
....
gi 495164891 149 LDEP 152
Cdd:COG1126 160 FDEP 163
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
318-505 |
2.56e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 69.43 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 318 ARLKSGDRVALLGHNGCGKSSLLRLLWRQWQTGETvpGVTFHPRVSLGYYDQSLHQLPDNAT-----------LLEALEP 386
Cdd:PRK10636 22 ATINPGQKVGLVGKNGCGKSTLLALLKNEISADGG--SYTFPGNWQLAWVNQETPALPQPALeyvidgdreyrQLEAQLH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 387 FAPE---------------------LQQRKLALISA-GFPWARHGQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNH 444
Cdd:PRK10636 100 DANErndghaiatihgkldaidawtIRSRAASLLHGlGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495164891 445 LDMEGKEALAQTLQTFEGGLLLVTHDRTLMEASCNRFWLVEDGGLSEWHNMEALLARLRAA 505
Cdd:PRK10636 180 LDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRAT 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-203 |
2.58e-12 |
|
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: 66.59 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 19 ELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGvvtraaRCLLARVE-QHLPdelhqqtlldallarlPEAE 97
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSG------KILLNGKDiTNLP----------------PEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 98 RESSAWRAQALLANMG-FAEAAWSL-----------------------------TAGSLSGGQHTRLLLARALIISPDLL 147
Cdd:cd03299 72 DISYVPQNYALFPHMTvYKNIAYGLkkrkvdkkeierkvleiaemlgidhllnrKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 148 LLDEPGNHLDLPTMLWLEQFLARWNGSF----ILVSHDSALLDSVTNRTWILRDGQLQAF 203
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFgvtvLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-200 |
2.68e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCL-LARVEQHLpdelhqqTLLD 87
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfrspRDAQAAgIAIIHQEL-------NLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 AL-------LARLP--------EAEREssawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:COG1129 93 NLsvaenifLGREPrrgglidwRAMRR----RARELLARLGLDIDPDTP-VGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495164891 153 --------GNHL-DLptmlwLEQFLARwnG-SFILVSHD----SALLDSVTnrtwILRDGQL 200
Cdd:COG1129 168 tasltereVERLfRI-----IRRLKAQ--GvAIIYISHRldevFEIADRVT----VLRDGRL 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-186 |
2.72e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.52 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRIDSPFGPELNA--------LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTL--APAEGVVtraarcllA 70
Cdd:COG2401 19 SVLDLSERVAIVLEAFGVELRVveryvlrdLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV--------D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 71 RVEQHLPDELhqqTLLDALLARLPEAEressawrAQALLANMGFAEAA-WSLTAGSLSGGQHTRLLLARALIISPDLLLL 149
Cdd:COG2401 91 VPDNQFGREA---SLIDAIGRKGDFKD-------AVELLNAVGLSDAVlWLRRFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495164891 150 DEPGNHLDLPTmlwlEQFLA--------RWNGSFILVSHDSALLD 186
Cdd:COG2401 161 DEFCSHLDRQT----AKRVArnlqklarRAGITLVVATHHYDVID 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
16-191 |
2.93e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.65 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 16 FGPE--LNALSFTLKKGDRIGLIGHNGCGKSTLLKAL-------------DGTLAPAEGVVTRAARCLLARVEQ--HLpd 78
Cdd:PRK09493 11 FGPTqvLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitsgdlivDGLKVNDPKVDERLIRQEAGMVFQqfYL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 79 eLHQQTLLDALL---ARLPEAERESSAWRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNH 155
Cdd:PRK09493 89 -FPHLTALENVMfgpLRVRGASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495164891 156 LDlPTM----LWLEQFLARWNGSFILVSHDSALLDSVTNR 191
Cdd:PRK09493 167 LD-PELrhevLKVMQDLAEEGMTMVIVTHEIGFAEKVASR 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-200 |
3.31e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 14 SPFGPE-LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDELHQQTlldALLAR 92
Cdd:PRK13646 16 TPYEHQaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRI---GMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 93 LPEA-------ERE-------------SSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:PRK13646 93 FPESqlfedtvEREiifgpknfkmnldEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495164891 153 GNHLD----LPTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:PRK13646 173 TAGLDpqskRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-180 |
3.96e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 66.97 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 8 HSLRIDSPFgpELNAL---SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQ---------- 74
Cdd:PRK13634 10 HRYQYKTPF--ERRALydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkplrkkv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 75 ----HLPDelHQqtLLDALLAR----------LPEAERESsawRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARAL 140
Cdd:PRK13634 88 givfQFPE--HQ--LFEETVEKdicfgpmnfgVSEEDAKQ---KAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 141 IISPDLLLLDEPGNHLD----LPTMLWLEQFLARWNGSFILVSH 180
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDpkgrKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-157 |
5.04e-12 |
|
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: 66.02 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQHlPDeLHQQTLLDA 88
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldgvdirdlnlRWLRSQIGLVSQE-PV-LFDGTIAEN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495164891 89 LLARLPEAERESsAWRAqALLAN-----MGFAEAAWSLT---AGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:cd03249 97 IRYGKPDATDEE-VEEA-AKKANihdfiMSLPDGYDTLVgerGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-202 |
5.41e-12 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 66.30 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT------------RAARCLLARVEQHlPDelHQ--- 82
Cdd:TIGR04520 16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvdgldtldeenlWEIRKKVGMVFQN-PD--NQfvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 83 QTLLDAlLA------RLPEAE-REssawRAQALLANMG---FAEAAWSLtagsLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:TIGR04520 93 ATVEDD-VAfglenlGVPREEmRK----RVDEALKLVGmedFRDREPHL----LSGGQKQRVAIAGVLAMRPDIIILDEA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495164891 153 GNHLD-------LPTMLWL--EQflarwNGSFILVSHDsalLDSVTN--RTWILRDGQLQA 202
Cdd:TIGR04520 164 TSMLDpkgrkevLETIRKLnkEE-----GITVISITHD---MEEAVLadRVIVMNKGKIVA 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
297-487 |
5.43e-12 |
|
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: 64.97 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 297 ELENLAVSAAPDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRL---LWRQWQTGETVPGVTFHPRV---SLGYYDQS 370
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSL-DLYAGEIIALTGKNGAGKTTLAKIlagLIKESSGSILLNGKPIKAKErrkSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 371 L-HQLPDNATLLEALE--PFAPELQQRKLALISAGFPWARHGQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDM 447
Cdd:cd03226 80 VdYQLFTDSVREELLLglKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495164891 448 EGKEALAQ---TLQTFEGGLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:cd03226 160 KNMERVGElirELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-157 |
5.50e-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: 64.64 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTraarclLARVEQHLpdelhQQTLLDALLARLPEAERE 99
Cdd:cd03247 18 LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT------LDGVPVSD-----LEKALSSLISVLNQRPYL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 100 SSAwraqALLANMGfaeaawsltaGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:cd03247 87 FDT----TLRNNLG----------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-199 |
6.89e-12 |
|
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: 67.79 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 3 TLLTAHSLRIDSP-----FGPE------LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGtLAPAEGVVT--------- 62
Cdd:COG4172 274 PLLEARDLKVWFPikrglFRRTvghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRfdgqdldgl 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 63 --RAARCLLAR-----------------VEQHL--PDELHQQtlldallaRLPEAERESsawRAQALLANMGfaeaawsL 121
Cdd:COG4172 353 srRALRPLRRRmqvvfqdpfgslsprmtVGQIIaeGLRVHGP--------GLSAAERRA---RVAEALEEVG-------L 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 122 TAGSL-------SGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT---MLWLEQFL-ARWNGSFILVSHDSALLDSVTN 190
Cdd:COG4172 415 DPAARhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVqaqILDLLRDLqREHGLAYLFISHDLAVVRALAH 494
|
....*....
gi 495164891 191 RTWILRDGQ 199
Cdd:COG4172 495 RVMVMKDGK 503
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-206 |
6.92e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.03 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGV-------VTRaarcLLAR------VEQHLPDELHQqTLL 86
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHirfhgtdVSR----LHARdrkvgfVFQHYALFRHM-TVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 DAL---LARLPEAERESSA---WRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:PRK10851 93 DNIafgLTVLPRRERPNAAaikAKVTQLLEMVQLAHLADRYPA-QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495164891 161 ML----WLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:PRK10851 172 RKelrrWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-201 |
7.47e-12 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 64.97 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEG-------VVT--RAARCLLARVEQHLPDELHQqTLLDAL- 89
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGriyiggrDVTdlPPKDRDIAMVFQNYALYPHM-TVYDNIa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 ----LARLPEAERESSAWRAQALLAnmgfAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD----LPTM 161
Cdd:cd03301 95 fglkLRKVPKDEIDERVREVAELLQ----IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495164891 162 LWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQ 201
Cdd:cd03301 171 AELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
7.60e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.21 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRIDSPFGPE----LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL-------L 69
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEqvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldadaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 70 ARVEQ----------HLPDEL--HQQTLLDALLARLPEAERESsawRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLA 137
Cdd:PRK10535 81 AQLRRehfgfifqryHLLSHLtaAQNVEVPAVYAGLERKQRLL---RAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 138 RALIISPDLLLLDEPGNHLD----LPTMLWLEQFLARWNgSFILVSHDsALLDSVTNRTWILRDGQLQAFdlPCTQARAA 213
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDshsgEEVMAILHQLRDRGH-TVIIVTHD-PQVAAQAERVIEIRDGEIVRN--PPAQEKVN 232
|
....*..
gi 495164891 214 LAARDES 220
Cdd:PRK10535 233 VAGGTEP 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-157 |
8.75e-12 |
|
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: 64.30 E-value: 8.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtRAARCLLARVEQHLPDELHQQTLLDALLARLPEAER- 98
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-RWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENl 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 99 -------ESSAWRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:TIGR01189 95 hfwaaihGGAQRTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-206 |
9.09e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 65.98 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 13 DSPfGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAP---AEGVVTRAARCLLAR-----------VEQHLPD 78
Cdd:PRK13640 17 DSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKtvwdirekvgiVFQNPDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 79 ELHQQTLLDALLARLP--EAERESSAWRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHL 156
Cdd:PRK13640 96 QFVGATVGDDVAFGLEnrAVPRPEMIKIVRDVLADVGMLDYIDSEPA-NLSGGQKQRVAIAGILAVEPKIIILDESTSML 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 157 DlPT----MLWLEQFLARWNG-SFILVSHD---SALLDSVTnrtwILRDGQLQAFDLP 206
Cdd:PRK13640 175 D-PAgkeqILKLIRKLKKKNNlTVISITHDideANMADQVL----VLDDGKLLAQGSP 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-157 |
9.43e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.90 E-value: 9.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQH---LPDE--LHQ-QTLLDAL--LA 91
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigyLPEErgLYPkMKVGEQLvyLA 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495164891 92 RL-----PEAERessawRAQALLANMGFAEaAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:COG4152 97 RLkglskAEAKR-----RADEWLERLGLGD-RANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-202 |
1.00e-11 |
|
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: 64.70 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT----------RAARCLLARV--EQHLPDELHQQTLLd 87
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvvkepAEARRRLGFVsdSTGLYDRLTARENL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ALLARLPEAERESSAWRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQF 167
Cdd:cd03266 100 EYFAGLYGLKGDELTARLEELADRLGMEELL-DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 495164891 168 LA--RWNGSFILVS-HDSALLDSVTNRTWILRDGQLQA 202
Cdd:cd03266 179 IRqlRALGKCILFStHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-157 |
1.16e-11 |
|
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: 64.11 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPA--EGVVT--------RAARCLLARVEQHlpdelhqqtllDAL 89
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLingrpldkRSFRKIIGYVPQD-----------DIL 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 90 LARLPEAEressawraqallaNMGFAeAAWSltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:cd03213 94 HPTLTVRE-------------TLMFA-AKLR----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
296-501 |
1.35e-11 |
|
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: 67.09 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTL----FTLPlarlkSGDRVALLGHNGCGKSSLLRLL--WRQWQTGE-TVPGVTFHP------RV 362
Cdd:COG4988 337 IELEDVSFSYPGGRPALdglsLTIP-----PGERVALVGPSGAGKSTLLNLLlgFLPPYSGSiLINGVDLSDldpaswRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 363 SLGYYDQSLHQLP----DN----------ATLLEALE-----PFAPELQQRKLALISAGfpwarhGQRvdtLSGGERSRL 423
Cdd:COG4988 412 QIAWVPQNPYLFAgtirENlrlgrpdasdEELEAALEaagldEFVAALPDGLDTPLGEG------GRG---LSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 424 lfvglSLAR-----YSLLMLDEPTNHLDMEGKEALAQTLQTFEGG--LLLVTHDRTLMeASCNRFWLVEDGGLSEWHNME 496
Cdd:COG4988 483 -----ALARallrdAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALL-AQADRILVLDDGRIVEQGTHE 556
|
....*
gi 495164891 497 ALLAR 501
Cdd:COG4988 557 ELLAK 561
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-201 |
1.36e-11 |
|
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: 67.73 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQ------HLP-----DEL---HQQ 83
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDvhqnmgYCPqfdaiDDLltgREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLDALLARLPEAERESSA-WRAQALlanmGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT-- 160
Cdd:TIGR01257 2033 LYLYARLRGVPAEEIEKVAnWSIQSL----GLSLYADRL-AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQArr 2107
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495164891 161 MLW-LEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQ 201
Cdd:TIGR01257 2108 MLWnTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-152 |
1.43e-11 |
|
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: 63.22 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 3 TLLTAHSLRIDSPFGPelnaLSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcllarveqhlpdELHQ 82
Cdd:cd03215 3 PVLEVRGLSVKGAVRD----VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK------------PVTR 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495164891 83 QTLLDAL---LARLPEaERessawRAQALLANMGFAEaawSLTAGS-LSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:cd03215 67 RSPRDAIragIAYVPE-DR-----KREGLVLDLSVAE---NIALSSlLSGGNQQKVVLARWLARDPRVLILDEP 131
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-180 |
1.48e-11 |
|
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: 64.41 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 15 PFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL-------LARVEQHLPDE--LHQQTL 85
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsqyehkyLHSKVSLVGQEpvLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LDALLARLPEAERESSAWRAQALLAN---MGFAEAAWSLT---AGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP 159
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHsfiSELASGYDTEVgekGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180
....*....|....*....|...
gi 495164891 160 TMLWLEQFLARW--NGSFILVSH 180
Cdd:cd03248 185 SEQQVQQALYDWpeRRTVLVIAH 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-200 |
1.51e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.77 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT------RAARCLlaRVEQHLPDELHQQ---------- 83
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditiDTARSL--SQQKGLIRQLRQHvgfvfqnfnl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 ----TLLDALL---ARLPEAERESSAWRAQALLANMGFA--EAAWsltAGSLSGGQHTRLLLARALIISPDLLLLDEPGN 154
Cdd:PRK11264 97 fphrTVLENIIegpVIVKGEPKEEATARARELLAKVGLAgkETSY---PRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495164891 155 HLD-------LPTMlwleQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:PRK11264 174 ALDpelvgevLNTI----RQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-191 |
1.79e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.50 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 21 NALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDELHQ-QTLLDALLARL------ 93
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDiQMIFQDPLASLnprmti 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 94 ------------PEAERESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL--- 158
Cdd:PRK15079 118 geiiaeplrtyhPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVsiq 197
|
170 180 190
....*....|....*....|....*....|....
gi 495164891 159 PTMLWLEQFLARWNG-SFILVSHDSALLDSVTNR 191
Cdd:PRK15079 198 AQVVNLLQQLQREMGlSLIFIAHDLAVVKHISDR 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-229 |
1.79e-11 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 65.89 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 19 ELNAlSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLL-ARVEQHLPDEL--------------H-- 81
Cdd:COG4148 15 TLDV-DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQdSARGIFLPPHRrrigyvfqearlfpHls 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 82 -QQTLLDALlARLPEAERESSAWRAQALLanmGFAEaawsL---TAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:COG4148 94 vRGNLLYGR-KRAPRAERRISFDEVVELL---GIGH----LldrRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 158 LPT----MLWLEQFLARWNGSFILVSHDsalLDSV---TNRTWILRDGQLQAFDLPctqarAALAARDESDALRHKAEQ 229
Cdd:COG4148 166 LARkaeiLPYLERLRDELDIPILYVSHS---LDEVarlADHVVLLEQGRVVASGPL-----AEVLSRPDLLPLAGGEEA 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-157 |
2.09e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 64.26 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKAL-------DGTLAPA-------EGVVTRAARCLLARV-----EQHLPDEL 80
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAghqfdfsQKPSEKAIRLLRQKVgmvfqQYNLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 81 hqqTLLDALLA---RLPEAERESSAWRAQALLANMGFAEAA--WSLtagSLSGGQHTRLLLARALIISPDLLLLDEPGNH 155
Cdd:COG4161 98 ---TVMENLIEapcKVLGLSKEQAREKAMKLLARLRLTDKAdrFPL---HLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
..
gi 495164891 156 LD 157
Cdd:COG4161 172 LD 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
320-501 |
2.41e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.39 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLWRQW--QTGE-TVPGVTFHP------RVSLGYYDQSLHQLpdNATLLEALEPFAPE 390
Cdd:PRK11160 363 IKAGEKVALLGRTGCGKSTLLQLLTRAWdpQQGEiLLNGQPIADyseaalRQAISVVSQRVHLF--SATLRDNLLLAAPN 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 391 ---------LQQ---RKLALISAGF-PWARHGQRvdTLSGGERSRllfvgLSLARY-----SLLMLDEPTNHLDMEG-KE 451
Cdd:PRK11160 441 asdealievLQQvglEKLLEDDKGLnAWLGEGGR--QLSGGEQRR-----LGIARAllhdaPLLLLDEPTEGLDAETeRQ 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 452 ALAQTLQTFEG-GLLLVTHDRTLMEaSCNRFWLVEDGGLSEWHNMEALLAR 501
Cdd:PRK11160 514 ILELLAEHAQNkTVLMITHRLTGLE-QFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-179 |
2.70e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.83 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT----------RAARCLLARVEQHL---PDELHQQTLL 86
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsraRHARQRVGVVPQFDnldPDFTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 daLLARLPEAERESSAWRAQALLAnmgFA--EAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT--ML 162
Cdd:PRK13537 103 --VFGRYFGLSAAAARALVPPLLE---FAklENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQArhLM 177
|
170
....*....|....*....
gi 495164891 163 W--LEQFLARwnGSFILVS 179
Cdd:PRK13537 178 WerLRSLLAR--GKTILLT 194
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-206 |
2.70e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.02 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------RAARCLLARVEQHLPdelhQQTLLDA---- 88
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrplaDWSPAELARRRAVLP----QHSSLSFpftv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 ----LLARLP------EAERESSAWRAQALLAnmGFAEAAWSltagSLSGGQHTRLLLARALI------ISPDLLLLDEP 152
Cdd:PRK13548 94 eevvAMGRAPhglsraEDDALVAAALAQVDLA--HLAGRDYP----QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 153 GNHLDL----PTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:PRK13548 168 TSALDLahqhHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-225 |
2.71e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.62 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARveqhLPDE-----LHQQTLLDALLA------- 91
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL----PPAErpvsmLFQENNLFPHLTvaqnigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 92 ------RLPEAEREssawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDlPT----M 161
Cdd:COG3840 95 glrpglKLTAEQRA----QVEQALERVGLAGLLDRL-PGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD-PAlrqeM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495164891 162 LWLEQFLARWNGSFIL-VSHDSALLDSVTNRTWILRDGQLQAfdlpcTQARAALAARDESDALRH 225
Cdd:COG3840 169 LDLVDELCRERGLTVLmVTHDPEDAARIADRVLLVADGRIAA-----DGPTAALLDGEPPPALAA 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-199 |
2.94e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDgTLAPAEGVVTRAARCL--LARvEQHLPDELHQQTLLD----ALLAR- 92
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWFDGQPLhnLNR-RQLLPVRHRIQVVFQdpnsSLNPRl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 93 ----------------LPEAERESsawRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHL 156
Cdd:PRK15134 380 nvlqiieeglrvhqptLSAAQREQ---QVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495164891 157 DLPT----MLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:PRK15134 457 DKTVqaqiLALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
287-470 |
3.35e-11 |
|
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: 65.84 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 287 GDALAADRLLELENLAVSAAPDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLWRQW--QTGE-TVPGVTFHP--- 360
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGYPGAPPVLDGVSL-DLPPGERVAILGPSGSGKSTLLATLAGLLdpLQGEvTLDGVPVSSldq 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 361 ---RVSLGYYDQSLHQLpdNATLLEALEPFAPELQQRKL--ALISAGF-PWARH---------GQRVDTLSGGERSRLLF 425
Cdd:TIGR02868 405 devRRRVSVCAQDAHLF--DTTVRENLRLARPDATDEELwaALERVGLaDWLRAlpdgldtvlGEGGARLSGGERQRLAL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495164891 426 VGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQTFEGGL--LLVTHD 470
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRtvVLITHH 529
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-200 |
4.03e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.34 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 19 ELNAL---SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV---------------------------------- 61
Cdd:PRK13651 19 ELKALdnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 62 -TRAARCLLARVEQHLPDELHQQTLLDALL--ARLPEAERESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLAR 138
Cdd:PRK13651 99 kIKEIRRRVGVVFQFAEYQLFEQTIEKDIIfgPVSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 139 ALIISPDLLLLDEPGNHLD---LPTMLWLEQFLARWNGSFILVSHDsalLDSV---TNRTWILRDGQL 200
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD---LDNVlewTKRTIFFKDGKI 243
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
296-501 |
4.12e-11 |
|
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: 63.02 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTL----FTLPlarlkSGDRVALLGHNGCGKSSLLRLLWRQWQT--------GETVPGVTFHP-RV 362
Cdd:cd03253 1 IEFENVTFAYDPGRPVLkdvsFTIP-----AGKKVAIVGPSGSGKSTILRLLFRFYDVssgsilidGQDIREVTLDSlRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 363 SLGYYDQslhqlpD----NATLLEALE---PFAPELQQRKLALISA------GFPWA---RHGQRVDTLSGGERSRllfv 426
Cdd:cd03253 76 AIGVVPQ------DtvlfNDTIGYNIRygrPDATDEEVIEAAKAAQihdkimRFPDGydtIVGERGLKLSGGEKQR---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 427 gLSLARYSL-----LMLDEPTNHLDMEGKEALAQTLQTFEGG--LLLVTHD-RTLMeaSCNRFWLVEDGGLSEWHNMEAL 498
Cdd:cd03253 146 -VAIARAILknppiLLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAHRlSTIV--NADKIIVLKDGRIVERGTHEEL 222
|
...
gi 495164891 499 LAR 501
Cdd:cd03253 223 LAK 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-202 |
4.67e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.60 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHL-----------PDELHQQTLLD- 87
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpDDQVFSSTVWDd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ----ALLARLPEAERESSAWRAQALLANMGFAEAAwsltAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLW 163
Cdd:PRK13647 101 vafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKP----PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495164891 164 LEQFLARWNG---SFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:PRK13647 177 LMEILDRLHNqgkTVIVATHDVDLAAEWADQVIVLKEGRVLA 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-206 |
4.67e-11 |
|
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: 64.44 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 35 LIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLAR---------------------VEQHLPDELHQQtlldallaRL 93
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVpphlrhinmvfqsyalfphmtVEENVAFGLKMR--------KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 94 PEAERESSAWRAQALLANMGFAEAAWSltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD--LPTMLWLE--QFLA 169
Cdd:TIGR01187 73 PRAEIKPRVLEALRLVQLEEFADRKPH----QLSGGQQQRVALARALVFKPKILLLDEPLSALDkkLRDQMQLElkTIQE 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 495164891 170 RWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:TIGR01187 149 QLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
20-157 |
5.01e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 64.33 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT--------------RAARCLLARVEQH--LpdeLHQQ 83
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdltalserelRAARRKIGMIFQHfnL---LSSR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 84 TLLD--AL---LARLPEAERESsawRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:COG1135 98 TVAEnvALpleIAGVPKAEIRK---RVAELLELVGLSDKADAYPS-QLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-157 |
5.03e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTraarclLARVEQHLPDELHQQTLL---DALLARLPEAE-- 97
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK------LDGGDIDDPDVAEACHYLghrNAMKPALTVAEnl 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 98 ------RESSAWRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PRK13539 95 efwaafLGGEELDIAAALEAVGLAPLA-HLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-200 |
5.23e-11 |
|
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: 65.74 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARclLARVEQHL---PDELHQQTLLDALLarlp 94
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQQAwiqNDSLRENILFGKAL---- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 95 EAERESSAWRAQALLANMGFAEAAWSLTAG----SLSGGQHTRLLLARALIISPDLLLLDEP--------GNHLdLPTML 162
Cdd:TIGR00957 726 NEKYYQQVLEACALLPDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSNADIYLFDDPlsavdahvGKHI-FEHVI 804
|
170 180 190
....*....|....*....|....*....|....*...
gi 495164891 163 WLEQFLArwNGSFILVSHDSALLDSVtNRTWILRDGQL 200
Cdd:TIGR00957 805 GPEGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
291-476 |
5.45e-11 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 65.00 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 291 AADRLLELENLAVSAAPDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLWRQWQTGE---TVPGVTFHPRVSLGYY 367
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRRPALRPVSF-TVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEgsiAVNGVPLADADADSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 368 DQS--LHQLPD--NATLLEAL---EPFAPELQQRKlALISAGF-------------PWARHGQRvdtLSGGERSRllfvg 427
Cdd:TIGR02857 396 DQIawVPQHPFlfAGTIAENIrlaRPDASDAEIRE-ALERAGLdefvaalpqgldtPIGEGGAG---LSGGQAQR----- 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 428 LSLARY-----SLLMLDEPTNHLDMEGKEALAQTLQTFEGG--LLLVTHDRTLMEA 476
Cdd:TIGR02857 467 LALARAflrdaPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALAAL 522
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-206 |
5.57e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 64.32 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEG-------VVTR---AARCLlARVEQ------HLpdelhqq 83
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGeiliggrDVTDlppKDRNI-AMVFQsyalypHM------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLD----AL-LARLPEAERESsawRAQALLANMGfaeaawsLT------AGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:COG3839 91 TVYEniafPLkLRKVPKAEIDR---RVREAAELLG-------LEdlldrkPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 153 GNHLD--LPTMLWLE--QFLARWNGSFILVSHDS--ALldSVTNRTWILRDGQLQAFDLP 206
Cdd:COG3839 161 LSNLDakLRVEMRAEikRLHRRLGTTTIYVTHDQveAM--TLADRIAVMNDGRIQQVGTP 218
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
20-199 |
8.16e-11 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 62.51 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKAL------------------------DGTLAPAEGVVTRAARCLLARVEQH 75
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdsgeirvggeeirlkpdrDGELVPADRRQLQRIRTRLGMVFQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 76 LPDELHQqTLLDALLA------RLPEAERESsawRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLL 149
Cdd:COG4598 104 FNLWSHM-TVLENVIEapvhvlGRPKAEAIE---RAEALLAKVGLADKRDAYPA-HLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495164891 150 DEPGNHLDlPTM----LWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:COG4598 179 DEPTSALD-PELvgevLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGR 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-202 |
8.77e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL-------LARVEQHLPDELHQ---QTLLDAL 89
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskaFARKVAYLPQQLPAaegMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 ----------LARLPEAEREssawRAQALLANMGFAEAAWSLTaGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP 159
Cdd:PRK10575 107 aigrypwhgaLGRFGAADRE----KVEEAISLVGLKPLAHRLV-DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495164891 160 ---TMLWLEQFLARWNG-SFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:PRK10575 182 hqvDVLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-201 |
1.26e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.43 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLlarveQHLPDE-LHQQTLLD--AL------- 89
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-----THVPAEnRHVNTVFQsyALfphmtvf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 --------LARLPEAERESSAWRAQALLANMGFAEAAWSltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD--LP 159
Cdd:PRK09452 105 envafglrMQKTPAAEITPRVMEALRMVQLEEFAQRKPH----QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDykLR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495164891 160 TMLWLE-QFLARWNG-SFILVSHDS--ALldSVTNRTWILRDGQLQ 201
Cdd:PRK09452 181 KQMQNElKALQRKLGiTFVFVTHDQeeAL--TMSDRIVVMRDGRIE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
297-480 |
1.51e-10 |
|
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: 61.01 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 297 ELENLAVSAaPDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLWRQ--WQTGE-TVPGVTFHP-RVSLGYYDQSLH 372
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSF-EVKPGEFLAIVGPNGAGKSTLLKAILGLlkPTSGSiRVFGKPLEKeRKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 373 QLPD-NATLLE--------ALEPFAPELQQRKLALISA-------GFpwaRHgQRVDTLSGGERSRLLfvglsLARY--- 433
Cdd:cd03235 79 IDRDfPISVRDvvlmglygHKGLFRRLSKADKAKVDEAlervglsEL---AD-RQIGELSGGQQQRVL-----LARAlvq 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495164891 434 --SLLMLDEPTNHLDMEGKEALAQTLQTF--EG-GLLLVTHDRTLMEASCNR 480
Cdd:cd03235 150 dpDLLLLDEPFAGVDPKTQEDIYELLRELrrEGmTILVVTHDLGLVLEYFDR 201
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-152 |
1.68e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.58 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarcLLARVE-QHLPdeLHQ----------Q--------T 84
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI------FLDGEDiTHLP--MHKrarlgigylpQeasifrklT 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164891 85 LLDALLA-----RLPEAERESsawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:COG1137 95 VEDNILAvlelrKLSKKEREE---RLEELLEEFGITHLRKSK-AYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-160 |
1.78e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.16 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAAR-CLLARVEQHLPDelhqqTLLDALLARLPEA 96
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSPQTSWIMPG-----TIKDNIIFGLSYD 514
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 97 E-RESSAWRAQALLANMG-FAEAAWS-LTAG--SLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:TIGR01271 515 EyRYTSVIKACQLEEDIAlFPEKDKTvLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-200 |
1.79e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.04 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-----------TRAARCLLARV-----EQHLpdeLHQQ 83
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlkNREVPFLRRQIgmifqDHHL---LMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLD--ALLARLPEAERESSAWRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD---L 158
Cdd:PRK10908 95 TVYDnvAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495164891 159 PTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:PRK10908 174 EGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
319-469 |
1.81e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLWRQWQTGET-----VPGVTFHPRVSLgyydqsLHQLPDNATLLEALEpfapelqq 393
Cdd:COG2401 52 EIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVagcvdVPDNQFGREASL------IDAIGRKGDFKDAVE-------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 394 rklALISAG----FPWARhgqRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLD----MEGKEALAQTLQTFEGGLL 465
Cdd:COG2401 118 ---LLNAVGlsdaVLWLR---RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGITLV 191
|
....
gi 495164891 466 LVTH 469
Cdd:COG2401 192 VATH 195
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-157 |
2.05e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.43 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEG--------VVTRAAR----CLLARVEQHLPdelhQQTLLD 87
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedVTHRSIQqrdiCMVFQSYALFP----HMSLGE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495164891 88 AL-----LARLPEAERESSAWRAQALLANMGFAEAawslTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PRK11432 98 NVgyglkMLGVPKEERKQRVKEALELVDLAGFEDR----YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-199 |
2.54e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.10 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRIDspFGPE--LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT---------------R 63
Cdd:PRK11701 3 DQPLLSVRGLTKL--YGPRkgCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlrdlyalsE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 64 AARCLLAR-----VEQHLPDELHQQTLLDA-----LLArlpEAERESSAWRAQAL--LANMGFAEAAWSLTAGSLSGGQH 131
Cdd:PRK11701 81 AERRRLLRtewgfVHQHPRDGLRMQVSAGGnigerLMA---VGARHYGDIRATAGdwLERVEIDAARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495164891 132 TRLLLARALIISPDLLLLDEPGNHLDLPT---MLWLEQFLARWNG-SFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVqarLLDLLRGLVRELGlAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-160 |
2.58e-10 |
|
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: 61.41 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAAR-CLLARVEQHLPDelhqqTLLDALLARLPEA 96
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRiSFSSQFSWIMPG-----TIKENIIFGVSYD 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 97 E-RESSAWRAQALLANMG-FAEAAWSLTAG---SLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:cd03291 126 EyRYKSVVKACQLEEDITkFPEKDNTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-185 |
2.74e-10 |
|
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: 59.09 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 5 LTAHSLRIDSPFG-PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGtLAPA-EGVVTRAARCLLARVEQH--LPdel 80
Cdd:cd03223 1 IELENLSLATPDGrVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPWgSGRIGMPEGEDLLFLPQRpyLP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 81 hQQTLLDALLarLPeaeressawraqallanmgfaeaaWSLTagsLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:cd03223 77 -LGTLREQLI--YP------------------------WDDV---LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....*
gi 495164891 161 MLWLEQFLARWNGSFILVSHDSALL 185
Cdd:cd03223 127 EDRLYQLLKELGITVISVGHRPSLW 151
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-170 |
3.00e-10 |
|
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: 60.36 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTL---APAEGVVTRAARCL--------LARVEQHlpDELH-----QQ 83
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRkpdqfqkcVAYVRQD--DILLpgltvRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLDALLARLPeaeRESSAWRAQALLANMGFAEAAWSLTAGS----LSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP 159
Cdd:cd03234 101 TLTYTAILRLP---RKSSDAIRKKRVEDVLLRDLALTRIGGNlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170
....*....|.
gi 495164891 160 TMLWLEQFLAR 170
Cdd:cd03234 178 TALNLVSTLSQ 188
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
313-489 |
3.09e-10 |
|
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: 60.39 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 313 FTLPLARLKSGDRVALLGHNGCGKSSLLRLLW--------------RQWQTGETVPGVTFHPRvSLGYYDQSLHQLPdNA 378
Cdd:cd03297 13 FTLKIDFDLNEEVTGIFGASGAGKSTLLRCIAglekpdggtivlngTVLFDSRKKINLPPQQR-KIGLVFQQYALFP-HL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 379 TLLEALEPFAPELQQRKL----ALISAGFPWARHGQR-VDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEA- 452
Cdd:cd03297 91 NVRENLAFGLKRKRNREDrisvDELLDLLGLDHLLNRyPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQl 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495164891 453 ---LAQTLQTFEGGLLLVTHDRTLMEASCNRFWLVEDGGL 489
Cdd:cd03297 171 lpeLKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-206 |
3.50e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 61.29 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAA-----------RCLLARVEQHLPDELHQQTLL 86
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdiRHKIGMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 DALLARL-----PEAERESSAWRAQALLANMGFAEAAWSltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTM 161
Cdd:PRK13650 101 DDVAFGLenkgiPHEEMKERVNEALELVGMQDFKEREPA----RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 162 LWLEQFLA----RWNGSFILVSHDsalLDSVT--NRTWILRDGQLQAFDLP 206
Cdd:PRK13650 177 LELIKTIKgirdDYQMTVISITHD---LDEVAlsDRVLVMKNGQVESTSTP 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
320-491 |
3.51e-10 |
|
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: 59.25 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLWRQW--QTGE-TVPGVTFHP-----RVSLGYYDQSLHQLpdNATLLEALepfapel 391
Cdd:cd03247 25 LKQGEKIALLGRSGSGKSTLLQLLTGDLkpQQGEiTLDGVPVSDlekalSSLISVLNQRPYLF--DTTLRNNL------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 392 qqrklalisagfpwarhGQRvdtLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTL--QTFEGGLLLVTH 469
Cdd:cd03247 96 -----------------GRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIfeVLKDKTLIWITH 155
|
170 180
....*....|....*....|..
gi 495164891 470 DRTLMEAScNRFWLVEDGGLSE 491
Cdd:cd03247 156 HLTGIEHM-DKILFLENGKIIM 176
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-156 |
3.52e-10 |
|
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: 59.79 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARclLARVEQhlpdE--LHQQTLLDALLARLP- 94
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQ----EpwIQNGTIRENILFGKPf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 95 EAERESSAWRAQALLANMGfaeaawSLTAG----------SLSGGQHTRLLLARALIISPDLLLLDEP--------GNHL 156
Cdd:cd03250 93 DEERYEKVIKACALEPDLE------ILPDGdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPlsavdahvGRHI 166
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-181 |
3.70e-10 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 61.61 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAP---AEGVVTRAARCLLarveqHLPD-ELHQ------------- 82
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLL-----KLSEkELRKirgreiqmifqdp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 83 -----------QTLLDALLA--RLPEAERESsawRAQALLANMGFAEAAWSLTA--GSLSGGQHTRLLLARALIISPDLL 147
Cdd:COG0444 96 mtslnpvmtvgDQIAEPLRIhgGLSKAEARE---RAIELLERVGLPDPERRLDRypHELSGGMRQRVMIARALALEPKLL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495164891 148 LLDEPGNHLD---------LptmlwLEQFLARWNGSFILVSHD 181
Cdd:COG0444 173 IADEPTTALDvtiqaqilnL-----LKDLQRELGLAILFITHD 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-157 |
3.83e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.41 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALD-------GTL-----------APAEGVVtRAARCLLARVEQ--HL-PDELH 81
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNllemprsGTLniagnhfdfskTPSDKAI-RELRRNVGMVFQqyNLwPHLTV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 82 QQTLLDALLARLPEAERESSAwRAQALLANMGFAEAA--WSLtagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PRK11124 100 QQNLIEAPCRVLGLSKDQALA-RAEKLLERLRLKPYAdrFPL---HLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-199 |
3.88e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.02 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 2 STLLTAHSLRIDSPFGPE-LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL------LARVEQ 74
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHaLKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrkgLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 75 HL------PD------ELHQQTLLDALLARLPEAERESsawRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALII 142
Cdd:PRK13636 83 SVgmvfqdPDnqlfsaSVYQDVSFGAVNLKLPEDEVRK---RVDNALKRTGIEHLKDKPTH-CLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495164891 143 SPDLLLLDEPGNHLDlPT-----MLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:PRK13636 159 EPKVLVLDEPTAGLD-PMgvseiMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-151 |
4.38e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.48 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------------RAArcLLARVEQ--------HLpd 78
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILidgkdvtklpeykRAK--YIGRVFQdpmmgtapSM-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 79 elhqqTLLDAL-LA-----------RLPEAEREssawRAQALLA--NMGFaEAAWSLTAGSLSGGQHTRLLLARALIISP 144
Cdd:COG1101 98 -----TIEENLaLAyrrgkrrglrrGLTKKRRE----LFRELLAtlGLGL-ENRLDTKVGLLSGGQRQALSLLMATLTKP 167
|
....*..
gi 495164891 145 DLLLLDE 151
Cdd:COG1101 168 KLLLLDE 174
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
321-489 |
5.12e-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: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 321 KSGDRVALLGHNGCGKSSLLRLLWRQWQTGET-----VPGVTFHPRV---SLGYYDQSLHQLPdNATLLEALEpFAPELQ 392
Cdd:cd03213 33 KPGELTAIMGPSGAGKSTLLNALAGRRTGLGVsgevlINGRPLDKRSfrkIIGYVPQDDILHP-TLTVRETLM-FAAKLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 393 QrklalisagfpwarhgqrvdtLSGGERSRLLfVGLSL-ARYSLLMLDEPTNHLD-------MEGKEALAQTLQTfeggL 464
Cdd:cd03213 111 G---------------------LSGGERKRVS-IALELvSNPSLLFLDEPTSGLDsssalqvMSLLRRLADTGRT----I 164
|
170 180
....*....|....*....|....*.
gi 495164891 465 LLVTHD-RTLMEASCNRFWLVEDGGL 489
Cdd:cd03213 165 ICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-157 |
6.05e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.72 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT------RAARcllarveqhlPDELHQQ---------- 83
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidgvdiRDLT----------LESLRRQigvvpqdtfl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 ---TLLDALLARLPEAEREsSAWRAqALLAN-MGFAEAawsLTAG----------SLSGGQHTRLLLARALIISPDLLLL 149
Cdd:COG1132 426 fsgTIRENIRYGRPDATDE-EVEEA-AKAAQaHEFIEA---LPDGydtvvgergvNLSGGQRQRIAIARALLKDPPILIL 500
|
....*...
gi 495164891 150 DEPGNHLD 157
Cdd:COG1132 501 DEATSALD 508
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
18-160 |
6.36e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 62.06 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcLLARVEQH--------LPDE--LHQQTLLD 87
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF-SLKDIDRHtlrqfinyLPQEpyIFSGSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ALLARLPEAERESSAWRAQAL------LANM--GFaEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP 159
Cdd:TIGR01193 567 NLLLGAKENVSQDEIWAACEIaeikddIENMplGY-QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
.
gi 495164891 160 T 160
Cdd:TIGR01193 646 T 646
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-157 |
6.99e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.00 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGvvtraaRCLLARVEQHLPDELHQQTLLDALLARLPEAE 97
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKG------KVLVSGIDTGDFSKLQGIRKLVGIVFQNPETQ 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 98 ------RESSAWRAQAL---------LANMGFAEAAWS----LTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PRK13644 90 fvgrtvEEDLAFGPENLclppieirkRVDRALAEIGLEkyrhRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-152 |
7.02e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.52 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEG-------VVTRAARCLLARVEQHL------------PDELHQQT 84
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGeilfdgqDITGLSGRELRPLRRRMqmvfqdpyaslnPRMTVGDI 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 85 LLDALLA--RLPEAERESsawRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:COG4608 118 IAEPLRIhgLASKAERRE---RVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEP 184
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-157 |
7.76e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.58 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 17 GPELNAL---SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT--------------RAARCLLARVEQH--Lp 77
Cdd:PRK11153 15 GRTIHALnnvSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLvdgqdltalsekelRKARRQIGMIFQHfnL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 78 deLHQQTLLD--AL---LARLPEAERESsawRAQALLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:PRK11153 94 --LSSRTVFDnvALpleLAGTPKAEIKA---RVTELLELVGLSDKADRYPA-QLSGGQKQRVAIARALASNPKVLLCDEA 167
|
....*
gi 495164891 153 GNHLD 157
Cdd:PRK11153 168 TSALD 172
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-200 |
8.53e-10 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 59.16 E-value: 8.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGV----------VTRAA-RCLLARVEQHlpDELHQQTLL 86
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQilidgidirdISRKSlRSMIGVVLQD--TFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 DALLARLPEAERESSAWRAQALLANM-------GFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP 159
Cdd:cd03254 95 ENIRLGRPNATDEEVIEAAKEAGAHDfimklpnGYDTVL-GENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 160 TMLWLEQFLARWNG---SFILVSHDSALLDSvtNRTWILRDGQL 200
Cdd:cd03254 174 TEKLIQEALEKLMKgrtSIIIAHRLSTIKNA--DKILVLDDGKI 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-206 |
9.62e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------------RAARCLlarveQHLPDE---LHQQTLL 86
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplhaRARRGI-----GYLPQEasiFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 DALLARLP---EAERESSAWRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLW 163
Cdd:PRK10895 97 DNLMAVLQirdDLSAEQREDRANELMEEFHIEHLRDSM-GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495164891 164 LEQFLA--RWNGSFILVS-HDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:PRK10895 176 IKRIIEhlRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-180 |
1.05e-09 |
|
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: 58.27 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARClLARVEQHLPDELHQQTLLDALLARLPEAER- 98
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-LDFQRDSIARGLLYLGHAPGIKTTLSVLENl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 99 --------ESSAWRAQALLANMGFAEAAwsltAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLA- 169
Cdd:cd03231 95 rfwhadhsDEQVEEALARVGLNGFEDRP----VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAg 170
|
170
....*....|...
gi 495164891 170 --RWNGSFILVSH 180
Cdd:cd03231 171 hcARGGMVVLTTH 183
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
320-487 |
1.59e-09 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 58.31 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLW--------RQWQTGETVP----GVTFHPRVSlGYydqslhqlpDNATLLEALEPF 387
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAgiyppdsgTVTVRGRVSSllglGGGFNPELT-GR---------ENIYLNGRLLGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 388 APELQQRKLALIsAGFpwARHGQRVD----TLSGGERSRLLFvGLSLA-RYSLLMLDEPTNHLDMEGKEALAQTLQTF-- 460
Cdd:cd03220 115 SRKEIDEKIDEI-IEF--SELGDFIDlpvkTYSSGMKARLAF-AIATAlEPDILLIDEVLAVGDAAFQEKCQRRLRELlk 190
|
170 180
....*....|....*....|....*...
gi 495164891 461 -EGGLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:cd03220 191 qGKTVILVSHDPSSIKRLCDRALVLEKG 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-152 |
1.60e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT---------RAARCLLARVE---QHLPDELHQqTL-- 85
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmadaRHRRAVCPRIAympQGLGKNLYP-TLsv 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 86 ---LDaLLARL---PEAEREssaWRAQALLANMG---FAEAAwsltAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:NF033858 96 fenLD-FFGRLfgqDAAERR---RRIDELLRATGlapFADRP----AGKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-202 |
2.22e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.66 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-----------TRAARCLLARVEQHLPDELHQQTlLDA 88
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitkenIREVRKFVGLVFQNPDDQIFSPT-VEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 LLARLP---EAERESSAWRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD----LPTM 161
Cdd:PRK13652 99 DIAFGPinlGLDEETVAHRVSSALHMLGLEELR-DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELI 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495164891 162 LWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:PRK13652 178 DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-157 |
2.29e-09 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 58.01 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQ--HLPDElhqqT 84
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdytlASLRRQIGLVSQdvFLFND----T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 85 LLDALLARLPEAEREssAWRAQALLAN-MGFAEaawSLTAG----------SLSGGQHTRLLLARALIISPDLLLLDEPG 153
Cdd:cd03251 92 VAENIAYGRPGATRE--EVEEAARAANaHEFIM---ELPEGydtvigergvKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
....
gi 495164891 154 NHLD 157
Cdd:cd03251 167 SALD 170
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-206 |
2.60e-09 |
|
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: 60.41 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 10 LRIDSPFG-PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL---LARVEQHL---PDE--- 79
Cdd:TIGR01257 935 VKIFEPSGrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnLDAVRQSLgmcPQHnil 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 80 LHQQTLLDALL--ARLPEAERESSAWRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:TIGR01257 1015 FHHLTVAEHILfyAQLKGRSWEEAQLEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 158 LPTM--LWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:TIGR01257 1094 PYSRrsIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-200 |
2.78e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.84 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHL-------PDELH--QQTLLDA 88
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALrqaisvvSQRVHlfSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 LLARLPEAEREssawRAQALLANMGFAE--------AAWSLTAG-SLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP 159
Cdd:PRK11160 434 LLLAAPNASDE----ALIEVLQQVGLEKlleddkglNAWLGEGGrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495164891 160 T----MLWLEQFLArwNGSFILVSHDSALLDSVtNRTWILRDGQL 200
Cdd:PRK11160 510 TerqiLELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-204 |
2.97e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.56 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT---------RAArcLLARV-------EQ---HLPdelhqq 83
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfkrRKE--FARRIgvvfgqrSQlwwDLP------ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 tLLDA--LLA---RLPEAEREssawRAQALLANMgfaeaawsLTAGS--------LSGGQHTRLLLARALIISPDLLLLD 150
Cdd:COG4586 113 -AIDSfrLLKaiyRIPDAEYK----KRLDELVEL--------LDLGElldtpvrqLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 151 EP--GnhLDLPTMLWLEQFL----ARWNGSFILVSHDSALLDSVTNRTWILRDGQLqAFD 204
Cdd:COG4586 180 EPtiG--LDVVSKEAIREFLkeynRERGTTILLTSHDMDDIEALCDRVIVIDHGRI-IYD 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
296-492 |
2.99e-09 |
|
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: 57.04 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLLWR--QWQTGE-TVPGVTFhPRVSLGYYDQSLH 372
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRflEAEEGKiEIDGIDI-STIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 373 QLPDNATLLEA-----LEPFA--PELQQRKLALISAGfpwarhGqrvDTLSGGERsRLLFVGLS-LARYSLLMLDEPTNH 444
Cdd:cd03369 86 IIPQDPTLFSGtirsnLDPFDeySDEEIYGALRVSEG------G---LNLSQGQR-QLLCLARAlLKRPRVLVLDEATAS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495164891 445 LDMEGKEALAQTL-QTFEGGLLLVTHDRTLMEASCNRFWLVEDGGLSEW 492
Cdd:cd03369 156 IDYATDALIQKTIrEEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEY 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
19-200 |
3.03e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.18 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 19 ELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLAR-----------VEQHLPDELHQQTLLD 87
Cdd:PRK13642 22 QLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnvwnlrrkigmVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ALLARLPEA--ERESSAWRA-QALLA-NM-GFAeaawSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDlPT-- 160
Cdd:PRK13642 102 DVAFGMENQgiPREEMIKRVdEALLAvNMlDFK----TREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD-PTgr 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495164891 161 ---MLWLEQFLARWNGSFILVSHDsalLDSV--TNRTWILRDGQL 200
Cdd:PRK13642 177 qeiMRVIHEIKEKYQLTVLSITHD---LDEAasSDRILVMKAGEI 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
319-473 |
3.50e-09 |
|
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: 57.11 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLL--WRQWQTGE-TVPGVTFHP----------RVSLGYYDQSLHQLP-----DNATL 380
Cdd:cd03255 26 SIEKGEFVAIVGPSGSGKSTLLNILggLDRPTSGEvRVDGTDISKlsekelaafrRRHIGFVFQSFNLLPdltalENVEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 381 -LEALEPFAPELQQRKLALI-SAGFPwARHGQRVDTLSGGERSRllfvgLSLARY-----SLLMLDEPTNHLDMEGKEAL 453
Cdd:cd03255 106 pLLLAGVPKKERRERAEELLeRVGLG-DRLNHYPSELSGGQQQR-----VAIARAlandpKIILADEPTGNLDSETGKEV 179
|
170 180
....*....|....*....|....
gi 495164891 454 AQTLQTF--EGG--LLLVTHDRTL 473
Cdd:cd03255 180 MELLRELnkEAGttIVVVTHDPEL 203
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
298-564 |
3.74e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.94 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 298 LENLAVSAAPdtptlftlplarlksGDRVALLGHNGCGKSSLLRLLWRQWQT-GE-TVPGVTFHpRVSLGYYDQSLHQLP 375
Cdd:cd03289 20 LENISFSISP---------------GQRVGLLGRTGSGKSTLLSAFLRLLNTeGDiQIDGVSWN-SVPLQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 376 D-----NATLLEALEPFA----PEL----QQRKLALISAGFPWARHGQRVD---TLSGGERSRLLFVGLSLARYSLLMLD 439
Cdd:cd03289 84 QkvfifSGTFRKNLDPYGkwsdEEIwkvaEEVGLKSVIEQFPGQLDFVLVDggcVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 440 EPTNHLDMEGKEALAQTL-QTFEGGLLLVTHDRTLMEASCNRFWLVEDGGLSEWHNMEALLAR---LRAAPTqeaeneap 515
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLkQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEkshFKQAIS-------- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 495164891 516 aalaappdeHSDahlleRLIELEMRLNADLERKPRHQKPALQAEWRKEI 564
Cdd:cd03289 236 ---------PSD-----RLKLFPRRNSSKSKRKPRPQIQALQEETEEEV 270
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
220-473 |
3.83e-09 |
|
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: 59.38 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 220 SDAL-RHKAEQKEIDRVTASAKRLATWGQVYDNEDLARKAKQMEKQvarlKEEQTELAQGSRwRLTLSGDALAADRLLEL 298
Cdd:TIGR00954 380 ADALgRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEE----IESGREGGRNSN-LVPGRGIVEYQDNGIKF 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 299 ENLAVsAAPDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLLWRQWQTGE---TVP--GVTFH----PRVSL----- 364
Cdd:TIGR00954 455 ENIPL-VTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGgrlTKPakGKLFYvpqrPYMTLgtlrd 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 365 --------------GYYDQSLHQLPDNATLLEALEpfapelqqRKLALiSAGFPWArhgqrvDTLSGGERSRLLFVGLSL 430
Cdd:TIGR00954 534 qiiypdssedmkrrGLSDKDLEQILDNVQLTHILE--------REGGW-SAVQDWM------DVLSGGEKQRIAMARLFY 598
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 495164891 431 ARYSLLMLDEPTN--HLDMEGKeaLAQTLQTFEGGLLLVTHDRTL 473
Cdd:TIGR00954 599 HKPQFAILDECTSavSVDVEGY--MYRLCREFGITLFSVSHRKSL 641
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
296-472 |
3.89e-09 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 56.76 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAApDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLL--------WRQWQTGETVPGVTFHPR-VSLGY 366
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSL-TVEPGEFLALLGPSGCGKTTLLRLIaglerpdsGEILIDGRDVTGVPPERRnIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 367 YDQSL--HQ-LPDN-ATLLEALEPFAPELQQRKLALIsAGFPWARHGQR-VDTLSGGERSRLlfvglSLARY-----SLL 436
Cdd:cd03259 79 QDYALfpHLtVAENiAFGLKLRGVPKAEIRARVRELL-ELVGLEGLLNRyPHELSGGQQQRV-----ALARAlarepSLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495164891 437 MLDEPTNHLDMEGKEALAQTLQTF--EGGL--LLVTHDRT 472
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELqrELGIttIYVTHDQE 192
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
105-200 |
5.53e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 105 AQALLANMGFAEAAWSLTAGS---LSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNG--SFILVS 179
Cdd:PRK14271 140 AQARLTEVGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVT 219
|
90 100
....*....|....*....|.
gi 495164891 180 HDSALLDSVTNRTWILRDGQL 200
Cdd:PRK14271 220 HNLAQAARISDRAALFFDGRL 240
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-202 |
6.96e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.08 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDELHQQTLL---DALLARLPEAE-- 97
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLfqsGALFTDMNVFDnv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 98 ----RESSAWRAQAL-------LANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQ 166
Cdd:PRK11831 106 ayplREHTQLPAPLLhstvmmkLEAVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495164891 167 FLARWNGSF----ILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:PRK11831 185 LISELNSALgvtcVVVSHDVPEVLSIADHAYIVADKKIVA 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
296-489 |
9.45e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.56 E-value: 9.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAApDTPTLFTLPLArLKSGDRVALLGHNGCGKSSLLRLLWRQW--QTGEtvpgvtfhprvsLGYYDQSLHQ 373
Cdd:PRK11231 3 LRTENLTVGYG-TKRILNDLSLS-LPTGKITALIGPNGCGKSTLLKCFARLLtpQSGT------------VFLGDKPISM 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 374 LPDN--ATLLEAL--EPFAPE-LQQRKLalISAGFP-----WARHGQ---------------------RVDTLSGGERSR 422
Cdd:PRK11231 69 LSSRqlARRLALLpqHHLTPEgITVREL--VAYGRSpwlslWGRLSAednarvnqameqtrinhladrRLTDLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164891 423 LlFVGLSLARYS-LLMLDEPTNHLDMEGKE---ALAQTLQTFEGGLLLVTHDrtLMEAS--CNRFWLVEDGGL 489
Cdd:PRK11231 147 A-FLAMVLAQDTpVVLLDEPTTYLDINHQVelmRLMRELNTQGKTVVTVLHD--LNQASryCDHLVVLANGHV 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-180 |
1.14e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.59 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 14 SPFGPE-LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------------RAARCLLARVEQHLPDE 79
Cdd:PRK13637 16 TPFEKKaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvditdkkvklSDIRKKVGLVFQYPEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 80 LHQQTLLDAL---LARLPEAERESSAwRAQALLANMGFA-EAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNH 155
Cdd:PRK13637 96 LFEETIEKDIafgPINLGLSEEEIEN-RVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190
....*....|....*....|....*....|
gi 495164891 156 LDlPT----MLWLEQFL-ARWNGSFILVSH 180
Cdd:PRK13637 175 LD-PKgrdeILNKIKELhKEYNMTIILVSH 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-157 |
1.26e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.25 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV------------TRAARCLLARVEQHlPDELHQQTLLD 87
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenLWDIRNKAGMVFQN-PDNQIVATIVE 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 88 ALLARLPE---AERESSAWRAQALLANMGFAE---AAWSLtagsLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PRK13633 105 EDVAFGPEnlgIPPEEIRERVDESLKKVGMYEyrrHAPHL----LSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-200 |
1.34e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-----------TRAArcLLARV-----EQHLPDELhqq 83
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIlidgqemrfasTTAA--LAAGVaiiyqELHLVPEM--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLDAL-LARLPEA----ERESSAWRAQALLANMGFaEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL 158
Cdd:PRK11288 95 TVAENLyLGQLPHKggivNRRLLNYEAREQLEHLGV-DIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495164891 159 PTmlwLEQFLA-----RWNGSFIL-VSHDS----ALLDSVTnrtwILRDGQL 200
Cdd:PRK11288 174 RE---IEQLFRvirelRAEGRVILyVSHRMeeifALCDAIT----VFKDGRY 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
320-476 |
1.41e-08 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 55.56 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRL---LWRQWQ-----TGETVPGvtfhPRVSLGYYDQSLHQLP-----DNATL-LEALE 385
Cdd:cd03293 27 VEEGEFVALVGPSGCGKSTLLRIiagLERPTSgevlvDGEPVTG----PGPDRGYVFQQDALLPwltvlDNVALgLELQG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 386 PFAPELQQRKLALIS----AGFPWARHGQrvdtLSGGERSRllfvgLSLARY-----SLLMLDEPTNHLDMEGKEALAQT 456
Cdd:cd03293 103 VPKAEARERAEELLElvglSGFENAYPHQ----LSGGMRQR-----VALARAlavdpDVLLLDEPFSALDALTREQLQEE 173
|
170 180
....*....|....*....|....
gi 495164891 457 L----QTFEGGLLLVTHDrtLMEA 476
Cdd:cd03293 174 LldiwRETGKTVLLVTHD--IDEA 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-157 |
1.45e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 55.57 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 15 PFGPE-LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV--------TRAARCLLARVEQHLPDE-LHQQT 84
Cdd:cd03252 12 PDGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaLADPAWLRRQVGVVLQENvLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 85 LLD--ALLARLPEAERESSAWR---AQALLANM--GFAEAAWSLTAGsLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:cd03252 92 IRDniALADPGMSMERVIEAAKlagAHDFISELpeGYDTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-200 |
1.74e-08 |
|
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: 54.87 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLP-DELHQQTLLDALLA----------- 91
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPvSMLFQENNLFAHLTvrqniglglhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 92 --RLPEAEREssawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD---LPTMLWL-E 165
Cdd:TIGR01277 98 glKLNAEQQE----KVVDAAQQVGIADYLDRL-PEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllREEMLALvK 172
|
170 180 190
....*....|....*....|....*....|....*
gi 495164891 166 QFLARWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-180 |
1.78e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 4 LLTAHSLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-------TRAARCLLARVEQHL 76
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDRSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 77 P------DELHQQTLLDALLARLPEaERESSAwraqalLANMGFAEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLD 150
Cdd:PRK13543 91 PglkadlSTLENLHFLCGLHGRRAK-QMPGSA------LAIVGLAGYEDTLVR-QLSAGQKKRLALARLWLSPAPLWLLD 162
|
170 180 190
....*....|....*....|....*....|...
gi 495164891 151 EPGNHLDLPTMLWLEQFLA---RWNGSFILVSH 180
Cdd:PRK13543 163 EPYANLDLEGITLVNRMISahlRGGGAALVTTH 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-198 |
1.85e-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: 54.84 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDG--TLAPAEGVVT-------------RAARCL-LARveQHlPDELHQQ 83
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILfkgeditdlppeeRARLGIfLAF--QY-PPEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLDALlarlpeaeREssawraqallANMGFaeaawsltagslSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLW 163
Cdd:cd03217 93 KNADFL--------RY----------VNEGF------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 495164891 164 LEQFLARW---NGSFILVSHDSALLDSV-TNRTWILRDG 198
Cdd:cd03217 143 VAEVINKLreeGKSVLIITHYQRLLDYIkPDRVHVLYDG 181
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
295-480 |
1.91e-08 |
|
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: 55.20 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 295 LLELENLAVSAAPDTPTLFTLP---LaRLKSGDRVALLGHNGCGKSSLLRLLWR--QWQTGEtvpgVTFHPRVSLGYYD- 368
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDdvsF-SIKKGETLGLVGESGSGKSTLARAILGllKPTSGS----IIFDGKDLLKLSRr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 369 ---------QSLHQLPDNA---------TLLEALE----PFAPELQQRKLALISAGFPWARH--GQRVDTLSGGERSRLL 424
Cdd:cd03257 76 lrkirrkeiQMVFQDPMSSlnprmtigeQIAEPLRihgkLSKKEARKEAVLLLLVGVGLPEEvlNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495164891 425 FVgLSLA-RYSLLMLDEPTNHLDMEGKEALAQTLQT----FEGGLLLVTHDRTLMEASCNR 480
Cdd:cd03257 156 IA-RALAlNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIADR 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
320-487 |
2.39e-08 |
|
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: 54.59 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLWRQWQ--TGETV---PGVTFHPRVSLGY------------------YDQSLHQLPD 376
Cdd:cd03269 23 VEKGEIFGLLGPNGAGKTTTIRMILGIILpdSGEVLfdgKPLDIAARNRIGYlpeerglypkmkvidqlvYLAQLKGLKK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 377 N---ATLLEALEPFapELQQRKLalisagfpwarhgQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEAL 453
Cdd:cd03269 103 EearRRIDEWLERL--ELSEYAN-------------KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 495164891 454 AQTLQTFEGG---LLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:cd03269 168 KDVIRELARAgktVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-157 |
2.45e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 54.42 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT---------RAARCLLARVEQ------HLPDELHQQTLLD 87
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLingvdvtaaPPADRPVSMLFQennlfaHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ALLaRLPEAEREssawRAQALLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:cd03298 97 PGL-KLTAEDRQ----AIEVALARVGLAGLEKRL-PGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-191 |
3.19e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 19 ELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARC-----------------LLARVEQHLPDELH 81
Cdd:PRK13409 354 SLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKIsykpqyikpdydgtvedLLRSITDDLGSSYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 82 QQTLLDAL-LARLPEAEressawraqallanmgfaeaawsltAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDlpt 160
Cdd:PRK13409 434 KSEIIKPLqLERLLDKN-------------------------VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--- 485
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495164891 161 mlwLEQFL---------ARWNGSFILV-SHDSALLDSVTNR 191
Cdd:PRK13409 486 ---VEQRLavakairriAEEREATALVvDHDIYMIDYISDR 523
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
319-489 |
3.21e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.70 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP--G-VTFHPRVSlgyydqslhqlpdnaTLLEALEPFAPELQQRK 395
Cdd:COG1134 48 EVERGESVGIIGRNGAGKSTLLKLI-----AGILEPtsGrVEVNGRVS---------------ALLELGAGFHPELTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 396 LALISA---GFPWARHGQRVD-----------------TLSGGERSRLLFvGLSLA-RYSLLMLDeptnhldmegkEALA 454
Cdd:COG1134 108 NIYLNGrllGLSRKEIDEKFDeivefaelgdfidqpvkTYSSGMRARLAF-AVATAvDPDILLVD-----------EVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495164891 455 -----------QTLQTF--EGG-LLLVTHDRTLMEASCNR-FWLvEDGGL 489
Cdd:COG1134 176 vgdaafqkkclARIRELreSGRtVIFVSHSMGAVRRLCDRaIWL-EKGRL 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-157 |
3.43e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLArveqhLPDELHQQ--------------TL 85
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST-----LKPEIYRQqvsycaqtptlfgdTV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495164891 86 LDALLarLPEAERESSAWRA--QALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PRK10247 98 YDNLI--FPWQIRNQQPDPAifLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
295-476 |
3.59e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 295 LLELENLAVSAApDTPTLFTLPLArLKSGDRVALLGHNGCGKSSLLRLLWRQWQTGETVpgVTFHPRVSLGYYDQSLH-- 372
Cdd:PRK09544 4 LVSLENVSVSFG-QRRVLSDVSLE-LKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV--IKRNGKLRIGYVPQKLYld 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 373 -QLPDNATLLEALEP------FAPELQQRKLALIsagfpwarHGQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHL 445
Cdd:PRK09544 80 tTLPLTVNRFLRLRPgtkkedILPALKRVQAGHL--------IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190
....*....|....*....|....*....|....*
gi 495164891 446 DMEGKEAL----AQTLQTFEGGLLLVTHDRTLMEA 476
Cdd:PRK09544 152 DVNGQVALydliDQLRRELDCAVLMVSHDLHLVMA 186
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-157 |
3.60e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.24 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEG------VVTRAARCLLARVEQHLPDELHQQTLLDALLA-- 91
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdIYIGDKKNNHELITNPYSKKIKNFKELRRRVSmv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 92 -RLPEAE--------------------RESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLD 150
Cdd:PRK13631 122 fQFPEYQlfkdtiekdimfgpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFD 201
|
....*..
gi 495164891 151 EPGNHLD 157
Cdd:PRK13631 202 EPTAGLD 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-180 |
4.17e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 56.27 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcllaRVEQHLPDELHQQTLLDAL-------- 89
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV----PLVQYDHHYLHRQVALVGQepvlfsgs 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 --------LARLPEAERESSAWRAQALLANMGFAEAAWSL---TAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL 158
Cdd:TIGR00958 571 vreniaygLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgeKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180
....*....|....*....|..
gi 495164891 159 PTMLWLEQFLARWNGSFILVSH 180
Cdd:TIGR00958 651 ECEQLLQESRSRASRTVLLIAH 672
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-152 |
4.23e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcllarveqhlpDELHQQT--LLDALLARLPEAE 97
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK-----------DITDWQTakIMREAVAIVPEGR 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495164891 98 RESSAWRAQALLANMGF----------AEAAWSL----------TAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:PRK11614 90 RVFSRMTVEENLAMGGFfaerdqfqerIKWVYELfprlherriqRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-169 |
4.72e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.04 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTL--------------APAEGVVTRAArcLLARVEQHLPDELHQQTL 85
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgnnftgtilannrKPTKQILKRTG--FVTQDDILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LDALLARLPEA-ERESSAWRAQALLANMGFAEAAWSLTAGS----LSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT 160
Cdd:PLN03211 162 VFCSLLRLPKSlTKQEKILVAESVISELGLTKCENTIIGNSfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
....*....
gi 495164891 161 MLWLEQFLA 169
Cdd:PLN03211 242 AYRLVLTLG 250
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
320-458 |
5.09e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.25 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLwRQWQTGETVPGVTFH------------------PRVSLGYYDQSLHqLPDNATLL 381
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHL-SGLITGDKSAGSHIEllgrtvqregrlardirkSRANTGYIFQQFN-LVNRLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 382 E---------------ALEPFAPELQQRKL-ALISAGFPWARHgQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHL 445
Cdd:PRK09984 105 EnvligalgstpfwrtCFSWFTREQKQRALqALTRVGMVHFAH-QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASL 183
|
170
....*....|...
gi 495164891 446 DMEGKEALAQTLQ 458
Cdd:PRK09984 184 DPESARIVMDTLR 196
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
319-487 |
5.45e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLWRQWQTGETVPGVTFHPRVSLGyyDQSLHQLPdnATLLEALEPFAPELQQRKLA- 397
Cdd:PRK13547 23 RIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRGARVTGDVTLN--GEPLAAID--APRLARLRAVLPQAAQPAFAf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 398 ----LISAG-FPWARH-------------------------GQRVDTLSGGERSRLLFV-----------GLSLARYslL 436
Cdd:PRK13547 99 sareIVLLGrYPHARRagalthrdgeiawqalalagatalvGRDVTTLSGGELARVQFArvlaqlwpphdAAQPPRY--L 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495164891 437 MLDEPTNHLDMEGKEALAQTLQT----FEGGLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:PRK13547 177 LLDEPTAALDLAHQHRLLDTVRRlardWNLGVLAIVHDPNLAARHADRIAMLADG 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-200 |
5.55e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAAR---CLLARVEQHLPDELH------------QQTLLD 87
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQfifqdpyasldpRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ALLARL-------PEAERESSAWraqaLLANMGF-AEAAWSLTAgSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP 159
Cdd:PRK10261 423 SIMEPLrvhgllpGKAAAARVAW----LLERVGLlPEHAWRYPH-EFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495164891 160 T---MLWLEQFLARWNG-SFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:PRK10261 498 IrgqIINLLLDLQRDFGiAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
296-442 |
5.76e-08 |
|
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: 53.59 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVsAAPDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRL---LWRQWQ-----TGETVPGVTFHPRVSLG-- 365
Cdd:cd03224 1 LEVENLNA-GYGKSQILFGVSL-TVPEGEIVALLGRNGAGKTTLLKTimgLLPPRSgsirfDGRDITGLPPHERARAGig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 366 YYDQSlHQLPDNATLLEALE----PFAPELQQRKLALISAGFP--WARHGQRVDTLSGGERsRLLFVGLSL-ARYSLLML 438
Cdd:cd03224 79 YVPEG-RRIFPELTVEENLLlgayARRRAKRKARLERVYELFPrlKERRKQLAGTLSGGEQ-QMLAIARALmSRPKLLLL 156
|
....
gi 495164891 439 DEPT 442
Cdd:cd03224 157 DEPS 160
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
296-487 |
5.95e-08 |
|
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: 53.57 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLWRQWQ--TGET-VPGV---------TFHPRVS 363
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINI-SISAGEFVFLVGPSGAGKSTLLKLIYKEELptSGTIrVNGQdvsdlrgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 364 LGYYDQSLHQLPDN------ATLLEALEPFAPELQQR-KLALISAGFPwARHGQRVDTLSGGERSRLlfvglSLARY--- 433
Cdd:cd03292 80 IGVVFQDFRLLPDRnvyenvAFALEVTGVPPREIRKRvPAALELVGLS-HKHRALPAELSGGEQQRV-----AIARAivn 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 434 --SLLMLDEPTNHLDMEGKEALAQTLQTFE--GGLLLV-THDRTLMEASCNRFWLVEDG 487
Cdd:cd03292 154 spTILIADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVaTHAKELVDTTRHRVIALERG 212
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-187 |
6.35e-08 |
|
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: 51.99 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 29 KGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAArcllarveqhlPDELHQQTLLDALLARLPEaeressawraqal 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-----------GEDILEEVLDQLLLIIVGG------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 109 lanmgfaeaawslTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD---------LPTMLWLEQFLARWNGSFILVS 179
Cdd:smart00382 57 -------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTT 123
|
....*...
gi 495164891 180 HDSALLDS 187
Cdd:smart00382 124 NDEKDLGP 131
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-204 |
6.44e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.01 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALD--GTLAPaEGVVTRAA-----------------RCLLARVEQH---LP 77
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNP-EVTITGSIvynghniysprtdtvdlRKEIGMVFQQpnpFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 78 DELHQQTLLDALLARLPEAERESSAWRAQALLANMgFAEAAWSL--TAGSLSGGQHTRLLLARALIISPDLLLLDEPGNH 155
Cdd:PRK14239 100 MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASI-WDEVKDRLhdSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 156 LDLPTMLWLEQFL--ARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFD 204
Cdd:PRK14239 179 LDPISAGKIEETLlgLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
321-489 |
6.63e-08 |
|
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: 53.37 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 321 KSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVPG---VTFhprvsLGYYDQSLHQLPDN-ATLLEALEpFAPELQQRKL 396
Cdd:cd03268 24 KKGEIYGFLGPNGAGKTTTMKII-----LGLIKPDsgeITF-----DGKSYQKNIEALRRiGALIEAPG-FYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 397 ALISA---GFPWARH-------------GQRVDTLSGGERSRLlfvGLSLA---RYSLLMLDEPTNHLDMEG-KE--ALA 454
Cdd:cd03268 93 LRLLArllGIRKKRIdevldvvglkdsaKKKVKGFSLGMKQRL---GIALAllgNPDLLILDEPTNGLDPDGiKElrELI 169
|
170 180 190
....*....|....*....|....*....|....*
gi 495164891 455 QTLQTFEGGLLLVTHDRTLMEASCNRFWLVEDGGL 489
Cdd:cd03268 170 LSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-199 |
7.56e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.22 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPA--EGVVTRAARCLLArveQHLPDE-------LHQQTlldALL 90
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKA---SNIRDTeragiviIHQEL---TLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 91 ARLPEAER----------------ESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGN 154
Cdd:TIGR02633 91 PELSVAENiflgneitlpggrmayNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495164891 155 HL---DLPTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:TIGR02633 171 SLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-200 |
7.71e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 53.76 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 35 LIGHNGCGKSTLLKALDGTL-----APAEGVVTRAARC--------LLARVEQ--HLPD-----ELHQQTLLDALLARLP 94
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDifkmdvieLRRRVQMvfQIPNpipnlSIFENVALGLKLNRLV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 95 EAERESSAWRAQALLANMGFAEAAWSLTA--GSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFL--AR 170
Cdd:PRK14247 114 KSKKELQERVRWALEKAQLWDEVKDRLDApaGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFleLK 193
|
170 180 190
....*....|....*....|....*....|
gi 495164891 171 WNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:PRK14247 194 KDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
24-206 |
8.08e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.65 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV---------------TRAARCLLARVEQHLPDELHQqTLLDA 88
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakisdaelREVRRKKIAMVFQSFALMPHM-TVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 L-----LARLPEAERESSAWRAqalLANMGFAEAAWSLtAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD--LPTM 161
Cdd:PRK10070 127 TafgmeLAGINAEERREKALDA---LRQVGLENYAHSY-PDELSGGMRQRVGLARALAINPDILLMDEAFSALDplIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495164891 162 LW--LEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAFDLP 206
Cdd:PRK10070 203 MQdeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-217 |
8.32e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 22 ALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV-------------TRAARCLLARVEQHLPDELHQQTLLDA 88
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaskEVARRIGLLAQNATTPGDITVQELVAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 llARLPEA------ERESSAWRAQALLANmGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTML 162
Cdd:PRK10253 105 --GRYPHQplftrwRKEDEEAVTKAMQAT-GITHLA-DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 163 WLEQFLARWNG----SFILVSHDSALLDSVTNRTWILRDGQLQAFDLPCTQARAALAAR 217
Cdd:PRK10253 181 DLLELLSELNRekgyTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIER 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
23-158 |
8.46e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------------RAARCLL------------ARVEQHLP 77
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplhfgdysyRSQRIRMifqdpstslnprQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 78 DELHQQTLLDAllarlpeAERESsawRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PRK15112 112 FPLRLNTDLEP-------EQREK---QIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
.
gi 495164891 158 L 158
Cdd:PRK15112 182 M 182
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
283-488 |
8.98e-08 |
|
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: 53.66 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 283 LTLSGDALAADRLLELENLAVSAAPdtptlftlplarlksGDRVALLGHNGCGKSSLLRLLwrqwqTGETVPGvtfHPRV 362
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPP---------------GSLTGLLGPNGSGKSTLLRLL-----AGALRPD---AGTV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 363 SLGYYDqsLHQLPDNA-----TLLEALEPFAPELQQRKLALIS--------AGFPWARHG----------------QRVD 413
Cdd:TIGR03873 59 DLAGVD--LHGLSRRArarrvALVEQDSDTAVPLTVRDVVALGriphrslwAGDSPHDAAvvdralartelshladRDMS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 414 TLSGGERSRLlFVGLSLA-RYSLLMLDEPTNHLDMEGKEALAQTLQTFEGG---LLLVTHDRTLMEASCNRFwLVEDGG 488
Cdd:TIGR03873 137 TLSGGERQRV-HVARALAqEPKLLLLDEPTNHLDVRAQLETLALVRELAATgvtVVAALHDLNLAASYCDHV-VVLDGG 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
124-204 |
9.03e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.50 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 124 GSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP----TMLWLEQFLARWNGSFILVSHDsalLDSV---TNRTWILR 196
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPrkreLLPYLERLAREINIPILYVSHS---LDEIlrlADRVVVLE 203
|
....*...
gi 495164891 197 DGQLQAFD 204
Cdd:PRK11144 204 QGKVKAFG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
13-157 |
9.33e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.60 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 13 DSPFgpELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL----LARVEQHL------PDE--- 79
Cdd:PRK13648 20 DASF--TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLRKHIgivfqnPDNqfv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 80 -----------LHQQTL-LDALLARLPEAeressawraqalLANMGFAEAAWSlTAGSLSGGQHTRLLLARALIISPDLL 147
Cdd:PRK13648 98 gsivkydvafgLENHAVpYDEMHRRVSEA------------LKQVDMLERADY-EPNALSGGQKQRVAIAGVLALNPSVI 164
|
170
....*....|
gi 495164891 148 LLDEPGNHLD 157
Cdd:PRK13648 165 ILDEATSMLD 174
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-195 |
9.50e-08 |
|
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: 53.00 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 15 PFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQHLPdeLHQQ 83
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRRAIGVVPQDTV--LFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLDALLARLPEA---ERESSAWRAQALLANMGFAEaAWSLTAGS----LSGGQHTRLLLARALIISPDLLLLDEPGNHL 156
Cdd:cd03253 90 TIGYNIRYGRPDAtdeEVIEAAKAAQIHDKIMRFPD-GYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 495164891 157 DLPTmlwlEQFLARwngsfilvshdsALLDSVTNRTWIL 195
Cdd:cd03253 169 DTHT----EREIQA------------ALRDVSKGRTTIV 191
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-160 |
1.03e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 52.80 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 9 SLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQhlp 77
Cdd:cd03369 13 SVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidistiplEDLRSSLTIIPQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 78 delhQQTLLDALLARLPEAERESSAWRAQALLanmgfaeaawSLTAG--SLSGGQHTRLLLARALIISPDLLLLDEPGNH 155
Cdd:cd03369 90 ----DPTLFSGTIRSNLDPFDEYSDEEIYGAL----------RVSEGglNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
....*
gi 495164891 156 LDLPT 160
Cdd:cd03369 156 IDYAT 160
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
320-499 |
1.03e-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: 55.30 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLWRQWQT-GE-TVPGVTFHpRVSLGYYDQSLHQLPD-----NATLLEALEPFA---- 388
Cdd:TIGR01271 1242 VEGGQRVGLLGRTGSGKSTLLSALLRLLSTeGEiQIDGVSWN-SVTLQTWRKAFGVIPQkvfifSGTFRKNLDPYEqwsd 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 389 PEL----QQRKLALISAGFPWARHGQRVD---TLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTL-QTF 460
Cdd:TIGR01271 1321 EEIwkvaEEVGLKSVIEQFPDKLDFVLVDggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLkQSF 1400
|
170 180 190
....*....|....*....|....*....|....*....
gi 495164891 461 EGGLLLVTHDRTLMEASCNRFWLVEDGGLSEWHNMEALL 499
Cdd:TIGR01271 1401 SNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-191 |
1.15e-07 |
|
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: 51.80 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 27 LKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarcllarveqhlpdelhqqtlldallarlpEAERESSAWRAQ 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND---------------------------------EWDGITPVYKPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 107 ALlanmgfaeaawsltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTML----WLEQFLARWNGSFILVSHDS 182
Cdd:cd03222 69 YI----------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLnaarAIRRLSEEGKKTALVVEHDL 132
|
....*....
gi 495164891 183 ALLDSVTNR 191
Cdd:cd03222 133 AVLDYLSDR 141
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-189 |
1.18e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.35 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDELHQQTLLD---------------- 87
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDwsfpvlvedvvmmgry 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 88 ---ALLARLPEAEREssawRAQALLANMGFAEAAWSlTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWL 164
Cdd:PRK15056 107 ghmGWLRRAKKRDRQ----IVTAALARVDMVEFRHR-QIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180
....*....|....*....|....*...
gi 495164891 165 EQFLA--RWNGSFILVS-HDsalLDSVT 189
Cdd:PRK15056 182 ISLLRelRDEGKTMLVStHN---LGSVT 206
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
304-469 |
1.25e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 52.72 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 304 SAAPDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLWRQWQT-------------GETVPGVTFHPRVSLGYYDQS 370
Cdd:cd03290 9 SWGSGLATLSNINI-RIPTGQLTMIVGQVGCGKSSLLLAILGEMQTlegkvhwsnknesEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 371 LHQLpdNATLLEALEPFAPELQQRKLALISAG--------FPWARH---GQRVDTLSGGERSRLLFVGLSLARYSLLMLD 439
Cdd:cd03290 88 PWLL--NATVEENITFGSPFNKQRYKAVTDACslqpdidlLPFGDQteiGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190
....*....|....*....|....*....|....*
gi 495164891 440 EPTNHLDMEGKEALAQT-----LQTFEGGLLLVTH 469
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgilkfLQDDKRTLVLVTH 200
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
320-487 |
1.30e-07 |
|
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: 51.80 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLWR-QWQT-------GETVPGVTFH---PRVSLGYYDQSlHQLPDNATLLEALepfa 388
Cdd:cd03229 23 IEAGEIVALLGPSGSGKSTLLRCIAGlEEPDsgsilidGEDLTDLEDElppLRRRIGMVFQD-FALFPHLTVLENI---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 389 pelqqrklalisaGFPwarhgqrvdtLSGGERSRLlfvglSLARY-----SLLMLDEPTNHLDMEGK---EALAQTLQTF 460
Cdd:cd03229 98 -------------ALG----------LSGGQQQRV-----ALARAlamdpDVLLLDEPTSALDPITRrevRALLKSLQAQ 149
|
170 180
....*....|....*....|....*...
gi 495164891 461 EG-GLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:cd03229 150 LGiTVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-200 |
1.31e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.92 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 35 LIGHNGCGKSTLLKALDGTL-----APAEGVVTRAARCLLA------RVEQHL------PDELHQQTLLDAL-----LAR 92
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSpdvdpiEVRREVgmvfqyPNPFPHLTIYDNVaigvkLNG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 93 LPEAERESSAWRAQALLANMGFAEAAWSLT--AGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLAR 170
Cdd:PRK14267 115 LVKSKKELDERVEWALKKAALWDEVKDRLNdyPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFE 194
|
170 180 190
....*....|....*....|....*....|..
gi 495164891 171 WNGSF--ILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:PRK14267 195 LKKEYtiVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
320-473 |
1.49e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.51 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLL--WRQWQTGETV-PGVTFHPRVS----------LGYYDQSLHQLPDNATLLEALEP 386
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLggLDTPTSGDVIfNGQPMSKLSSaakaelrnqkLGFIYQFHHLLPDFTALENVAMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 387 F------APELQQRKLALISAGFPWARHGQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQTF 460
Cdd:PRK11629 112 LligkkkPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL 191
|
170
....*....|....*..
gi 495164891 461 E----GGLLLVTHDRTL 473
Cdd:PRK11629 192 NrlqgTAFLVVTHDLQL 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
296-469 |
1.75e-07 |
|
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: 51.98 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAapDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLL--WRQWQTGETVPGVTFHPRVSLGYYDQSL-- 371
Cdd:TIGR01189 1 LAARNLACSR--GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILagLLRPDSGEVRWNGTPLAEQRDEPHENILyl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 372 -HQ--LPDNATLLEALEPFAPELQQRKL----ALISAGFPWARHgQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNH 444
Cdd:TIGR01189 79 gHLpgLKPELSALENLHFWAAIHGGAQRtiedALAAVGLTGFED-LPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*...
gi 495164891 445 LDMEGKEALAQTLQTF---EGGLLLVTH 469
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
123-152 |
1.89e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 52.35 E-value: 1.89e-07
10 20 30
....*....|....*....|....*....|
gi 495164891 123 AGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEP 181
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
319-487 |
1.98e-07 |
|
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: 51.99 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLW--------RQWQTGETVPGVTFHPRVSLGYYDQSLhQLPDNATLLEALEPFA-- 388
Cdd:cd03265 22 RVRRGEIFGLLGPNGAGKTTTIKMLTtllkptsgRATVAGHDVVREPREVRRRIGIVFQDL-SVDDELTGWENLYIHArl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 389 -----PELQQRKLALISAGFPWARHGQRVDTLSGGERSRLLfVGLSLA-RYSLLMLDEPTNHLDMEGK----EALAQTLQ 458
Cdd:cd03265 101 ygvpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLE-IARSLVhRPEVLFLDEPTIGLDPQTRahvwEYIEKLKE 179
|
170 180
....*....|....*....|....*....
gi 495164891 459 TFEGGLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:cd03265 180 EFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
261-470 |
2.21e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 261 MEKQVARLKEEQTELAQGSRwrlTLSgdalaadrllelENLAVSAaPDtptlftlplarlksGDRVALLGHNGCGKSSLL 340
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKY---TVA------------ENLTVEI-PD--------------GHFTAIIGPNGCGKSTLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 341 RLLWRQ--------WQTGE---------------------TVPG-VTFHPRVSLGYYDqslHQLPDNATLLEALEPFAPE 390
Cdd:PRK10253 51 RTLSRLmtpahghvWLDGEhiqhyaskevarrigllaqnaTTPGdITVQELVARGRYP---HQPLFTRWRKEDEEAVTKA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 391 LQQRKLALISagfpwarhGQRVDTLSGGERSRlLFVGLSLAR-YSLLMLDEPTNHLDMEGKEALAQTLQTF--EGGLLL- 466
Cdd:PRK10253 128 MQATGITHLA--------DQSVDTLSGGQRQR-AWIAMVLAQeTAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLa 198
|
....*
gi 495164891 467 -VTHD 470
Cdd:PRK10253 199 aVLHD 203
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-205 |
2.97e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.96 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDgTLAPAEGVVtraarcllaRVEQHLpdELHQQTLLDAL--LARL---- 93
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEV---------RVEGRV--EFFNQNIYERRvnLNRLrrqv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 94 ----------PEAERESSA-------WRAQALLAnmGFAEAA------WS-------LTAGSLSGGQHTRLLLARALIIS 143
Cdd:PRK14258 91 smvhpkpnlfPMSVYDNVAygvkivgWRPKLEID--DIVESAlkdadlWDeikhkihKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495164891 144 PDLLLLDEPGNHLDLPTMLWLEQFLA----RWNGSFILVSHDSALLDSVTNRTWIL-----RDGQLQAFDL 205
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQslrlRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGL 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
123-200 |
3.24e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.97 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 123 AGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNG--SFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:PRK14246 151 ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
296-469 |
3.35e-07 |
|
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: 50.99 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAApDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGetvpgvtfHP--RVSLG---YYDQS 370
Cdd:cd03217 1 LEIKDLHVSVG-GKEILKGVNL-TIKKGEVHALMGPNGSGKSTLAKTI-----MG--------HPkyEVTEGeilFKGED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 371 LHQLPdnatllealepfaPELQQRKLALISAGFPWARHGQRV--------DTLSGGERSRLLFVGLSLARYSLLMLDEPT 442
Cdd:cd03217 66 ITDLP-------------PEERARLGIFLAFQYPPEIPGVKNadflryvnEGFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190
....*....|....*....|....*....|
gi 495164891 443 NHLDMEGKEALAQTLQTF--EG-GLLLVTH 469
Cdd:cd03217 133 SGLDIDALRLVAEVINKLreEGkSVLIITH 162
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
320-487 |
3.59e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 51.70 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVPGvtfHPRVSLgyYDQSLHQLPdnatllealepfAPELQQRKLAL- 398
Cdd:PRK13548 25 LRPGEVVAILGPNGAGKSTLLRAL-----SGELSPD---SGEVRL--NGRPLADWS------------PAELARRRAVLp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 399 ----ISAGF-----------PWARHGQRVD---------------------TLSGGERSRllfvgLSLAR---------- 432
Cdd:PRK13548 83 qhssLSFPFtveevvamgraPHGLSRAEDDalvaaalaqvdlahlagrdypQLSGGEQQR-----VQLARvlaqlwepdg 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 433 -YSLLMLDEPTNHLDMEGKEALAQTLQTF--EGGL--LLVTHDRTLMEASCNRFWLVEDG 487
Cdd:PRK13548 158 pPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLavIVVLHDLNLAARYADRIVLLHQG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-152 |
3.59e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSlrIDSPFG--PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL--LARVEQH- 75
Cdd:PRK15439 8 APPLLCARS--ISKQYSgvEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarLTPAKAHq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 76 -----LPDELH---QQTLLDALLARLPEAERESSawRAQALLANMGfAEAAWSLTAGSLSGGQHTRLLLARALIISPDLL 147
Cdd:PRK15439 86 lgiylVPQEPLlfpNLSVKENILFGLPKRQASMQ--KMKQLLAALG-CQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
....*
gi 495164891 148 LLDEP 152
Cdd:PRK15439 163 ILDEP 167
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
320-487 |
3.65e-07 |
|
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: 51.28 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLWRQWQT----------GETVPGVTFHPRV-------SLGYYDQSLHQLPDNATLLE 382
Cdd:COG4778 34 VAAGECVALTGPSGAGKSTLLKCIYGNYLPdsgsilvrhdGGWVDLAQASPREilalrrrTIGYVSQFLRVIPRVSALDV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 383 ALEPfapelqqrklaLISAGFPWARHGQRVDTL------------------SGGERSRLlfvglSLAR-----YSLLMLD 439
Cdd:COG4778 114 VAEP-----------LLERGVDREEARARARELlarlnlperlwdlppatfSGGEQQRV-----NIARgfiadPPLLLLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 440 EPTNHLDMEGKEALAQTLQTF--EG-GLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:COG4778 178 EPTASLDAANRAVVVELIEEAkaRGtAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-487 |
4.05e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.11 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLWRQWQ--------TGETVPGVTFHPRVSLGYYDQSLHQLPDnATLLEALEPFA-- 388
Cdd:PRK13537 29 HVQRGECFGLLGPNGAGKTTTLRMLLGLTHpdagsislCGEPVPSRARHARQRVGVVPQFDNLDPD-FTVRENLLVFGry 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 389 ---PELQQRklALISAGFPWARHGQRVDT----LSGGERSRllfvgLSLARY-----SLLMLDEPTNHLDMEGKEALAQT 456
Cdd:PRK13537 108 fglSAAAAR--ALVPPLLEFAKLENKADAkvgeLSGGMKRR-----LTLARAlvndpDVLVLDEPTTGLDPQARHLMWER 180
|
170 180 190
....*....|....*....|....*....|....
gi 495164891 457 LQTFEGG---LLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:PRK13537 181 LRSLLARgktILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-61 |
4.14e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.53 E-value: 4.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 495164891 9 SLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV 61
Cdd:PRK13632 14 SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI 66
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
18-157 |
4.49e-07 |
|
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: 52.80 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVEQHLpdELHQQTLL 86
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILldghdladytlASLRRQVALVSQDV--VLFNDTIA 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 87 D----ALLARLPEAERESSAWRA--QALLANM--GFAEAAWSlTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:TIGR02203 424 NniayGRTEQADRAEIERALAAAyaQDFVDKLplGLDTPIGE-NGVLLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-151 |
5.74e-07 |
|
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: 52.49 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 13 DSPF--GPelnaLSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV----------TRAA-RCLLARV--EQHLP 77
Cdd:COG4615 343 DEGFtlGP----IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIlldgqpvtadNREAyRQLFSAVfsDFHLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 78 DElhqqtLLDALLARLPEaeressawRAQALLANMG------FAEAAWSLTAgsLSGGQHTRLLLARALIISPDLLLLDE 151
Cdd:COG4615 419 DR-----LLGLDGEADPA--------RARELLERLEldhkvsVEDGRFSTTD--LSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
291-489 |
6.35e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 291 AADRLLELENLAVSAAPDT---PTLFTLPLARLksgdrVALLGHNGCGKSSLLRLLWR-----------------QWQTG 350
Cdd:PRK10575 7 HSDTTFALRNVSFRVPGRTllhPLSLTFPAGKV-----TGLIGHNGSGKSTLLKMLGRhqppsegeilldaqpleSWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 351 ETVPGVTFHPRV----------------------SLGYYDQSLHQLPDNATLLEALEPFAPELqqrklalisagfpwarh 408
Cdd:PRK10575 82 AFARKVAYLPQQlpaaegmtvrelvaigrypwhgALGRFGAADREKVEEAISLVGLKPLAHRL----------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 409 gqrVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKE---ALAQTLQTFEG-GLLLVTHDRTLMEASCNRFWLV 484
Cdd:PRK10575 145 ---VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVdvlALVHRLSQERGlTVIAVLHDINMAARYCDYLVAL 221
|
....*
gi 495164891 485 EDGGL 489
Cdd:PRK10575 222 RGGEM 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-180 |
6.56e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 50.74 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-------------RAARCLLA--------RVEQHLPDELH- 81
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlngqdhtttppsrRPVSMLFQennlfshlTVAQNIGLGLNp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 82 ----------------QQTLLDALLARLPeaeressawraqallanmgfaeaawsltaGSLSGGQHTRLLLARALIISPD 145
Cdd:PRK10771 99 glklnaaqreklhaiaRQMGIEDLLARLP-----------------------------GQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495164891 146 LLLLDEPGNHLDlPT----MLWL-EQFLARWNGSFILVSH 180
Cdd:PRK10771 150 ILLLDEPFSALD-PAlrqeMLTLvSQVCQERQLTLLMVSH 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-191 |
6.95e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 26 TLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARclLARVEQHL-PDelhQQTLLDALLARLPEAERESSAWR 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--ISYKPQYIsPD---YDGTVEEFLRSANTDDFGSSYYK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 105 AQ--------ALLANMgfaeaawsltAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDlptmlwLEQFL-------- 168
Cdd:COG1245 437 TEiikplgleKLLDKN----------VKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD------VEQRLavakairr 500
|
170 180
....*....|....*....|....*
gi 495164891 169 -ARWNG-SFILVSHDSALLDSVTNR 191
Cdd:COG1245 501 fAENRGkTAMVVDHDIYLIDYISDR 525
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-206 |
7.44e-07 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 50.18 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 11 RIDSPfgPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCLLARVeqhlPDE 79
Cdd:cd03244 13 RPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiglHDLRSRISII----PQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 80 --LHQQTL---LDAlLARLPEAERessaWRAqalLANMGFAEAAWSLTAG----------SLSGGQHTRLLLARALIISP 144
Cdd:cd03244 87 pvLFSGTIrsnLDP-FGEYSDEEL----WQA---LERVGLKEFVESLPGGldtvveeggeNLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495164891 145 DLLLLDEPGNHLDLPTMLWLEQFLARW--NGSFILVSHD-SALLDSvtNRTWILRDGQLQAFDLP 206
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAHRlDTIIDS--DRILVLDKGRVVEFDSP 221
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
320-458 |
9.84e-07 |
|
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: 49.55 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLwRQWQTGETVPG----------VTFHPRVslGYYDQ-SLHqlPDNATLLEALEpfa 388
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVL-AGRKTAGVITGeilingrpldKNFQRST--GYVEQqDVH--SPNLTVREALR--- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495164891 389 pelqqrklalISAgfpWARhgqrvdTLSGGERSRLLfVGLSL-ARYSLLMLDEPTNHLDMEGKEALAQTLQ 458
Cdd:cd03232 102 ----------FSA---LLR------GLSVEQRKRLT-IGVELaAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
125-181 |
1.03e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 50.55 E-value: 1.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 125 SLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWNGSF--ILVSHD 181
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYtiIIVTHN 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-198 |
1.31e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.94 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 12 IDSPFGP--ELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT------------RAARCLLARVEQHLP 77
Cdd:PRK09700 11 IGKSFGPvhALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinninynkldhkLAAQLGIGIIYQELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 78 --DELhqqTLLDAL-LARLPEAE------------REssawRAQALLANMGFaEAAWSLTAGSLSGGQHTRLLLARALII 142
Cdd:PRK09700 91 viDEL---TVLENLyIGRHLTKKvcgvniidwremRV----RAAMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 143 SPDLLLLDEPGNHL---DLPTMLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDG 198
Cdd:PRK09700 163 DAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-63 |
1.38e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 1.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTR 63
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDR 83
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-202 |
1.55e-06 |
|
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: 50.98 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 5 LTAHSlrIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPA-EGVV------------TRAARCLLAR 71
Cdd:TIGR02633 263 LTCWD--VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVfingkpvdirnpAQAIRAGIAM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 72 VEQH------LPDELHQQTLLDALLARLPEAERESSAWRAQALLANMG---FAEAAWSLTAGSLSGGQHTRLLLARALII 142
Cdd:TIGR02633 341 VPEDrkrhgiVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQrlkVKTASPFLPIGRLSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164891 143 SPDLLLLDEPGNHLDLPT---MLWLEQFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQA 202
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-181 |
1.60e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.49 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRID--SPFG--PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLApAEGVVTRAA----RCLLARV 72
Cdd:PRK09473 9 ADALLDVKDLRVTfsTPDGdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIGGSAtfngREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 73 EQHL--------------------P-----DELHQQTLLDALLARlPEAERESsawrAQALLA-NMGFAEAAWSLTAGSL 126
Cdd:PRK09473 88 EKELnklraeqismifqdpmtslnPymrvgEQLMEVLMLHKGMSK-AEAFEES----VRMLDAvKMPEARKRMKMYPHEF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 127 SGGQHTRLLLARALIISPDLLLLDEPGNHLDLPT----MLWLEQFLARWNGSFILVSHD 181
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqiMTLLNELKREFNTAIIMITHD 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-200 |
1.64e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.82 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 10 LRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTraarcllarVEQHLPDELHQQTLLDAL 89
Cdd:PRK15439 269 LTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIM---------LNGKEINALSTAQRLARG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 LARLPEaERESS--------AWRAQALLAN-MGF-----AEAA---------------WSLTAGSLSGGQHTRLLLARAL 140
Cdd:PRK15439 340 LVYLPE-DRQSSglyldaplAWNVCALTHNrRGFwikpaRENAvleryrralnikfnhAEQAARTLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164891 141 IISPDLLLLDEPGNHLDLPTMLWLEQF---LARWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLirsIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-160 |
1.67e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 50.73 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 17 GPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGV----------VTRAA-RCLLARVEQHlpDELHQQTL 85
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRilidgtdirtVTRASlRRNIAVVFQD--AGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 86 LDALLARLP---EAERESSAWRAQALlanmGFAEAA---WSLTAG----SLSGGQHTRLLLARALIISPDLLLLDEPGNH 155
Cdd:PRK13657 426 EDNIRVGRPdatDEEMRAAAERAQAH----DFIERKpdgYDTVVGergrQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
....*
gi 495164891 156 LDLPT 160
Cdd:PRK13657 502 LDVET 506
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-187 |
1.98e-06 |
|
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: 48.76 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 35 LIGHNGCGKSTLLKALD----GTLAPAegvvtraarcllARVEQHLPD-----------ELHQQTLLDALLarlpEAERE 99
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPN------------SKGGAHDPKliregevraqvKLAFENANGKKY----TITRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 100 SSAWRaQALLANMGfaEAAWSL--TAGSLSGGQHT------RLLLARALIISPDLLLLDEPGNHLDLPTmlwLEQFLAR- 170
Cdd:cd03240 91 LAILE-NVIFCHQG--ESNWPLldMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---IEESLAEi 164
|
170 180
....*....|....*....|....
gi 495164891 171 -------WNGSFILVSHDSALLDS 187
Cdd:cd03240 165 ieerksqKNFQLIVITHDEELVDA 188
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-174 |
3.12e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEG-VVTRAARCLLARVEQhlpdelhQQTLLDALLAR-----LPEAE 97
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGeRQSQFSHITRLSFEQ-------LQKLVSDEWQRnntdmLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 98 RESSAWRAQALLANMGFAEAAWSLTA------------GSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLE 165
Cdd:PRK10938 96 DDTGRTTAEIIQDEVKDPARCEQLAQqfgitalldrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
....*....
gi 495164891 166 QFLARWNGS 174
Cdd:PRK10938 176 ELLASLHQS 184
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
296-498 |
3.18e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.84 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAaPDTPTLfTLPLA-RLKSGDRVALLGHNGCGKSSLLRLL------------------------WRQ---W 347
Cdd:PRK11174 350 IEAEDLEILS-PDGKTL-AGPLNfTLPAGQRIALVGPSGAGKTSLLNALlgflpyqgslkingielreldpesWRKhlsW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 348 qTGE--TVPGVTFHPRVSLG---YYDQSLHQLPDNATLLEalepFAPELQQRKLALIsagfpwarhGQRVDTLSGGERSR 422
Cdd:PRK11174 428 -VGQnpQLPHGTLRDNVLLGnpdASDEQLQQALENAWVSE----FLPLLPQGLDTPI---------GDQAAGLSVGQAQR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 423 LlfvglSLAR-----YSLLMLDEPTNHLDMEGKEALAQTLQTFEGG--LLLVTH--DRTlmeASCNRFWLVEDGGLSEWH 493
Cdd:PRK11174 494 L-----ALARallqpCQLLLLDEPTASLDAHSEQLVMQALNAASRRqtTLMVTHqlEDL---AQWDQIWVMQDGQIVQQG 565
|
....*
gi 495164891 494 NMEAL 498
Cdd:PRK11174 566 DYAEL 570
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
321-487 |
3.27e-06 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 48.97 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 321 KSGDRVALLGHNGCGKSSLLRLLwrqwqTG-------------------ETVPGVtfhpRVSLGYydqsLHQLPDN---A 378
Cdd:TIGR04520 26 EKGEFVAIIGHNGSGKSTLAKLL-----NGlllptsgkvtvdgldtldeENLWEI----RKKVGM----VFQNPDNqfvG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 379 TLLEALEPFAPELQqrklalisaGFPWARHGQRVD-----------------TLSGGERSRLLFVGLsLA-RYSLLMLDE 440
Cdd:TIGR04520 93 ATVEDDVAFGLENL---------GVPREEMRKRVDealklvgmedfrdrephLLSGGQKQRVAIAGV-LAmRPDIIILDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495164891 441 PTNHLDMEGKEALAQTLQTF--EGGL--LLVTHDrtlME--ASCNRFWLVEDG 487
Cdd:TIGR04520 163 ATSMLDPKGRKEVLETIRKLnkEEGItvISITHD---MEeaVLADRVIVMNKG 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-157 |
4.45e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 49.30 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRIDspFGPE------LNALSFTLKKGDRIGLIGHNGCGKS----TLLKALDGTLAPAEGVVTRAARCLLA 70
Cdd:COG4172 3 SMPLLSVEDLSVA--FGQGggtveaVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 71 RVEQHL--------------------PdeLH---QQ---TLldALLARLPEAERESsawRAQALLANMGFAEAAWSLTA- 123
Cdd:COG4172 81 LSERELrrirgnriamifqepmtslnP--LHtigKQiaeVL--RLHRGLSGAAARA---RALELLERVGIPDPERRLDAy 153
|
170 180 190
....*....|....*....|....*....|....*
gi 495164891 124 -GSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:COG4172 154 pHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-186 |
4.82e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.40 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 26 TLKKGDRIGLIGHNGCGKSTLLKALDGTLAP------------------------------AEG---------------- 59
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPnlgdydeepswdevlkrfrgtelqdyfkklANGeikvahkpqyvdlipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 60 VVTRAARCLLARV-EQHLPDELHQQTLLDALLarlpeaERESSawraqallanmgfaeaawsltagSLSGGQHTRLLLAR 138
Cdd:COG1245 175 VFKGTVRELLEKVdERGKLDELAEKLGLENIL------DRDIS-----------------------ELSGGELQRVAIAA 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 139 ALIISPDLLLLDEPGNHLDLP---TMLWLEQFLARWNGSFILVSHDSALLD 186
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIYqrlNVARLIRELAEEGKYVLVVEHDLAILD 276
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-157 |
5.16e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 49.28 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPA---EGVVT-----RAARCLLAR---VEQhlpDELHQQTL--L 86
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLlngmpIDAKEMRAIsayVQQ---DDLFIPTLtvR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 87 DALL--------ARLPEAERESsawRAQALLANMGFAEAAWSLTA-----GSLSGGQHTRLLLARALIISPDLLLLDEPG 153
Cdd:TIGR00955 118 EHLMfqahlrmpRRVTKKEKRE---RVDEVLQALGLRKCANTRIGvpgrvKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
....
gi 495164891 154 NHLD 157
Cdd:TIGR00955 195 SGLD 198
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
318-446 |
5.71e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 47.65 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 318 ARLKSGDRVALLGHNGCGKSSLLRLLWRQWQTGETVPGvtfhpRVSLGYYDQSLHQLPDNATLLEALEPFAPELQQRKLA 397
Cdd:cd03234 28 LHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSG-----QILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 398 LISAGFPWARH------------------------GQRVDTLSGGERSRllfvgLSLARY-----SLLMLDEPTNHLD 446
Cdd:cd03234 103 TYTAILRLPRKssdairkkrvedvllrdlaltrigGNLVKGISGGERRR-----VSIAVQllwdpKVLILDEPTSGLD 175
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-200 |
8.11e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARcllarveqhlpdELHQQTLLDAL---LARLP 94
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGK------------KINNHNANEAInhgFALVT 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 95 EaERESSAWRAQ------ALLANMGFAEAAWSL--------------------------TAGSLSGGQHTRLLLARALII 142
Cdd:PRK10982 330 E-ERRSTGIYAYldigfnSLISNIRNYKNKVGLldnsrmksdtqwvidsmrvktpghrtQIGSLSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495164891 143 SPDLLLLDEPGNHLDLPTMLWLEQF---LARWNGSFILVSHDSALLDSVTNRTWILRDGQL 200
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLiaeLAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-180 |
8.12e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.87 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 4 LLTAHSLRIDSPFGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL---LARVEQHLPDEL 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 81 HQQTLLDALLArlpeaeRESSAWRAQALLANMGFAEAA--WSL------TAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:PRK13540 81 HRSGINPYLTL------RENCLYDIHFSPGAVGITELCrlFSLehlidyPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 495164891 153 GNHLD----LPTMLWLEQFLARwNGSFILVSH 180
Cdd:PRK13540 155 LVALDelslLTIITKIQEHRAK-GGAVLLTSH 185
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
290-491 |
8.72e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.08 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 290 LAADRLLELENLAVSAAPDTPTLFTLPLARL--KSGDRVALLGHNGCGKSSLLRLL--------WRQWQTGETVPGVTFH 359
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELvvKRGETIALIGESGSGKSTLLAILaglddgssGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 360 PRVSL-----GYYDQSLHQLPDNATL----LEALEPFAPELQQRKLA---LISAGFpwarhGQRVD----TLSGGERSRL 423
Cdd:PRK10584 81 ARAKLrakhvGFVFQSFMLIPTLNALenveLPALLRGESSRQSRNGAkalLEQLGL-----GKRLDhlpaQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495164891 424 LFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTL----QTFEGGLLLVTHDRTLmEASCNRFWLVEDGGLSE 491
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQL-AARCDRRLRLVNGQLQE 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
33-180 |
9.16e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.56 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 33 IGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPD--ELHQQ---TLLDALLA--RLPEAERESSAWRA 105
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQgvAMVQQdpvVLADTFLAnvTLGRDISEEQVWQA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 106 qalLANMGFAEAAWSLTAG----------SLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLA--RWNG 173
Cdd:PRK10790 450 ---LETVQLAELARSLPDGlytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAavREHT 526
|
....*..
gi 495164891 174 SFILVSH 180
Cdd:PRK10790 527 TLVVIAH 533
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
296-446 |
9.23e-06 |
|
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: 47.18 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTLFTLPLArLKSGDRVALLGHNGCGKSSLLRLLWR--QWQTGE-TVPGVTFH---------PRVS 363
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLS-INPGEFVALIGPSGAGKSTLLRCLNGlvEPTSGSvLIDGTDINklkgkalrqLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 364 LGYYDQSlHQLPDNATLLEA---------------LEPFAPELQQRKLALISAGFPWARHGQRVDTLSGGERSRllfVGL 428
Cdd:cd03256 80 IGMIFQQ-FNLIERLSVLENvlsgrlgrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQR---VAI 155
|
170 180
....*....|....*....|.
gi 495164891 429 --SLARYSLLML-DEPTNHLD 446
Cdd:cd03256 156 arALMQQPKLILaDEPVASLD 176
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
296-501 |
9.71e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 48.24 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTL--FTLplaRLKSGDRVALLGHNGCGKSSLLRLLWRQWQTGEtvpGvtfhpRVSLG---YYDQS 370
Cdd:COG1132 340 IEFENVSFSYPGDRPVLkdISL---TIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS---G-----RILIDgvdIRDLT 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 371 LHQLPD------------NATLLEALEPFAP-----ELQQrklALISAGF-PWARH---------GQRVDTLSGGERSRL 423
Cdd:COG1132 409 LESLRRqigvvpqdtflfSGTIRENIRYGRPdatdeEVEE---AAKAAQAhEFIEAlpdgydtvvGERGVNLSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 424 lfvglSLARY-----SLLMLDEPTNHLDMEGKEALAQTLQTFEGG--LLLVTHdR--TLMEAscNRFWLVEDGGLSEWHN 494
Cdd:COG1132 486 -----AIARAllkdpPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH-RlsTIRNA--DRILVLDDGRIVEQGT 557
|
....*..
gi 495164891 495 MEALLAR 501
Cdd:COG1132 558 HEELLAR 564
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-487 |
1.13e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 47.52 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLWRQWQT--------GETVPGVTFHPRVSLGYYDQsLHQLPDNATLLEALEPFAP- 389
Cdd:PRK13536 63 TVASGECFGLLGPNGAGKSTIARMILGMTSPdagkitvlGVPVPARARLARARIGVVPQ-FDNLDLEFTVRENLLVFGRy 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 390 -ELQQRKL-ALISAGFPWARHGQRVDT----LSGGERSRllfvgLSLARY-----SLLMLDEPTNHLDMEGKEALAQTLQ 458
Cdd:PRK13536 142 fGMSTREIeAVIPSLLEFARLESKADArvsdLSGGMKRR-----LTLARAlindpQLLILDEPTTGLDPHARHLIWERLR 216
|
170 180 190
....*....|....*....|....*....|..
gi 495164891 459 TFEG---GLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:PRK13536 217 SLLArgkTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-152 |
1.21e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 48.09 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 17 GPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT------------RAARCLLArveqHLPDELHQQT 84
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsprDAIRAGIA----YVPEDRKGEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 85 L-LD---------ALLARL-------PEAEREssawRAQALLANMGFAEAAWSLTAGSLSGG--QhtRLLLARALIISPD 145
Cdd:COG1129 341 LvLDlsirenitlASLDRLsrgglldRRRERA----LAEEYIKRLRIKTPSPEQPVGNLSGGnqQ--KVVLAKWLATDPK 414
|
....*..
gi 495164891 146 LLLLDEP 152
Cdd:COG1129 415 VLILDEP 421
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
319-487 |
1.28e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 46.98 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLL--WRQWQTGE----TVPGVTFHPRVSLGYYDQSLhqLP-----DNATL------- 380
Cdd:PRK11247 34 HIPAGQFVAVVGRSGCGKSTLLRLLagLETPSAGEllagTAPLAEAREDTRLMFQDARL--LPwkkviDNVGLglkgqwr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 381 ---LEALEpfAPELQQRklaliSAGFPWArhgqrvdtLSGGERSRllfVGLSLA---RYSLLMLDEPTNHLD----MEGK 450
Cdd:PRK11247 112 daaLQALA--AVGLADR-----ANEWPAA--------LSGGQKQR---VALARAlihRPGLLLLDEPLGALDaltrIEMQ 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 495164891 451 EALAQTLQTFEGGLLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:PRK11247 174 DLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-186 |
1.65e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 26 TLKKGDRIGLIGHNGCGKSTLLKALDGTLAP------------------------------AEG---------------- 59
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdyeeepswdevlkrfrgtelqnyfkklYNGeikvvhkpqyvdlipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 60 VVTRAARCLLARV-EQHLPDELHQQTLLDALLarlpeaERESSawraqallanmgfaeaawsltagSLSGGQHTRLLLAR 138
Cdd:PRK13409 175 VFKGKVRELLKKVdERGKLDEVVERLGLENIL------DRDIS-----------------------ELSGGELQRVAIAA 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495164891 139 ALIISPDLLLLDEPGNHLDLP---TMLWLEQFLARwNGSFILVSHDSALLD 186
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRqrlNVARLIRELAE-GKYVLVVEHDLAVLD 275
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
320-487 |
1.69e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 46.93 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRL---LWRQWQTGETVPGVTFHP------RVSLGYydqsLHQLPDN---ATLLEALEPF 387
Cdd:PRK13635 30 VYEGEWVAIVGHNGSGKSTLAKLlngLLLPEAGTITVGGMVLSEetvwdvRRQVGM----VFQNPDNqfvGATVQDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 388 APELQqrklalisaGFPWARHGQRVD-----------------TLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGK 450
Cdd:PRK13635 106 GLENI---------GVPREEMVERVDqalrqvgmedflnrephRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495164891 451 EALAQTLQTF--EGGL--LLVTHDrtLME-ASCNRFWLVEDG 487
Cdd:PRK13635 177 REVLETVRQLkeQKGItvLSITHD--LDEaAQADRVIVMNKG 216
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-186 |
1.81e-05 |
|
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: 46.59 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 28 KKGDRIGLIGHNGCGKSTLLKALDGTLAPAEG----------------------------------------------VV 61
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselqnyftkllegdvkvivkpqyvdlipkAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 62 TRAARCLLARV-EQHLPDELHQQTLLDALLarlpeaERESSawraqallanmgfaeaawsltagSLSGGQHTRLLLARAL 140
Cdd:cd03236 104 KGKVGELLKKKdERGKLDELVDQLELRHVL------DRNID-----------------------QLSGGELQRVAIAAAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495164891 141 IISPDLLLLDEPGNHLDLP---TMLWLEQFLARWNGSFILVSHDSALLD 186
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
295-487 |
1.90e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.61 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 295 LLELENLAVSAAPDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP--GVTFHPRVSLGYYDQSL- 371
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINF-KAEKGEMVALLGPNGAGKSTLFLHF-----NGILKPtsGEVLIKGEPIKYDKKSLl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 372 ---------HQLPDNatllealEPFAPELQQR-KLALISAGFPWARHGQRVDT-----------------LSGGERSRLL 424
Cdd:PRK13639 75 evrktvgivFQNPDD-------QLFAPTVEEDvAFGPLNLGLSKEEVEKRVKEalkavgmegfenkpphhLSGGQKKRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 425 FVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQTF-EGGLLLV--THDRTLMEASCNRFWLVEDG 487
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIisTHDVDLVPVYADKVYVMSDG 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-280 |
1.91e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKAL------------DG---------TLAPAEGVV-------TRAARCLLAR 71
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALlrllstegeiqiDGvswnsvtlqTWRKAFGVIpqkvfifSGTFRKNLDP 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 72 VEQHLPDEL---HQQTLLDALLARLPEaeressawRAQALLANMGFAeaawsltagsLSGGQHTRLLLARALIISPDLLL 148
Cdd:TIGR01271 1315 YEQWSDEEIwkvAEEVGLKSVIEQFPD--------KLDFVLVDGGYV----------LSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 149 LDEPGNHLDLPTMlwleQFLARwngsfilvshdsALLDSVTNRTWILRDGQLQAFdLPCTQaraaLAARDESDALRHKAE 228
Cdd:TIGR01271 1377 LDEPSAHLDPVTL----QIIRK------------TLKQSFSNCTVILSEHRVEAL-LECQQ----FLVIEGSSVKQYDSI 1435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 229 QKEID------RVTASAKRLATWGQVYDNEDlARKAKqmeKQVARLKEEQTELAQGSR 280
Cdd:TIGR01271 1436 QKLLNetslfkQAMSAADRLKLFPLHRRNSS-KRKPQ---PKITALREEAEEEVQNTR 1489
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
410-477 |
2.15e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 410 QRVDTLSGGERSRLLF-VGLSLARY-----SLLMLDEPTNHLDMEGKEALAQTLQTF---EGG---LLLVTHDRTLMEAS 477
Cdd:PRK01156 797 EGIDSLSGGEKTAVAFaLRVAVAQFlnndkSLLIMDEPTAFLDEDRRTNLKDIIEYSlkdSSDipqVIMISHHRELLSVA 876
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
412-485 |
2.16e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.68 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 412 VDTLSGGERSRL-LFVGLSLARY-----SLLMLDEPTNHLDMEGKE-ALAQTLQTFEGG----LLLVTHDRTLMEAScNR 480
Cdd:cd03240 113 RGRCSGGEKVLAsLIIRLALAETfgsncGILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIVITHDEELVDAA-DH 191
|
....*
gi 495164891 481 FWLVE 485
Cdd:cd03240 192 IYRVE 196
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
295-476 |
2.21e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 46.63 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 295 LLELENLAVSAApDTPTL--FTLplaRLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGetvpgvtFHP----RVSLGyyD 368
Cdd:COG3842 5 ALELENVSKRYG-DVTALddVSL---SIEPGEFVALLGPSGCGKTTLLRMI-----AG-------FETpdsgRILLD--G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 369 QSLHQLP----------------------DN-ATLLEALEPFAPELQQR---KLALIS-AGFpwarHGQRVDTLSGGERS 421
Cdd:COG3842 67 RDVTGLPpekrnvgmvfqdyalfphltvaENvAFGLRMRGVPKAEIRARvaeLLELVGlEGL----ADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 422 RllfVGL--SLA-RYSLLMLDEPTNHLDMEGKEALAQTLQ--------TFegglLLVTHDRTlmEA 476
Cdd:COG3842 143 R---VALarALApEPRVLLLDEPLSALDAKLREEMREELRrlqrelgiTF----IYVTHDQE--EA 199
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
294-508 |
2.72e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.85 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 294 RLLELENLAVSAAPdtPTLFTLPLArLKSGDRVALLGHNGCGKS----SLLRLL---WRQWQ----------TGETVPGV 356
Cdd:PRK10418 3 QQIELRNIALQAAQ--PLVHGVSLT-LQRGRVLALVGGSGSGKSltcaAALGILpagVRQTAgrvlldgkpvAPCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 357 T-----------FHPRVSLGYYD----QSLHQLPDNATLLEALEPFAPELQQRKLALisagFPWarhgqrvdTLSGGERS 421
Cdd:PRK10418 80 KiatimqnprsaFNPLHTMHTHAretcLALGKPADDATLTAALEAVGLENAARVLKL----YPF--------EMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 422 RLLFVGLSLARYSLLMLDEPTNHLDMEGK----EALAQTLQTFEGGLLLVTHDRTLMEASCNRFWLVEDGGLSEWHNMEA 497
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQarilDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
250
....*....|.
gi 495164891 498 LLARLRAAPTQ 508
Cdd:PRK10418 228 LFNAPKHAVTR 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
293-470 |
2.82e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 46.27 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 293 DRLLELENLAVSAAPDTPTLFTLPLArLKSGDRVALLGHNGCGKSSLLRLL---WRQWQTGETVPGVTFHP--------R 361
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLS-IPEGSKTALLGPNGAGKSTLLLHLngiYLPQRGRVKVMGREVNAenekwvrsK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 362 VSLGYYDqslhqlPDN----ATLLEALePFAP--------ELQQRKLALISAGFPWARHGQRVDTLSGGERSRLLFVGLS 429
Cdd:PRK13647 81 VGLVFQD------PDDqvfsSTVWDDV-AFGPvnmgldkdEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 430 LARYSLLMLDEPTNHLDMEGKEALAQTLQTF--EGG-LLLVTHD 470
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGKtVIVATHD 197
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-151 |
3.05e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 19 ELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVtraarcLLARVEQHLPDELHQQTLLDA------LLAR 92
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI------LLDGKPVTAEQPEDYRKLFSAvftdfhLFDQ 411
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495164891 93 L--PEAErESSAWRAQALLANMGFAE----AAWSLTAGSLSGGQHTRLLLARALIISPDLLLLDE 151
Cdd:PRK10522 412 LlgPEGK-PANPALVEKWLERLKMAHklelEDGRISNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-157 |
3.08e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAE--GVVTRAARCLLARVEQHLPDELHQQTLLDALLarlpE 95
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtsSVVIRGSVAYVPQVSWIFNATVRENILFGSDF----E 706
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 96 AERESSAWRAQALLANMGFAEAAWSLTAG----SLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PLN03232 707 SERYWRAIDVTALQHDLDLLPGRDLTEIGergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
313-477 |
3.60e-05 |
|
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: 44.62 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 313 FTLPLARLksgdrVALLGHNGCGKSSLLRllwrqwQTGETVpgvtfhprvSLGYYDQSLHQLPDNATLlealepFAPELQ 392
Cdd:cd03238 16 VSIPLNVL-----VVVTGVSGSGKSTLVN------EGLYAS---------GKARLISFLPKFSRNKLI------FIDQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 393 qrklALISAGFPWARHGQRVDTLSGGERSRLL---FVGLSLARySLLMLDEPTNHLDMEGKEALAQTLQTF--EGG-LLL 466
Cdd:cd03238 70 ----FLIDVGLGYLTLGQKLSTLSGGELQRVKlasELFSEPPG-TLFILDEPSTGLHQQDINQLLEVIKGLidLGNtVIL 144
|
170
....*....|.
gi 495164891 467 VTHDRTLMEAS 477
Cdd:cd03238 145 IEHNLDVLSSA 155
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-181 |
3.84e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.46 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 1 MSTLLTAHSLRIDSPfGPELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPaeGVVTRAARCLLARVEQHlPDEL 80
Cdd:PRK10418 1 MPQQIELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVA-PCAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 81 HQ-----------------QTLLDALLARLPEAERESSAWRAQALLANMGFAEAA--WSLTAGSLSGGQHTRLLLARALI 141
Cdd:PRK10418 77 RGrkiatimqnprsafnplHTMHTHARETCLALGKPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 495164891 142 ISPDLLLLDEPGNHLDLPTML----WLEQFLARWNGSFILVSHD 181
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQArildLLESIVQKRALGMLLVTHD 200
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
321-501 |
4.66e-05 |
|
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: 44.91 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 321 KSGDRVALLGHNGCGKSSLLRLLWRQWQT--------GETVPGVTFHP-RVSLGYYDQSLHQLpdNATLLEAL---EPFA 388
Cdd:cd03251 26 PAGETVALVGPSGSGKSTLVNLIPRFYDVdsgrilidGHDVRDYTLASlRRQIGLVSQDVFLF--NDTVAENIaygRPGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 389 PELQQRKLALISA------GFPWARH---GQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQT 459
Cdd:cd03251 104 TREEVEEAARAANahefimELPEGYDtviGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALER 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495164891 460 F-EGGLLLVTHDR--TLMEAscNRFWLVEDGGLSEWHNMEALLAR 501
Cdd:cd03251 184 LmKNRTTFVIAHRlsTIENA--DRIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-199 |
4.87e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.08 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGtLAPA---EGVVTRAARCLLARveqHLPDE-------LHQQTlldAL 89
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQAS---NIRDTeragiaiIHQEL---AL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 LARLPEAE-----RESSA-----W-----RAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGN 154
Cdd:PRK13549 94 VKELSVLEniflgNEITPggimdYdamylRAQKLLAQLKLDINP-ATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495164891 155 HL---DLPTMLWLEQFLARWNGSFILVSHD----SALLDSVTnrtwILRDGQ 199
Cdd:PRK13549 173 SLtesETAVLLDIIRDLKAHGIACIYISHKlnevKAISDTIC----VIRDGR 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
320-491 |
4.88e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 45.45 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLL------------WRqwqtGETVPGV------TFHPRVSLGYYDqSLHQLPDNATLL 381
Cdd:PRK10419 35 LKSGETVALLGRSGCGKSTLARLLvglespsqgnvsWR----GEPLAKLnraqrkAFRRDIQMVFQD-SISAVNPRKTVR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 382 EAL-EPF-------APELQQRKLALISA-GFPWARHGQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEA 452
Cdd:PRK10419 110 EIIrEPLrhllsldKAERLARASEMLRAvDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAG 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495164891 453 LAQTL----QTFEGGLLLVTHDRTLMEASCNRFWLVEDGGLSE 491
Cdd:PRK10419 190 VIRLLkklqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-151 |
5.72e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQHLPDELH--QQTLLDALLARLPEAE 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTgiENIELKGLMMGLTKEK 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 98 REssawraQALLANMGFAEAAWSLT--AGSLSGGQHTRLLLARALIISPDLLLLDE 151
Cdd:PRK13545 120 IK------EIIPEIIEFADIGKFIYqpVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-157 |
6.12e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 23 LSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAE-----------------------GVVTRAARCLLARVEQHLPDE 79
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEgdiiindshnlkdinlkwwrskiGVVSQDPLLFSNSIKNNIKYS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 80 LHQQTLLDALLARLPE---------AERESSAWRAQALLANMGFAEAAWSL----------------------------- 121
Cdd:PTZ00265 484 LYSLKDLEALSNYYNEdgndsqenkNKRNSCRAKCAGDLNDMSNTTDSNELiemrknyqtikdsevvdvskkvlihdfvs 563
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495164891 122 ------------TAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PTZ00265 564 alpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
320-470 |
6.66e-05 |
|
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: 44.71 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP--GVTFHPRVSLGYYDQSLHqlPDNATLLEAL----------EPF 387
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKML-----AGVLKPdeGDIEIELDTVSYKPQYIK--ADYEGTVRDLlssitkdfytHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 388 -----APELQQRKLalisagfpwarHGQRVDTLSGGERSRLLfVGLSLAR-YSLLMLDEPTNHLDMEGKEALAQTLQTF- 460
Cdd:cd03237 95 fkteiAKPLQIEQI-----------LDREVPELSGGELQRVA-IAACLSKdADIYLLDEPSAYLDVEQRLMASKVIRRFa 162
|
170
....*....|...
gi 495164891 461 ---EGGLLLVTHD 470
Cdd:cd03237 163 ennEKTAFVVEHD 175
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-198 |
7.67e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 44.24 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVV--------TRAARCLLARVEQHLPDELHQQTLLDAL 89
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesEPSFEATRSRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 90 LARLPEAERESSAWRAQALLANMGFAEAAWSLTAG----------SLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLP 159
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495164891 160 TMLWLEQ-----FLARWNGSFILVSHDsalLDSVTNRTWI--LRDG 198
Cdd:cd03290 175 LSDHLMQegilkFLQDDKRTLVLVTHK---LQYLPHADWIiaMKDG 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
296-501 |
7.84e-05 |
|
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: 44.40 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAAPDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLL------------------------WRQWQTGE 351
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIqrfyvpengrvlvdghdlaladpaWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 352 TVPGVTFHPR-----VSLGYYDQSLHQLPDNATLLEALEpFAPELQQRKLALIsagfpwarhGQRVDTLSGGERSRLLFV 426
Cdd:cd03252 81 VLQENVLFNRsirdnIALADPGMSMERVIEAAKLAGAHD-FISELPEGYDTIV---------GEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 427 GLSLARYSLLMLDEPTNHLDMEGKEALAQTLQTFEGG--LLLVTHD-RTLMEAscNRFWLVEDGGLSEWHNMEALLAR 501
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAHRlSTVKNA--DRIIVMEKGRIVEQGSHDELLAE 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
126-508 |
8.36e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 126 LSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLA----RWNGSFILVSHDSALLDSVTNRTWILRDGQlq 201
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelqqELNMGLLFITHNLSIVRKLADRVAVMQNGR-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 202 afdlpCTQARAALAArdeSDALRHKAEQkeidrvtasakrlatwgQVYDNEDLARKAKQMEKQVARLKEEQTELAQGSRW 281
Cdd:PRK15134 235 -----CVEQNRAATL---FSAPTHPYTQ-----------------KLLNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 282 RLTlsgdalaadRLLELENLAVSAAPdtptlFTLplarlKSGDRVALLGHNGCGKSS----LLRLLWRQ---WQTGEtvP 354
Cdd:PRK15134 290 GIL---------KRTVDHNVVVKNIS-----FTL-----RPGETLGLVGESGSGKSTtglaLLRLINSQgeiWFDGQ--P 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 355 GVTFHPRVSLGYYD--QSLHQLPDNA---------TLLEALEPFAPEL--QQRKLALISA----GF-PWARHgqRVDT-L 415
Cdd:PRK15134 349 LHNLNRRQLLPVRHriQVVFQDPNSSlnprlnvlqIIEEGLRVHQPTLsaAQREQQVIAVmeevGLdPETRH--RYPAeF 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 416 SGGERSRLLFVGLSLARYSLLMLDEPTNHLDmegKEALAQTL-------QTFEGGLLLVTHDRTLMEASCNRFWLVEDGG 488
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLD---KTVQAQILallkslqQKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
410 420
....*....|....*....|
gi 495164891 489 LSEWHNMEALLARLRAAPTQ 508
Cdd:PRK15134 504 VVEQGDCERVFAAPQQEYTR 523
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
18-158 |
8.77e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 44.30 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCL-------LARVEQHLPDELHQQTLL--DA 88
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsreLAKRLAILRQENHINSRLtvRE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 89 LLA---------RLPEAERESSAwRAQALLANMGFAEAawSLTagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDL 158
Cdd:COG4604 95 LVAfgrfpyskgRLTAEDREIID-EAIAYLDLEDLADR--YLD--ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
320-489 |
1.03e-04 |
|
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: 43.86 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLL--WRQWQTGET-----VPG---VTFHPRVSL--GYYDQSLHQLP--DNATLLEALE 385
Cdd:cd03267 44 IEKGEIVGFIGPNGAGKTTTLKILsgLLQPTSGEVrvaglVPWkrrKKFLRRIGVvfGQKTQLWWDLPviDSFYLLAAIY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 386 PFAPELQQRKLALISAGFPWARH-GQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQTF---- 460
Cdd:cd03267 124 DLPPARFKKRLDELSELLDLEELlDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrer 203
|
170 180
....*....|....*....|....*....
gi 495164891 461 EGGLLLVTHDRTLMEASCNRFWLVEDGGL 489
Cdd:cd03267 204 GTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-157 |
1.09e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTrAARCLlARVEQHLpdELHQQTLLDALLARLPE-AER 98
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-AERSI-AYVPQQA--WIMNATVRGNILFFDEEdAAR 751
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164891 99 ESSAWRAQALLANMGFAEAAWSLTAG----SLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PTZ00243 752 LADAVRVSQLEADLAQLGGGLETEIGekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-184 |
1.36e-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: 44.74 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARCLLARVEQH----------------LPDELHQQ 83
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRpymtlgtlrdqiiypdSSEDMKRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 TLLDA-LLARLPEAEREssawraQALLANMGF-AEAAWSltaGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTM 161
Cdd:TIGR00954 548 GLSDKdLEQILDNVQLT------HILEREGGWsAVQDWM---DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
170 180
....*....|....*....|...
gi 495164891 162 LWLEQFLARWNGSFILVSHDSAL 184
Cdd:TIGR00954 619 GYMYRLCREFGITLFSVSHRKSL 641
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
414-501 |
1.58e-04 |
|
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: 43.48 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 414 TLSGGERSRllfvgLSLARY-----SLLMLDEPTNHLDMEGKEALAQTLQT----FEGGLLLVTHDRTLMEASCNRFWLV 484
Cdd:cd03299 129 TLSGGEQQR-----VAIARAlvvnpKILLLDEPFSALDVRTKEKLREELKKirkeFGVTVLHVTHDFEEAWALADKVAIM 203
|
90
....*....|....*..
gi 495164891 485 EDGGLSEWHNMEALLAR 501
Cdd:cd03299 204 LNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
295-487 |
1.66e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 43.82 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 295 LLELENLAVSAAPDTPTLFTLPLArLKSGDRVALLGHNGCGKSSLL------------RLLWRQWQTGE--TVPGVtfhp 360
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLV-IKKGEYIGIIGKNGSGKSTLAlhlngllrpqkgKVLVSGIDTGDfsKLQGI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 361 RVSLGYYDQSLHQLPDNATLLEALePFAPE------LQQRKL---ALISAGFPWARHgQRVDTLSGGERSRLLFVGLSLA 431
Cdd:PRK13644 76 RKLVGIVFQNPETQFVGRTVEEDL-AFGPEnlclppIEIRKRvdrALAEIGLEKYRH-RSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 432 RYSLLMLDEPTNHLDME-GKEALAQTLQTFEGG--LLLVTHDRTLMEAScNRFWLVEDG 487
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDsGIAVLERIKKLHEKGktIVYITHNLEELHDA-DRIIVMDRG 211
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
89-253 |
1.76e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 89 LLARLPEAERESSAWRAQALLANMGFAEAAwSLTAGSLSGGQHTRLLLARALIISPDLLLLDEPGNHLDLPTM--LWLE- 165
Cdd:NF000106 109 MIGR*LDLSRKDARARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRneVWDEv 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 166 QFLARWNGSFILVSHDSALLDSVTNRTWILRDGQLQAfDLPCTQARAALAARDESDALRHKAEQKEIDRVTASAKRLATW 245
Cdd:NF000106 188 RSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIA-DGKVDELKTKVGGRTLQIRPAHAAELDRMVGAIAQAGLDGIA 266
|
....*...
gi 495164891 246 GQVYDNED 253
Cdd:NF000106 267 GATADHED 274
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
295-469 |
2.02e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.87 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 295 LLELENLAVSAapDTPTLFT-LPLaRLKSGDRVALLGHNGCGKSSLLRLL------------WRqwqtGETVPGVTFHPR 361
Cdd:PRK13538 1 MLEARNLACER--DERILFSgLSF-TLNAGELVQIEGPNGAGKTSLLRILaglarpdagevlWQ----GEPIRRQRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 362 VSLGY------------------YDQSLHQLPDNATLLEALEpfapelqqrKLALisAGF---PwarhgqrVDTLSGGER 420
Cdd:PRK13538 74 QDLLYlghqpgikteltalenlrFYQRLHGPGDDEALWEALA---------QVGL--AGFedvP-------VRQLSAGQQ 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495164891 421 SRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQ--TFEGGL-LLVTH 469
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAqhAEQGGMvILTTH 187
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
321-472 |
2.14e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.18 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 321 KSGDRVALLGHNGCGKSSLLRLLWRQWQ--------TGETVPGVTfhpRVSL-----------GYYDQSLHQ-----LPD 376
Cdd:PRK13657 359 KPGQTVAIVGPTGAGKSTLINLLQRVFDpqsgriliDGTDIRTVT---RASLrrniavvfqdaGLFNRSIEDnirvgRPD 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 377 --NATLLEALE-PFAPELQQRKlaliSAGFPwARHGQRVDTLSGGERSRllfvgLSLARYSL-----LMLDEPTNHLDME 448
Cdd:PRK13657 436 atDEEMRAAAErAQAHDFIERK----PDGYD-TVVGERGRQLSGGERQR-----LAIARALLkdppiLILDEATSALDVE 505
|
170 180
....*....|....*....|....
gi 495164891 449 GKEALAQTLQTfegglllVTHDRT 472
Cdd:PRK13657 506 TEAKVKAALDE-------LMKGRT 522
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-152 |
2.39e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.86 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 24 SFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVT-----------RAARCL-LARVEQH--LPDELhqqTLLD-- 87
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvrirspRDAIALgIGMVHQHfmLVPNL---TVAEni 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 88 --------ALLARLPEAERessawRAQALLANMGFA---EAawslTAGSLSGGQHTRLLLARALIISPDLLLLDEP 152
Cdd:COG3845 102 vlgleptkGGRLDRKAARA-----RIRELSERYGLDvdpDA----KVEDLSVGEQQRVEILKALYRGARILILDEP 168
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-180 |
2.40e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDG----------TLAPAEgvvtRAARCLLARVEQHL---PDELHQQ- 83
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndlTLFGRR----RGSGETIWDIKKHIgyvSSSLHLDy 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 84 ----TLLDALLA----------RLPEAEREssawRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLLL 149
Cdd:PRK10938 350 rvstSVRNVILSgffdsigiyqAVSDRQQK----LAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLIL 425
|
170 180 190
....*....|....*....|....*....|....*
gi 495164891 150 DEPGNHLD-LPTML---WLEQFLARWNGSFILVSH 180
Cdd:PRK10938 426 DEPLQGLDpLNRQLvrrFVDVLISEGETQLLFVSH 460
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
320-470 |
2.60e-04 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 42.71 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLL--------WRQWQTGETVPGVTFHPRvSLGYYDQSlHQLPDNATLLE--------- 382
Cdd:cd03296 25 IPSGELVALLGPSGSGKTTLLRLIaglerpdsGTILFGGEDATDVPVQER-NVGFVFQH-YALFRHMTVFDnvafglrvk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 383 --ALEPFAPELQQRKLALIS-AGFPWarHGQRVDT-LSGGERSRllfvgLSLARY-----SLLMLDEPTNHLDMEGKEAL 453
Cdd:cd03296 103 prSERPPEAEIRAKVHELLKlVQLDW--LADRYPAqLSGGQRQR-----VALARAlavepKVLLLDEPFGALDAKVRKEL 175
|
170 180
....*....|....*....|.
gi 495164891 454 AQTLQTFEGGL----LLVTHD 470
Cdd:cd03296 176 RRWLRRLHDELhvttVFVTHD 196
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
307-463 |
2.75e-04 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 42.91 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 307 PDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLWRQW--QTGE-TVPGV---TFHP---RVSLGYYDQSlhqlPD- 376
Cdd:cd03249 14 PDVPILKGLSL-TIPPGKTVALVGSSGCGKSTVVSLLERFYdpTSGEiLLDGVdirDLNLrwlRSQIGLVSQE----PVl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 377 -NATLLEALEPFAPELQQR------KLALIS---AGFPWARH---GQRVDTLSGGERSRllfvgLSLARY-----SLLML 438
Cdd:cd03249 89 fDGTIAENIRYGKPDATDEeveeaaKKANIHdfiMSLPDGYDtlvGERGSQLSGGQKQR-----IAIARAllrnpKILLL 163
|
170 180
....*....|....*....|....*
gi 495164891 439 DEPTNHLDMEGKEALAQTLQTFEGG 463
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMKG 188
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
126-200 |
3.15e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 126 LSGGQHTRLLLARALIISPDLLLLDEPGNHLD-------LPTMLWLEQflaRWNGSFILVSHDSALLDSVTNRTWILRDG 198
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqaqiIELLLELQQ---KENMALVLITHDLALVAEAAHKIIVMYAG 230
|
..
gi 495164891 199 QL 200
Cdd:PRK11022 231 QV 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
296-489 |
3.63e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 42.61 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSaapdtPTLftLPL-ARLKSGDRVALLGHNGCGKSSLL-----------------RLLwRQWQTGE------ 351
Cdd:PRK03695 1 MQLNDVAVS-----TRL--GPLsAEVRAGEILHLVGPNGAGKSTLLarmagllpgsgsiqfagQPL-EAWSAAElarhra 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 352 ----------TVPgvTFHprvslgYYDQSLHQLPDNATLLEALEPFAPELQ-QRKLAlisagfpwaRHgqrVDTLSGGE- 419
Cdd:PRK03695 73 ylsqqqtppfAMP--VFQ------YLTLHQPDKTRTEAVASALNEVAEALGlDDKLG---------RS---VNQLSGGEw 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 420 -RSRLLFVGLSLARYS-----LLMLDEPTNHLDMEGKEALAQTLQTFE---GGLLLVTHD--RTLMEAscNRFWLVEDGG 488
Cdd:PRK03695 133 qRVRLAAVVLQVWPDInpagqLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHDlnHTLRHA--DRVWLLKQGK 210
|
.
gi 495164891 489 L 489
Cdd:PRK03695 211 L 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
296-469 |
3.66e-04 |
|
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: 42.09 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAapDTPTLFTLPLARLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVP--GVTFHPRVSLGYYDQSLHQ 373
Cdd:cd03231 1 LEADELTCER--DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRIL-----AGLSPPlaGRVLLNGGPLDFQRDSIAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 374 -------LPDNATLLEALEP---FAP--ELQQRKLALISAGFPWARHgQRVDTLSGGERSRLLFVGLSLARYSLLMLDEP 441
Cdd:cd03231 74 gllylghAPGIKTTLSVLENlrfWHAdhSDEQVEEALARVGLNGFED-RPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|.
gi 495164891 442 TNHLDMEGKEALAQTL--QTFEGGL-LLVTH 469
Cdd:cd03231 153 TTALDKAGVARFAEAMagHCARGGMvVLTTH 183
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
309-447 |
3.73e-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: 43.75 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 309 TPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVPG---------VTFHPRVS------------LGY- 366
Cdd:TIGR01271 439 TPVLKNISF-KLEKGQLLAVAGSTGSGKSSLLMMI-----MGELEPSegkikhsgrISFSPQTSwimpgtikdniiFGLs 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 367 YDQSLHQLPDNATLLEalEPFAPELQQRKLALISAGFpwarhgqrvdTLSGGERSRllfVGLSLARYS---LLMLDEPTN 443
Cdd:TIGR01271 513 YDEYRYTSVIKACQLE--EDIALFPEKDKTVLGEGGI----------TLSGGQRAR---ISLARAVYKdadLYLLDSPFT 577
|
....
gi 495164891 444 HLDM 447
Cdd:TIGR01271 578 HLDV 581
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
296-505 |
3.74e-04 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 42.91 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 296 LELENLAVSAApDTPTLFTLPLaRLKSGDRVALLGHNGCGKSSLLRLLWRQWQTGE---TVPGVTFHPRvSLGYYDQSLH 372
Cdd:PRK09536 4 IDVSDLSVEFG-DTTVLDGVDL-SVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAgtvLVAGDDVEAL-SARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 373 QLPDNATL---------LEA-----LEPFAPELQQRKLALISAgfpWARHG------QRVDTLSGGERSRLLfVGLSLAR 432
Cdd:PRK09536 81 SVPQDTSLsfefdvrqvVEMgrtphRSRFDTWTETDRAAVERA---MERTGvaqfadRPVTSLSGGERQRVL-LARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 433 YS-LLMLDEPTNHLDMEGKE---ALAQTLQTFEGGLLLVTHDRTLMEASCNRFWLVEDGGLSEWHNMEALLA--RLRAA 505
Cdd:PRK09536 157 ATpVLLLDEPTASLDINHQVrtlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTadTLRAA 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
319-487 |
4.60e-04 |
|
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: 41.97 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRL---LWRQWQTGETVPGVTFH--------------------PRVS----LGYYdQSL 371
Cdd:cd03266 27 TVKPGEVTGLLGPNGAGKTTTLRMlagLLEPDAGFATVDGFDVVkepaearrrlgfvsdstglyDRLTarenLEYF-AGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 372 HQL-PDNATllEALEPFAPELQQRKLAlisagfpwarhGQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGK 450
Cdd:cd03266 106 YGLkGDELT--ARLEELADRLGMEELL-----------DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495164891 451 EALAQTLQTF-EGG--LLLVTHDRTLMEASCNRFWLVEDG 487
Cdd:cd03266 173 RALREFIRQLrALGkcILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
397-477 |
4.66e-04 |
|
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: 41.19 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 397 ALISAGFPWARHGqrvdtLSGGERSR----LLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQTFEGG---LLLVTH 469
Cdd:cd03227 65 AAVSAELIFTRLQ-----LSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgaqVIVITH 139
|
....*...
gi 495164891 470 DRTLMEAS 477
Cdd:cd03227 140 LPELAELA 147
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
320-496 |
4.70e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 41.78 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLW--------RQWQTGETVP-----GVTFHPRvSLGYYDQSLHQLPDNATLLEALEP 386
Cdd:PRK10908 25 MRPGEMAFLTGHSGAGKSTLLKLICgierpsagKIWFSGHDITrlknrEVPFLRR-QIGMIFQDHHLLMDRTVYDNVAIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 387 F------APELQQR------KLALI--SAGFPWarhgqrvdTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEA 452
Cdd:PRK10908 104 LiiagasGDDIRRRvsaaldKVGLLdkAKNFPI--------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 495164891 453 LAQTLQTFEG---GLLLVTHDRTLMEASCNRFWLVEDGGLSEWHNME 496
Cdd:PRK10908 176 ILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-469 |
6.17e-04 |
|
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: 40.87 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGetvpgvtfhprvslgyydqsLHQlPDNATLLEALEPFAP----ELQQR 394
Cdd:cd03216 22 SVRRGEVHALLGENGAGKSTLMKIL-----SG--------------------LYK-PDSGEILVDGKEVSFasprDARRA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 395 KLALISagfpwarhgQrvdtLSGGERSRLLfVGLSLARYS-LLMLDEPTNHLDMEGKEALAQTLQTF--EG-GLLLVTH 469
Cdd:cd03216 76 GIAMVY---------Q----LSVGERQMVE-IARALARNArLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISH 140
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
125-157 |
6.45e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 6.45e-04
10 20 30
....*....|....*....|....*....|...
gi 495164891 125 SLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
320-501 |
7.94e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 41.64 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLL--WRQWQTGETV-------PGVTFHPRVSLGYydqsLHQLPDN----ATLLE---- 382
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIdgLLEAESGQIIidgdlltEENVWDIRHKIGM----VFQNPDNqfvgATVEDdvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 383 ALEPFAPELQQRK------LALISAGFPWARHGQRvdtLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQT 456
Cdd:PRK13650 106 GLENKGIPHEEMKervneaLELVGMQDFKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495164891 457 LQT----FEGGLLLVTHDrtLME-ASCNRFWLVEDGGLSEWHNMEALLAR 501
Cdd:PRK13650 183 IKGirddYQMTVISITHD--LDEvALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
320-446 |
9.56e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.96 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 320 LKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVPGVTFHPRVSL--------------GYYDQSLHQLPdNATLLEALE 385
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNAL-----AFRSPKGVKGSGSVLLngmpidakemraisAYVQQDDLFIP-TLTVREHLM 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495164891 386 pFAPEL-----------QQRKLALISA-GFPWARH-----GQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLD 446
Cdd:TIGR00955 122 -FQAHLrmprrvtkkekRERVDEVLQAlGLRKCANtrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
323-480 |
1.08e-03 |
|
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: 40.88 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 323 GDRVALLGHNGCGKSSLLRLLwrqwqTGETVP-------------GVTFHPRVSLGyydqsL---HQLP---DNATLLEA 383
Cdd:cd03219 26 GEIHGLIGPNGAGKTTLFNLI-----SGFLRPtsgsvlfdgeditGLPPHEIARLG-----IgrtFQIPrlfPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 384 LEpfAPELQQRKLALISAGFP-------------------WARHGQRVDTLSGGERsRLLFVGLSLA-RYSLLMLDEPTN 443
Cdd:cd03219 96 VM--VAAQARTGSGLLLARARreereareraeellervglADLADRPAGELSYGQQ-RRLEIARALAtDPKLLLLDEPAA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 495164891 444 HLDMEGKEALAQTLQTF-EGGL--LLVTHDRTLMEASCNR 480
Cdd:cd03219 173 GLNPEETEELAELIRELrERGItvLLVEHDMDVVMSLADR 212
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
412-470 |
1.19e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 1.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 412 VDTLSGGERSRllfvgLSLARYSLLMLDepTNHLDMEGKEALAQTLQTfeggLLLVTHD 470
Cdd:COG0419 156 IETLSGGERLR-----LALADLLSLILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
319-469 |
1.49e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 40.24 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 319 RLKSGDRVALLGHNGCGKSSLLRLLwrqwqTGETVPgvtFHPRVSLGYYDQSL-----------HQ--LPDNATLLEALE 385
Cdd:PRK13539 24 TLAAGEALVLTGPNGSGKTTLLRLI-----AGLLPP---AAGTIKLDGGDIDDpdvaeachylgHRnaMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 386 PFAPELQQRKLALISA----GFPWARHgQRVDTLSGGERSRLLFVGLSLARYSLLMLDEPTNHLDMEGKEALAQTLQTF- 460
Cdd:PRK13539 96 FWAAFLGGEELDIAAAleavGLAPLAH-LPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHl 174
|
170
....*....|.
gi 495164891 461 -EGGL-LLVTH 469
Cdd:PRK13539 175 aQGGIvIAATH 185
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-157 |
1.68e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 39.94 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGV--------------VTRAARCLLARVEQ--HLPDELH 81
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVegdihyngipykefAEKYPGEIIYVSEEdvHFPTLTV 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 82 QQTLLDALLARLPEAERessawraqallanmgfaeaawsltagSLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:cd03233 101 RETLDFALRCKGNEFVR--------------------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
379-458 |
1.88e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 379 TLLEALEPFAPELQ-QRKL-ALISAGFPWARHGQRVDTLSGGERSRllfvgLSLARY--------SLLMLDEPTNHLDME 448
Cdd:TIGR00630 792 TVEEAYEFFEAVPSiSRKLqTLCDVGLGYIRLGQPATTLSGGEAQR-----IKLAKElskrstgrTLYILDEPTTGLHFD 866
|
90
....*....|
gi 495164891 449 GKEALAQTLQ 458
Cdd:TIGR00630 867 DIKKLLEVLQ 876
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
327-447 |
2.06e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 40.07 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 327 ALLGHNGCGKSSLL----RLLWRQwqTGE-TVPGV---------------------TFHPR------VSLGYY------- 367
Cdd:COG4604 31 ALIGPNGAGKSTLLsmisRLLPPD--SGEvLVDGLdvattpsrelakrlailrqenHINSRltvrelVAFGRFpyskgrl 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 368 --------DQSLHQLpdnatlleALEPfapeLQQRKLalisagfpwarhgqrvDTLSGGERSRLlFVGLSLA---RYslL 436
Cdd:COG4604 109 taedreiiDEAIAYL--------DLED----LADRYL----------------DELSGGQRQRA-FIAMVLAqdtDY--V 157
|
170
....*....|.
gi 495164891 437 MLDEPTNHLDM 447
Cdd:COG4604 158 LLDEPLNNLDM 168
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
125-157 |
2.49e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 40.40 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|...
gi 495164891 125 SLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PRK11000 133 ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-199 |
3.22e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 4 LLTAHSLRID--SPFGP--ELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEGVVTRAARC----LLA----- 70
Cdd:PRK15093 3 LLDIRNLTIEfkTSDGWvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFddidLLRlspre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 71 --RVEQHLPDELHQ--QTLLD-------ALLARLPEAERESSAW--------RAQALLANMGFAE--AAWSLTAGSLSGG 129
Cdd:PRK15093 83 rrKLVGHNVSMIFQepQSCLDpservgrQLMQNIPGWTYKGRWWqrfgwrkrRAIELLHRVGIKDhkDAMRSFPYELTEG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495164891 130 QHTRLLLARALIISPDLLLLDEPGNHLDLPTMLWLEQFLARWN----GSFILVSHDSALLDSVTNRTWILRDGQ 199
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqnnnTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-204 |
3.89e-03 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 39.45 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKAL------DGTLA---------------PAEGVVTRAA-------RCLLAR 71
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFlrllntEGDIQidgvswnsvplqkwrKAFGVIPQKVfifsgtfRKNLDP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 72 VEQHLPDEL---HQQTLLDALLARLPEaeressawRAQALLANMGFAeaawsltagsLSGGQHTRLLLARALIISPDLLL 148
Cdd:cd03289 100 YGKWSDEEIwkvAEEVGLKSVIEQFPG--------QLDFVLVDGGCV----------LSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495164891 149 LDEPGNHLDLPTMLWLEQFL--ARWNGSFILVSHD-SALLDsvTNRTWILRDGQLQAFD 204
Cdd:cd03289 162 LDEPSAHLDPITYQVIRKTLkqAFADCTVILSEHRiEAMLE--CQRFLVIEENKVRQYD 218
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
379-459 |
4.19e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 379 TLLEALEPFA--PELQQRKLALISAGFPWARHGQRVDTLSGGERSRllfVGLS--LARYS----LLMLDEPTNHLDMEGK 450
Cdd:cd03271 132 TVEEALEFFEniPKIARKLQTLCDVGLGYIKLGQPATTLSGGEAQR---IKLAkeLSKRStgktLYILDEPTTGLHFHDV 208
|
....*....
gi 495164891 451 EALAQTLQT 459
Cdd:cd03271 209 KKLLEVLQR 217
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
121-186 |
4.31e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 4.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495164891 121 LTAGSLSGGqhTRLLLARALII-----SPDLLLLDEPGNHLDlPTML-----WLEQfLARWNGSFILVSHDSALLD 186
Cdd:pfam13304 232 LPAFELSDG--TKRLLALLAALlsalpKGGLLLIDEPESGLH-PKLLrrlleLLKE-LSRNGAQLILTTHSPLLLD 303
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-157 |
5.17e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.09 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 20 LNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLapAEGVVTRAARCLLAR------------VEQ---HLPdelhQQT 84
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRpldssfqrsigyVQQqdlHLP----TST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 85 LLDALL--ARL------PEAERESSAWRAQALLANMGFAEAAWSLTAGSLSGGQHTRLLLARALIISPDLLL-LDEPGNH 155
Cdd:TIGR00956 853 VRESLRfsAYLrqpksvSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
..
gi 495164891 156 LD 157
Cdd:TIGR00956 933 LD 934
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-157 |
6.28e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 18 PELNALSFTLKKGDRIGLIGHNGCGKSTLLKALDGTLAPAEG--VVTRAArclLARVEQhlPDELHQQTLLDALLARLP- 94
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDasVVIRGT---VAYVPQ--VSWIFNATVRDNILFGSPf 705
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495164891 95 EAERESSAWRAQALLANMgfaeaawSLTAG-----------SLSGGQHTRLLLARALIISPDLLLLDEPGNHLD 157
Cdd:PLN03130 706 DPERYERAIDVTALQHDL-------DLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
410-508 |
7.53e-03 |
|
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: 38.93 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164891 410 QRVDTLSGGERSRllfVGLS---LARYSLLMLDEPTNHLDMEGK-------EALAQTLQTfegGLLLVTHDRTLMEASCN 479
Cdd:COG4148 129 RRPATLSGGERQR---VAIGralLSSPRLLLMDEPLAALDLARKaeilpylERLRDELDI---PILYVSHSLDEVARLAD 202
|
90 100
....*....|....*....|....*....
gi 495164891 480 RFWLVEDGGLSEWHNMEALLARLRAAPTQ 508
Cdd:COG4148 203 HVVLLEQGRVVASGPLAEVLSRPDLLPLA 231
|
|
| |
