|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-541 |
4.99e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 148.00 E-value: 4.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 3 KILKSEIASSRGKLTLGLVLLISLALSASAVYaeVFVQRMINGVTVPGSANVLhnfYIYLALGLILLAGRTVFSAFSYVV 82
Cdd:COG1132 10 RRLLRYLRPYRGLLILALLLLLLSALLELLLP--LLLGRIIDALLAGGDLSAL---LLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 83 FLKMTHRV-----RKGYLNLISFgdEIRDSESFQTGDLNDRLTKDIDQCRLFCQQTLIPVWSDVIQVITIICVLFFQSVL 157
Cdd:COG1132 85 LARLAQRVvadlrRDLFEHLLRL--PLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 158 IGAAFTGYLLLSILVLRHVNTSGNDVIPKLRKREAKTADFLQDVFVNNNDVAPMQASSRVIAWFNKQYDKLLPLELHAQS 237
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 238 FIYRSWIAALVLIAFLEVTSLALGGYSFLRGVIGLGTVYMMIDYATRIQAPLESMQFHANNVQYLKGAFANLAE-LERKF 316
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFElLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 317 VMQSGNSPYPTKPtIRLHISnLRN--F----DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYS 390
Cdd:COG1132 323 EIPDPPGAVPLPP-VRGEIE-FENvsFsypgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 391 KTPISKISASEMGANVAYVSVDQSLFHVSIEKSLqGFSVNNATQN-VWQRLEQLGVSkarlDYLRTT---LSAQVGEDGA 466
Cdd:COG1132 401 GVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENI-RYGRPDATDEeVEEAAKAAQAH----EFIEALpdgYDTVVGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 467 NidkLADGdrqlllilrallqEK-------------DLIILDETLSSLDTARFAEV----SRLLRHYvdTfkikMILISH 529
Cdd:COG1132 476 N---LSGG-------------QRqriaiarallkdpPILILDEATSALDTETEALIqealERLMKGR--T----TIVIAH 533
|
570
....*....|....*
gi 491954606 530 ktnRLH---FADHVY 541
Cdd:COG1132 534 ---RLStirNADRIL 545
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
108-547 |
6.09e-31 |
|
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: 128.03 E-value: 6.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 108 ESFQTGDLNDRLtKDIDQCRLFCQQTLIPVWSDVIQVITIICVLFFQSVLIGAAFTGYLLLSILVLRHVNTSGNDVIPKL 187
Cdd:COG2274 248 ESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 188 RKREAKTADFLQDVFVNNNDVAPMQASSRVIAWFNKQYDKLLPLELHAQ--SFIYRSWIAALVLIAFLEVtsLALGGYSF 265
Cdd:COG2274 327 SEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRrlSNLLSTLSGLLQQLATVAL--LWLGAYLV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 266 LRGVIGLGTVYMMIDYATRIQAPLESMQFHANNVQYLKGAFANLAELERKFVMQSGNSPYPTKPTIRLHISnLRN--F-- 341
Cdd:COG2274 405 IDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIE-LENvsFry 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 ---DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHV 418
Cdd:COG2274 484 pgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSG 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 419 SIEKSLQGFSVNNATQNVWQRLEQLGVskarLDYLRTT---LSAQVGEDGANidkLADGdrqlllilrallqEK------ 489
Cdd:COG2274 564 TIRENITLGDPDATDEEIIEAARLAGL----HDFIEALpmgYDTVVGEGGSN---LSGG-------------QRqrlaia 623
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 490 -------DLIILDETLSSLDTARFAEVSRLLRHYvdTFKIKMILISHKTNRLHFADHVYGITKGE 547
Cdd:COG2274 624 rallrnpRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLADRIIVLDKGR 686
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
244-541 |
1.60e-22 |
|
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: 101.37 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 244 IAALVLIAFLevtSLALG----GYSFLRGVIGLGTVYMMIDYATRIQAPLESM--QFHA--NNVqylkGAFANLAEL--E 313
Cdd:COG4988 245 SAVLEFFASL---SIALVavyiGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLgsFYHAraNGI----AAAEKIFALldA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 314 RKFVMQSGNSPYPTKPTIRLHISNLrNF----DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDY 389
Cdd:COG4988 318 PEPAAPAGTAPLPAAGPPSIELEDV-SFsypgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 390 SKTPISKISASEMGANVAYVSVDQSLFHVSIEKSLqGFSVNNATQN-VWQRLEQLGVSkARLDYLRTTLSAQVGEDGANI 468
Cdd:COG4988 397 NGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL-RLGRPDASDEeLEAALEAAGLD-EFVAALPDGLDTPLGEGGRGL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 469 DK------------LADgdrqlllilrallqeKDLIILDETLSSLDTARFAEVSRLLRHYVDTfKIkMILISHKTNRLHF 536
Cdd:COG4988 475 SGgqaqrlalaralLRD---------------APLLLLDEPTAHLDAETEAEILQALRRLAKG-RT-VILITHRLALLAQ 537
|
....*
gi 491954606 537 ADHVY 541
Cdd:COG4988 538 ADRIL 542
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
110-549 |
6.81e-21 |
|
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: 96.37 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 110 FQTGDLNDRLTKDIDQCRLFCQQTLIPVWSDVIQVITIICVLFFQSVLIGAAFTGYLLLSILVL-----RHVNTSGNDVI 184
Cdd:COG4987 109 LRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGLLLpllaaRLGRRAGRRLA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 185 PKLRKREAKTADFLQdvfvNNNDVAPMQASSRVIAWFNKQYDKLLPLELHAQSF-IYRSWIAALVLIAFLeVTSLALGGY 263
Cdd:COG4987 189 AARAALRARLTDLLQ----GAAELAAYGALDRALARLDAAEARLAAAQRRLARLsALAQALLQLAAGLAV-VAVLWLAAP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 264 SFLRGVIG---LGTVYMMIdyatriQAPLESMQFHANNVQYL---KGAFANLAEL-ERKFVMQSGNSPYPTKPTIRLHIS 336
Cdd:COG4987 264 LVAAGALSgplLALLVLAA------LALFEALAPLPAAAQHLgrvRAAARRLNELlDAPPAVTEPAEPAPAPGGPSLELE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 337 NLR----NFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVD 412
Cdd:COG4987 338 DVSfrypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 413 QSLFHVSIEKSLQgFSVNNATQN-VWQRLEQLGVSKArLDYLRTTLSAQVGEDGANIDK------------LADgdrqll 479
Cdd:COG4987 418 PHLFDTTLRENLR-LARPDATDEeLWAALERVGLGDW-LAALPDGLDTWLGEGGRRLSGgerrrlalaralLRD------ 489
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491954606 480 lilrallqeKDLIILDETLSSLD--TARfaevsRLLRHYVDTFKIK-MILISHKTNRLHFADHVYGITKGECV 549
Cdd:COG4987 490 ---------APILLLDEPTEGLDaaTEQ-----ALLADLLEALAGRtVLLITHRLAGLERMDRILVLEDGRIV 548
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
333-541 |
8.11e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 91.79 E-value: 8.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNL------RNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANV 406
Cdd:COG1124 2 LEVRNLsvsygqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 407 AYV------------SVDQSLfhvsiEKSLQGFSVNNATQNVWQRLEQLGVSKARLDYLRTTLSaqvgeDG--------- 465
Cdd:COG1124 82 QMVfqdpyaslhprhTVDRIL-----AEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLS-----GGqrqrvaiar 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 466 AnidkLAdgdrqlllilrallQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRL-HFADHVY 541
Cdd:COG1124 152 A----LI--------------LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVaHLCDRVA 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
333-549 |
1.30e-18 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 84.86 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNL------RNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEM---G 403
Cdd:cd03257 2 LEVKNLsvsfptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 404 ANVAYVSVD--QSL-FHVSIEKSL-QGFSVNNATQNVWQR-------LEQLGVSKARLDYLRTTLSaqvgedG-----AN 467
Cdd:cd03257 82 KEIQMVFQDpmSSLnPRMTIGEQIaEPLRIHGKLSKKEARkeavlllLVGVGLPEEVLNRYPHELS------GgqrqrVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 468 I-DKLAdgdrqlllilrallQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISH--KTNRlHFADHVYGIT 544
Cdd:cd03257 156 IaRALA--------------LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHdlGVVA-KIADRVAVMY 220
|
....*
gi 491954606 545 KGECV 549
Cdd:cd03257 221 AGKIV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-549 |
2.10e-18 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 88.42 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNL----RNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGL---QHQYEGQIDYSKTPISKISASEMGAN 405
Cdd:COG1123 5 LEVRDLsvryPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 406 VAYV--SVDQSLFHVSIEK------SLQGFSVNNATQNVWQRLEQLGVSKARLDYlrttlsaqvgedganIDKLADGDRQ 477
Cdd:COG1123 85 IGMVfqDPMTQLNPVTVGDqiaealENLGLSRAEARARVLELLEAVGLERRLDRY---------------PHQLSGGQRQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491954606 478 LLLILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNR-LHFADHVYGITKGECV 549
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIV 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
335-547 |
2.40e-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: 83.67 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 335 ISNLR----NFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYV- 409
Cdd:cd03225 2 LKNLSfsypDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 410 -SVDQSLFHVSIEKSLqGFSvnnatqnvwqrLEQLGVSKARLDYLRTTLSAQVGEDG---ANIDKLADGdrqlllilral 485
Cdd:cd03225 82 qNPDDQFFGPTVEEEV-AFG-----------LENLGLPEEEIEERVEEALELVGLEGlrdRSPFTLSGG----------- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491954606 486 lqEK-------------DLIILDETLSSLDTARFAEVSRLLRHYVDTfKIKMILISHKTNRL-HFADHVYGITKGE 547
Cdd:cd03225 139 --QKqrvaiagvlamdpDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
333-547 |
8.68e-18 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 82.17 E-value: 8.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNL--RNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVS 410
Cdd:COG4619 1 LELEGLsfRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 411 VDQSLFHVSIE------KSLQGFSVNNATQNVWqrLEQLGVSKARLDYLRTTLSaqVGEdganidK--------LAdgdr 476
Cdd:COG4619 81 QEPALWGGTVRdnlpfpFQLRERKFDRERALEL--LERLGLPPDILDKPVERLS--GGE------RqrlaliraLL---- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 477 qlllilrallQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTN-RLHFADHVYGITKGE 547
Cdd:COG4619 147 ----------LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEqIERVADRVLTLEAGR 208
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
342-547 |
1.09e-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: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIE 421
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 kslqgfsvnnatQNV-----WQRLeqlgvSKARLdYLRttlsaqvgedganidkladgdrqlllilrallqEKDLIILDE 496
Cdd:cd03228 94 ------------ENIlsggqRQRI-----AIARA-LLR---------------------------------DPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491954606 497 TLSSLDTARFAEVSRLLRHYVDtfKIKMILISHKTNRLHFADHVYGITKGE 547
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
340-549 |
4.15e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 77.63 E-value: 4.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 340 NFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVS 419
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 420 IEKSLQGFSVNNATQNVWQRLEQLGVSkarlDYLRTT---LSAQVGEDGANidkLADGDRQLLLILRALLQEKDLIILDE 496
Cdd:cd03245 94 LRDNITLGAPLADDERILRAAELAGVT----DFVNKHpngLDLQIGERGRG---LSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 497 TLSSLDT---ARFAE-VSRLLRHyvDTfkikMILISHKTNRLHFADHVYGITKGECV 549
Cdd:cd03245 167 PTSAMDMnseERLKErLRQLLGD--KT----LIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-549 |
5.98e-16 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 80.72 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISAS---EMGANVAYV--SVDQSLF 416
Cdd:COG1123 277 GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVfqDPYSSLN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 417 -HVSIEKSL-------QGFSVNNATQNVWQRLEQLGVSKARLDYLRTTLS---------AQVgedganidkLAdgdrqll 479
Cdd:COG1123 357 pRMTVGDIIaeplrlhGLLSRAERRERVAELLERVGLPPDLADRYPHELSggqrqrvaiARA---------LA------- 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491954606 480 lilrallQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHktnRL----HFADHVYGITKGECV 549
Cdd:COG1123 421 -------LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH---DLavvrYIADRVAVMYDGRIV 484
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
342-551 |
9.38e-16 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 75.55 E-value: 9.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSvdqslfhvsie 421
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 kslqgfsvnnatqnvwQRLEQLGvskarLDYLR----TTLS---------AQVgedganidkLAdgdrqlllilrallQE 488
Cdd:cd03214 80 ----------------QALELLG-----LAHLAdrpfNELSggerqrvllARA---------LA--------------QE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491954606 489 KDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNR-LHFADHVYGITKGECVYF 551
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLaARYADRVILLKDGRIVAQ 179
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
342-550 |
1.03e-15 |
|
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: 76.60 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYV--SVDQSLFHVS 419
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVfqNPDDQLFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 420 IEKSLqGFSvnnatqnvwqrLEQLGVSKARLD-YLRTTLsAQVGedganIDKLAD--------GdrqlllilrallqEK- 489
Cdd:COG1122 93 VEEDV-AFG-----------PENLGLPREEIReRVEEAL-ELVG-----LEHLADrpphelsgG-------------QKq 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491954606 490 ------------DLIILDETLSSLDTARFAEVSRLLRHYVDTfKIKMILISHKTNRL-HFADHVYGITKGECVY 550
Cdd:COG1122 142 rvaiagvlamepEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVaELADRVIVLDDGRIVA 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
346-458 |
3.91e-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: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLF-------HV 418
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFprltvreNL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 491954606 419 SIEKSLQGFSVNNATQNVWQRLEQLGVS---KARLDYLRTTLS 458
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGdlaDRPVGERPGTLS 123
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
343-529 |
5.43e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.11 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 343 HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGAnvayvsvdqslFHVSIEK 422
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA-----------FRRDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 423 SLQ-GFSVNNATQNVWQRLEQ-----LGVSKARLDYLRTTLSAQVGEDGANIDK----LADGDRQLLLILRALLQEKDLI 492
Cdd:PRK10419 94 VFQdSISAVNPRKTVREIIREplrhlLSLDKAERLARASEMLRAVDLDDSVLDKrppqLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 491954606 493 ILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISH 529
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
110-529 |
6.15e-15 |
|
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: 77.40 E-value: 6.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 110 FQTGDLNDRLTKDIDQCRLFCQQTLIPVWSDVIQVITIICVLFFQSVLIGAAFTGYLLLSILV-----LRHVNTSGNDVI 184
Cdd:TIGR02868 107 LRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVaplvsLRAARAAEQALA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 185 PKLRKREAKTADFLQDVfvnnndvAPMQASSR---VIAWFNKQYDKLLPLELHAQSFiyRSWIAAL-VLIAFLEVTS-LA 259
Cdd:TIGR02868 187 RLRGELAAQLTDALDGA-------AELVASGAlpaALAQVEEADRELTRAERRAAAA--TALGAALtLLAAGLAVLGaLW 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 260 LGGYSFLRGVIG---LGTVYMMIDYATRIQAPLesmqfhANNVQYL---KGAFANLAELER-KFVMQSGNSP-----YPT 327
Cdd:TIGR02868 258 AGGPAVADGRLApvtLAVLVLLPLAAFEAFAAL------PAAAQQLtrvRAAAERIVEVLDaAGPVAEGSAPaagavGLG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 328 KPTIRL-HISNLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANV 406
Cdd:TIGR02868 332 KPTLELrDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 407 AYVSVDQSLFHVSIEKSLQgFSVNNAT-QNVWQRLEQLGVskarLDYLRTT---LSAQVGEDGAnidKLADGDRQLLLIL 482
Cdd:TIGR02868 412 SVCAQDAHLFDTTVRENLR-LARPDATdEELWAALERVGL----ADWLRALpdgLDTVLGEGGA---RLSGGERQRLALA 483
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 491954606 483 RALLQEKDLIILDETLSSLDTARFAEVSRLLRHyVDTFKIKmILISH 529
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTV-VLITH 528
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
332-547 |
1.88e-14 |
|
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: 71.12 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 332 RLHISNLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVsv 411
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 412 dqslFHVSiekslQGfsvnnatqnvwQRleqlgvskarldyLRTTLSAQVgedganidkladgdrqlllilralLQEKDL 491
Cdd:cd00267 79 ----PQLS-----GG-----------QR-------------QRVALARAL------------------------LLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 492 IILDETLSSLDTARFAEVSRLLRHYVDTFKIkMILISHKTNRL-HFADHVYGITKGE 547
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
332-540 |
1.90e-14 |
|
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: 72.13 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 332 RLHISNL---RNfDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKiSASEMGANVAY 408
Cdd:COG4133 2 MLEAENLscrRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 409 V----------SVDQSL-FHVsiekSLQGFSVNNATqnVWQRLEQLGVSKARLDYLRtTLSA----QVgedganidKLAd 473
Cdd:COG4133 80 LghadglkpelTVRENLrFWA----ALYGLRADREA--IDEALEAVGLAGLADLPVR-QLSAgqkrRV--------ALA- 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491954606 474 gdrqlllilRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDtfKIKMILI-SHKTNRLHFADHV 540
Cdd:COG4133 144 ---------RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLA--RGGAVLLtTHQPLELAAARVL 200
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
332-551 |
4.20e-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: 72.38 E-value: 4.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 332 RLHISNLRnF---DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAY 408
Cdd:COG1120 1 MLEAENLS-VgygGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 409 VSVDQSL-FHVSIE-----------KSLQGFSVNNATQnVWQRLEQLGVSKARLDYLrTTLS---------AQVgedgan 467
Cdd:COG1120 80 VPQEPPApFGLTVRelvalgryphlGLFGRPSAEDREA-VEEALERTGLEHLADRPV-DELSggerqrvliARA------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 468 idkLAdgdrqlllilrallQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNR-LHFADHVYGITKG 546
Cdd:COG1120 152 ---LA--------------QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLaARYADRLVLLKDG 214
|
....*
gi 491954606 547 ECVYF 551
Cdd:COG1120 215 RIVAQ 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
345-420 |
9.67e-13 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 66.47 E-value: 9.67e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSI 420
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSI 92
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
245-540 |
1.32e-12 |
|
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: 70.39 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 245 AALVLIAFLEVTSLALggysflrgVIGLGTVYMMIDYAT---------RIQAPLE--SMQFHANnvQYLKGAFANLAE-L 312
Cdd:TIGR02857 232 AVLELFATLSVALVAV--------YIGFRLLAGDLDLATglfvlllapEFYLPLRqlGAQYHAR--ADGVAAAEALFAvL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 313 ERKFVMQSGNSPYPTKPTIRLHISNLrNFDH----QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQID 388
Cdd:TIGR02857 302 DAAPRPLAGKAPVTAAPASSLEFSGV-SVAYpgrrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 389 YSKTPISKISASEMGANVAYVSVDQSLFHVSIEKSLQgFSVNNATQNVWQR-LEQLGVSKArLDYLRTTLSAQVGEDGAn 467
Cdd:TIGR02857 381 VNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIR-LARPDASDAEIREaLERAGLDEF-VAALPQGLDTPIGEGGA- 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491954606 468 idKLADGDRQLLLILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIkmILISHKTNRLHFADHV 540
Cdd:TIGR02857 458 --GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTV--LLVTHRLALAALADRI 526
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
342-546 |
1.54e-12 |
|
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: 66.79 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKisaseMGANVAYV----SVDQSlFH 417
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVpqrrSIDRD-FP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 418 VSIEK----SLQGFSV--NNATQNVWQR----LEQLGVSKARlDYLRTTLS---------AQVgedganidkLAdgdrql 478
Cdd:cd03235 85 ISVRDvvlmGLYGHKGlfRRLSKADKAKvdeaLERVGLSELA-DRQIGELSggqqqrvllARA---------LV------ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491954606 479 llilrallQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTfKIKMILISHKTNRLH-FADHVYGITKG 546
Cdd:cd03235 149 --------QDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLeYFDRVLLLNRT 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
342-549 |
2.59e-12 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 66.48 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIE 421
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 KSLQgFSVNNATQNVWQRLEQLgvskARLDYLRTTL----SAQVGEDGANidkLADGDRQLLLILRALLQEKDLIILDET 497
Cdd:cd03254 95 ENIR-LGRPNATDEEVIEAAKE----AGAHDFIMKLpngyDTVLGENGGN---LSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 498 LSSLDT---ARFAEVSRLLRHYVDTfkikmILISHKTNRLHFADHVYGITKGECV 549
Cdd:cd03254 167 TSNIDTeteKLIQEALEKLMKGRTS-----IIIAHRLSTIKNADKILVLDDGKII 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
335-529 |
3.91e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.80 E-value: 3.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 335 ISNL-RNFDH-QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMgaNVAYVSVD 412
Cdd:PRK10851 5 IANIkKSFGRtQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR--KVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 413 QSLF-HVSIEKSLQ-GFSV-------NNAT--QNVWQRLEQLgvskaRLDYLRTTLSAQvgedganidkLADGDRQLLLI 481
Cdd:PRK10851 83 YALFrHMTVFDNIAfGLTVlprrerpNAAAikAKVTQLLEMV-----QLAHLADRYPAQ----------LSGGQKQRVAL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491954606 482 LRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISH 529
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTH 195
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-546 |
1.44e-11 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 64.73 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKisaseMGANVAYV----SVDQSlFH 417
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYVpqraEVDWD-FP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 418 VSIE----------KSLQGFSVNNATQNVWQRLEQLGVSkarlDYLRT---TLS---------AQVgedganidkLAdgd 475
Cdd:COG1121 92 ITVRdvvlmgrygrRGLFRRPSRADREAVDEALERVGLE----DLADRpigELSggqqqrvllARA---------LA--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 476 rqlllilrallQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIkMILISHKTNRL-HFADHVYGITKG 546
Cdd:COG1121 156 -----------QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKT-ILVVTHDLGAVrEYFDRVLLLNRG 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
333-546 |
1.59e-11 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 64.08 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNL-RNF-DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEmgANVAYVS 410
Cdd:cd03259 1 LELKGLsKTYgSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 411 VDQSLF-HVSIEK------SLQGFSVNNATQNVWQRLEQLGVSkARLDYLRTTLS---AQ-VGedganidkLADGdrqll 479
Cdd:cd03259 79 QDYALFpHLTVAEniafglKLRGVPKAEIRARVRELLELVGLE-GLLNRYPHELSggqQQrVA--------LARA----- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491954606 480 lilraLLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISH-KTNRLHFADHVYGITKG 546
Cdd:cd03259 145 -----LAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHdQEEALALADRIAVMNEG 207
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
325-547 |
2.05e-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: 64.03 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 325 YPTKPtirlhisnlrnfDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGA 404
Cdd:cd03248 21 YPTRP------------DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 405 NVAYVSVDQSLFHVSIEKS----LQGFSVNNATQNVWQRLEQLGVSKARLDYlrttlSAQVGEDGAnidKLADGDRQLLL 480
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNiaygLQSCSFECVKEAAQKAHAHSFISELASGY-----DTEVGEKGS---QLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 481 ILRALLQEKDLIILDETLSSLDTARFAEVSRLlrHYVDTFKIKMILISHKTNRLHFADHVYGITKGE 547
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQA--LYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
332-540 |
3.35e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.83 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 332 RLHISNL--RNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYV 409
Cdd:PRK10619 5 KLNVIDLhkRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 410 SVDQSLfHVSIEKSLQGF---SVNNATQNVWQR-LEQLGVSKARLDYLRTTLSAQVGEDGANIDK----LADGDRQLLLI 481
Cdd:PRK10619 85 NQLRLL-RTRLTMVFQHFnlwSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKypvhLSGGQQQRVSI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491954606 482 LRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKiKMILISHKtnrLHFADHV 540
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHE---MGFARHV 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
258-502 |
5.47e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.12 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 258 LALGGYSFL--RGVIGLG--TVYMMidYATRIQAPLESMQFHANNVQYLKGAFANL-AELERKFVMQSGNSPYPTKPTIr 332
Cdd:PRK10789 237 LAIGGGSWMvvNGSLTLGqlTSFVM--YLGLMIWPMLALAWMFNIVERGSAAYSRIrAMLAEAPVVKDGSEPVPEGRGE- 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHIsNLRNF-----DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIvglQHQY---EGQIDYSKTPISKISASEMGA 404
Cdd:PRK10789 314 LDV-NIRQFtypqtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI---QRHFdvsEGDIRFHDIPLTKLQLDSWRS 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 405 NVAYVSVDQSLFHVSIEKSLqGFSVNNATQnvwQRLEQLgvskARL-----DYLR--TTLSAQVGEDGAnidKLADGDRQ 477
Cdd:PRK10789 390 RLAVVSQTPFLFSDTVANNI-ALGRPDATQ---QEIEHV----ARLasvhdDILRlpQGYDTEVGERGV---MLSGGQKQ 458
|
250 260
....*....|....*....|....*
gi 491954606 478 LLLILRALLQEKDLIILDETLSSLD 502
Cdd:PRK10789 459 RISIARALLLNAEILILDDALSAVD 483
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
345-535 |
8.37e-11 |
|
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: 62.13 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEKSL 424
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 425 QGFSVNNATQnVWQRLEQLGVsKARLDYLRTTLSAQVGEDGANidkLADGdrqlllilrallqEKDL------------- 491
Cdd:cd03244 99 DPFGEYSDEE-LWQALERVGL-KEFVESLPGGLDTVVEEGGEN---LSVG-------------QRQLlclarallrkski 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491954606 492 IILDETLSSLDTARFAEVSRLLRHYvdtFK-IKMILISHktnRLH 535
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREA---FKdCTVLTIAH---RLD 199
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
326-402 |
8.45e-11 |
|
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: 62.30 E-value: 8.45e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491954606 326 PTKPTIRlhISNLRN-F-DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEM 402
Cdd:COG1127 1 MSEPMIE--VRNLTKsFgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL 77
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
333-547 |
1.06e-10 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 61.74 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNLR------NFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGA-- 404
Cdd:cd03255 1 IELKNLSktygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 405 --NVAYV----------SVDQslfHVSIEKSLQGFSVNNATQNVWQRLEQLGVsKARLDYLRTTLS-----------AQV 461
Cdd:cd03255 81 rrHIGFVfqsfnllpdlTALE---NVELPLLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSggqqqrvaiarALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 462 GedganidkladgdrqlllilrallqEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRLHFADHVY 541
Cdd:cd03255 157 N-------------------------DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRII 211
|
....*.
gi 491954606 542 GITKGE 547
Cdd:cd03255 212 ELRDGK 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
343-402 |
1.20e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.94 E-value: 1.20e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 343 HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQyEGQIDYSKTPISKISASEM 402
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRAL 357
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
339-549 |
1.54e-10 |
|
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: 61.44 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 339 RNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGA---NVAYVSvdqsl 415
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKarrRIGMIF----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 416 fhvsiekslQGF---SVNNATQNVWQRLEQLGVSKARLDYLRTTLSAQVG-EDGANI--DKLADGDRQLLLILRALLQEK 489
Cdd:cd03258 89 ---------QHFnllSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGlEDKADAypAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491954606 490 DLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTN---RLhfADHVYGITKGECV 549
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEvvkRI--CDRVAVMEKGEVV 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
342-402 |
2.06e-10 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 60.98 E-value: 2.06e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEM 402
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAEL 72
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
18-314 |
2.19e-10 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 61.80 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 18 LGLVLLISLALSASAVYAEVFVQRMINGVTVPGSANVLHNFyiyLALGLILLAGRTVFSAFSYVVFLKMTHRVRKG---- 93
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWI---ALLLLLLALLRALLSYLRRYLAARLGQRVVFDlrrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 94 -YLNLISFGdeIRDSESFQTGDLNDRLTKDIDQCRLFCQQTLIPVWSDVIQVITIICVLFFQSVLIGAAFTGYLLLSILV 172
Cdd:cd07346 78 lFRHLQRLS--LSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 173 LRHVNTSGNDVIPKLRKREAKTADFLQDVFVNNNDVAPMQASSRVIAWFNKQYDKLLPLELHAQSFIYRSWIAALVLIAF 252
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 253 LEVTSLALGGYSFLRGVIGLGTVYMMIDYATRIQAPLesMQFHANNVQYLKGafanLAELER 314
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPI--QRLANLYNQLQQA----LASLER 291
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
344-549 |
2.22e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 60.83 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGA----NVAYVSvdQSlFH-- 417
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARlrrrHIGFVF--QF-FNll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 418 --------VSIEKSLQGFSVNNATQNVWQRLEQLGVSKaRLDYLRTTLS-----------AQVGedganidkladgdrql 478
Cdd:COG1136 99 peltalenVALPLLLAGVSRKERRERARELLERVGLGD-RLDHRPSQLSggqqqrvaiarALVN---------------- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954606 479 llilrallqEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRLHFADHVYGITKGECV 549
Cdd:COG1136 162 ---------RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
344-417 |
2.61e-10 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 60.53 E-value: 2.61e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASE---MGanVAYVSVDQSLFH 417
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErarAG--IGYVPEGRRIFP 88
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
342-547 |
3.29e-10 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 59.51 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISAS--EMGANVAYVSVDQSLF-HV 418
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 419 SIEkslqgfsvnnatQNVwqrleQLGVS---KARLDYLRTtlsaqvgedganidkLAdgdrqlllilrallQEKDLIILD 495
Cdd:cd03229 92 TVL------------ENI-----ALGLSggqQQRVALARA---------------LA--------------MDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491954606 496 ETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRL-HFADHVYGITKGE 547
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
346-550 |
3.61e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.92 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVD-QSLFHVSIEK-- 422
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNpDNQFVGSIVKyd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 423 ---SLQGFSV--NNATQNVWQRLEQLGVSkARLDYLRTTLSAQVGEDGANIDKLADGdrqlllilrallqeKDLIILDET 497
Cdd:PRK13648 105 vafGLENHAVpyDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALN--------------PSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491954606 498 LSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRLHFADHVYGITKGEcVY 550
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGT-VY 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
342-563 |
3.84e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.39 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTpiskisasemgANVAYVSVDQSLFHVsiE 421
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET-----------VKIGYFDQHQEELDP--D 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 KS----LQGFSVNNATQNVWQRLEQLGVS---------------KARLDYLRTTLSaqvgedGANidkladgdrqlllil 482
Cdd:COG0488 394 KTvldeLRDGAPGGTEQEVRGYLGRFLFSgddafkpvgvlsggeKARLALAKLLLS------PPN--------------- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 483 rallqekdLIILDETLSSLDTArfaevSR-LLRHYVDTFKIKMILISHktNRlHF----ADHVYGITKGecvyfsKLADW 557
Cdd:COG0488 453 --------VLLLDEPTNHLDIE-----TLeALEEALDDFPGTVLLVSH--DR-YFldrvATRILEFEDG------GVREY 510
|
....*.
gi 491954606 558 ASTYED 563
Cdd:COG0488 511 PGGYDD 516
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
345-549 |
4.65e-10 |
|
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: 60.19 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEKsl 424
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRD-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 425 qgfsvNNATQNVWQRLEQLgVSKARL----DY---LRTTLSAQVGEDGANidkLADGDRQLLLILRALLQEKDLIILDET 497
Cdd:cd03252 95 -----NIALADPGMSMERV-IEAAKLagahDFiseLPEGYDTIVGEQGAG---LSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491954606 498 LSSLDTARFAEVSRLLRHYVDTFKIkmILISHKTNRLHFADHVYGITKGECV 549
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICAGRTV--IIIAHRLSTVKNADRIIVMEKGRIV 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
333-416 |
7.24e-10 |
|
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: 58.18 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNLRNF--DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKiSASEMGANVAYVS 410
Cdd:cd03230 1 IEVRNLSKRygKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
....*.
gi 491954606 411 VDQSLF 416
Cdd:cd03230 80 EEPSLY 85
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
242-549 |
8.03e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.66 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 242 SWIAALVLIAFLevtslALGGYSfLRGVIGLGTVYMMIDYATRIQAPLESMQFHANNVQYLKGAFANLAELERKFVMQSG 321
Cdd:PRK10790 257 SLFSALILCGLL-----MLFGFS-ASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 322 NSPYPTKpTIRLHISNLrNF----DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKI 397
Cdd:PRK10790 331 NDDRPLQ-SGRIDIDNV-SFayrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 398 SASEMGANVAYVSVD-----QSLF-HVSIEKSLqgfsvnnATQNVWQRLEQLGVSkarlDYLRTT---LSAQVGEDGANi 468
Cdd:PRK10790 409 SHSVLRQGVAMVQQDpvvlaDTFLaNVTLGRDI-------SEEQVWQALETVQLA----ELARSLpdgLYTPLGEQGNN- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 469 dkLADGDRQLLLILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDtfKIKMILISHKTNRLHFADHVYGITKGEC 548
Cdd:PRK10790 477 --LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
.
gi 491954606 549 V 549
Cdd:PRK10790 553 V 553
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
331-412 |
1.07e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 57.83 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 331 IRLHISNLRNFDHqvLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEM-GANVAYV 409
Cdd:cd03215 3 PVLEVRGLSVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGIAYV 80
|
...
gi 491954606 410 SVD 412
Cdd:cd03215 81 PED 83
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
333-409 |
1.37e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 59.68 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNLR-NFDH-----QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGL---QHQYEGQIDYSKTPISKISASEM- 402
Cdd:COG0444 2 LEVRNLKvYFPTrrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKELr 81
|
90
....*....|
gi 491954606 403 ---GANVAYV 409
Cdd:COG0444 82 kirGREIQMI 91
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
343-416 |
2.53e-09 |
|
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: 57.48 E-value: 2.53e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491954606 343 HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPIskisaSEMGANVAYVSVDQSLF 416
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDRGYVFQQDALL 85
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
354-529 |
2.71e-09 |
|
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: 57.30 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 354 APGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPI----SKISASEMGANVAYVSVDQSLF-HVS----IEKSL 424
Cdd:cd03297 21 LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpHLNvrenLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 425 QGFSVNNATQNVWQRLEQLGVSKARldylrttlsaqvgedGANIDKLADGDRQLLLILRALLQEKDLIILDETLSSLDTA 504
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLL---------------NRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180
....*....|....*....|....*
gi 491954606 505 RFAEVSRLLRHYVDTFKIKMILISH 529
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTH 190
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
342-550 |
3.86e-09 |
|
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: 56.84 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIdysktpisKISASEMGANVAYVSVDQSLfhvsIE 421
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI--------TFDGKSYQKNIEALRRIGAL----IE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 KslQGFSVN-NATQNVWQRLEQLGVSKARLDYLRTTlsaqVGEDGANIDKLAD---GDRQLLLILRALLQEKDLIILDET 497
Cdd:cd03268 80 A--PGFYPNlTARENLRLLARLLGIRKKRIDEVLDV----VGLKDSAKKKVKGfslGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491954606 498 LSSLDTARFAEVSRLLRHYVDTfKIKMILISHKTNRLH-FADHVYGITKGECVY 550
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQkVADRIGIINKGKLIE 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
342-458 |
4.22e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQ--VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGA----NVAYVSvdQS- 414
Cdd:PRK10584 20 EHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakHVGFVF--QSf 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 491954606 415 --------LFHVSIEKSLQGFSVNNATQNVWQRLEQLGVSKaRLDYLRTTLS 458
Cdd:PRK10584 98 mliptlnaLENVELPALLRGESSRQSRNGAKALLEQLGLGK-RLDHLPAQLS 148
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
344-551 |
5.02e-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: 56.65 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEKS 423
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 424 LQGFSVNNATQnvwqrleqlgvskarldyLRTTLSaqVGEDGANidkLADGDRQLLLILRALLQEKDLIILDETLSSLDT 503
Cdd:cd03369 102 LDPFDEYSDEE------------------IYGALR--VSEGGLN---LSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491954606 504 ARFAEVSRLLRhyvDTFKIKMIL-ISHKTNRLHFADHVYGITKGECVYF 551
Cdd:cd03369 159 ATDALIQKTIR---EEFTNSTILtIAHRLRTIIDYDKILVMDAGEVKEY 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
333-563 |
5.48e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.41 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNL-----RNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEG--QIDYSKTPISKISASEMGAN 405
Cdd:PRK13642 5 LEVENLvfkyeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 406 VAYVSVDQSLFHVSIEKSLqGFSVNNA---TQNVWQRLEQLGVSKARLDYlRTTLSAqvgedganidKLADGDRQLLLIL 482
Cdd:PRK13642 85 MVFQNPDNQFVGATVEDDV-AFGMENQgipREEMIKRVDEALLAVNMLDF-KTREPA----------RLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 483 RALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRLHFADHVYGITKGECVYFSKLADWASTYE 562
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
.
gi 491954606 563 D 563
Cdd:PRK13642 233 D 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
111-549 |
7.67e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.58 E-value: 7.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 111 QTGDLNDRLTKDidqCRLFCQqTLipvwSDVIQVITIICVLFFqsVLIGAAFTGYLLLSILVLRHVNTSGndVIPK-LRK 189
Cdd:TIGR00958 256 KTGELTSRLSSD---TQTMSR-SL----SLNVNVLLRNLVMLL--GLLGFMLWLSPRLTMVTLINLPLVF--LAEKvFGK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 190 REAKTADFLQDVFVNNNDVAPMQASS-RVIAWF-------NKQYDKLlplelhaQSFIYRSWIAALVLIAFLEVTS---- 257
Cdd:TIGR00958 324 RYQLLSEELQEAVAKANQVAEEALSGmRTVRSFaaeegeaSRFKEAL-------EETLQLNKRKALAYAGYLWTTSvlgm 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 258 ------LALGGYSFLRG--------------------VIGLGTVY--MM------------IDYATRIQAPLESMQFHAN 297
Cdd:TIGR00958 397 liqvlvLYYGGQLVLTGkvssgnlvsfllyqeqlgeaVRVLSYVYsgMMqavgasekvfeyLDRKPNIPLTGTLAPLNLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 298 -NVQYLKGAFAnlaelerkfvmqsgnspYPTKPtirlhisnlrnfDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAi 376
Cdd:TIGR00958 477 gLIEFQDVSFS-----------------YPNRP------------DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAAL- 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 377 vgLQHQYE---GQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEKSLqGFSVNNATQNVWQRLEQLGVSKARLDYL 453
Cdd:TIGR00958 527 --LQNLYQptgGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI-AYGLTDTPDEEIMAAAKAANAHDFIMEF 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 454 RTTLSAQVGEDGAnidKLADGDRQLLLILRALLQEKDLIILDETLSSLDtarfAEVSRLLRHYVDTFKIKMILISHKTNR 533
Cdd:TIGR00958 604 PNGYDTEVGEKGS---QLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLST 676
|
490
....*....|....*.
gi 491954606 534 LHFADHVYGITKGECV 549
Cdd:TIGR00958 677 VERADQILVLKKGSVV 692
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-547 |
1.09e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.55 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 338 LRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPI--SKISASEMGANVAYV--SVDQ 413
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVfqDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 414 SLFHVSIEKSLqGFSVNNatqnvwqrleqLGVSKA----RLDYLRTTLSAQvGEDGANIDKLADGDRQLLLILRALLQEK 489
Cdd:PRK13638 89 QIFYTDIDSDI-AFSLRN-----------LGVPEAeitrRVDEALTLVDAQ-HFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491954606 490 DLIILDETLSSLDTARFAEVSRLLRHYVDTFKiKMILISHKTNRLH-FADHVYGITKGE 547
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYeISDAVYVLRQGQ 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
350-556 |
1.11e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 55.92 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 350 DMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI-----DYSKTPISKisasemgANVAYVSVDQSLF-HVSIEKS 423
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwngqDLTALPPAE-------RPVSMLFQENNLFpHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 424 LQ-GFSVN---NATQ--NVWQRLEQLGVSKArLDYLRTTLS---------AQVgedganidkLADgdrqlllilrallqE 488
Cdd:COG3840 92 IGlGLRPGlklTAEQraQVEQALERVGLAGL-LDRLPGQLSggqrqrvalARC---------LVR--------------K 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491954606 489 KDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNR-LHFADHVYGITKGECVYFSKLAD 556
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDaARIADRVLLVADGRIAADGPTAA 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
340-559 |
2.67e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.04 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 340 NFdHQVLKKVDMAIA---PGQ-IIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKisaSEMGANVA-------Y 408
Cdd:PRK11144 5 NF-KQQLGDLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFD---AEKGICLPpekrrigY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 409 VSVDQSLF-HVSIEKSLQgFSVNNATQNVWQRLEQLGVSKARLDYLRTTLSAqvGEDganiDKLADGdrqlllilRALLQ 487
Cdd:PRK11144 81 VFQDARLFpHYKVRGNLR-YGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSG--GEK----QRVAIG--------RALLT 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491954606 488 EKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNR-LHFADHVYGITKGECVYFSKLAD-WAS 559
Cdd:PRK11144 146 APELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEiLRLADRVVVLEQGKVKAFGPLEEvWAS 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
342-550 |
2.82e-08 |
|
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: 54.88 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASE---MGANVAYVSVDQSLfhv 418
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQIGMIFQQFNL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 419 sIEKSlqgfsvnNATQNV----------WQRLEQLgVSKArlDYLRtTLSA--QVG-EDGANI--DKLADGDRQLLLILR 483
Cdd:cd03256 90 -IERL-------SVLENVlsgrlgrrstWRSLFGL-FPKE--EKQR-ALAAleRVGlLDKAYQraDQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491954606 484 ALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTN-RLHFADHVYGITKGECVY 550
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDlAREYADRIVGLKDGRIVF 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
333-387 |
2.89e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 55.92 E-value: 2.89e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 333 LHISNLR-NFDH-QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:COG1118 3 IEVRNISkRFGSfTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRI 59
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
345-553 |
3.46e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 54.91 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEKSL 424
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 425 QGfSVNNATQNVWQRLE--QLgvsKARLDYLRTTLSAQVGEDGANidkLADGDRQLLLILRALLQEKDLIILDETLSSLD 502
Cdd:cd03288 116 DP-ECKCTDDRLWEALEiaQL---KNMVKSLPGGLDAVVTEGGEN---FSVGQRQLFCLARAFVRKSSILIMDEATASID 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491954606 503 TArfaeVSRLLRHYVDT-FKIKMIL-ISHKTNRLHFADHVYGITKGECVYFSK 553
Cdd:cd03288 189 MA----TENILQKVVMTaFADRTVVtIAHRVSTILDADLVLVLSRGILVECDT 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
333-549 |
4.74e-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: 53.82 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNLRNF--DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGanvaY-- 408
Cdd:cd03269 1 LEVENVTKRfgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIG----Ylp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 409 --------VSVDQSLFHVSiekSLQGFSVNNATQNVWQRLEQLGVSKARLdylrttlsaqvgedgANIDKLADGDRQLLL 480
Cdd:cd03269 77 eerglypkMKVIDQLVYLA---QLKGLKKEEARRRIDEWLERLELSEYAN---------------KRVEELSKGNQQKVQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 481 ILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKiKMILISHKTNRLH-FADHVYGITKGECV 549
Cdd:cd03269 139 FIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEeLCDRVLLLNKGRAV 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
344-551 |
5.78e-08 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 52.94 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGL--QHQYEGQIDYSKTPISKISASEMganVAYVSVDQSLFhvsie 421
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI---IGYVPQDDILH----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 kslqgfsvnnATQNVWqrlEQLGVSkarldylrttlsaqvgedgANIDKLADGDRQLLLILRALLQEKDLIILDETLSSL 501
Cdd:cd03213 95 ----------PTLTVR---ETLMFA-------------------AKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491954606 502 DTARFAEVSRLLRHYVDTFKIKMILIsH--KTNRLHFADHVYGITKGECVYF 551
Cdd:cd03213 143 DSSSALQVMSLLRRLADTGRTIICSI-HqpSSEIFELFDKLLLLSQGRVIYF 193
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
350-550 |
1.17e-07 |
|
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: 52.50 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 350 DMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI-----DYSKTPISKisasemgANVAYVSVDQSLF-HVSIEKS 423
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvDVTAAPPAD-------RPVSMLFQENNLFaHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 424 LqGFSVNnatqnvwQRLEQLGVSKARLDylrtTLSAQVGEDGANI---DKLADGDRQLLLILRALLQEKDLIILDETLSS 500
Cdd:cd03298 91 V-GLGLS-------PGLKLTAEDRQAIE----VALARVGLAGLEKrlpGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491954606 501 LDTARFAEVSRLLRHYVDTFKIKMILISHK-TNRLHFADHVYGITKGECVY 550
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQpEDAKRLAQRVVFLDNGRIAA 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-387 |
1.20e-07 |
|
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: 51.66 E-value: 1.20e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEI 57
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
345-552 |
1.59e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEKSL 424
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 425 QGFSVNNATqNVWQRLEQLGVSKArLDYLRTTLSAQVGEDGANidkLADGDRQLLLILRALLQEKDLIILDETLSSLDTA 504
Cdd:PLN03232 1331 DPFSEHNDA-DLWEALERAHIKDV-IDRNPFGLDAEVSEGGEN---FSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491954606 505 RFAEVSRLLRhyvDTFK-IKMILISHKTNRLHFADHVYGITKGECVYFS 552
Cdd:PLN03232 1406 TDSLIQRTIR---EEFKsCTMLVIAHRLNTIIDCDKILVLSSGQVLEYD 1451
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
345-556 |
1.77e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKIS---ASEMGanvayvsvdqsLFHVSIE 421
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLG-----------IYLVPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 KSLqgFSVNNATQNVWQRLEQLGVSKARLDYLRTTLSAQVGEDgANIDKLADGDRQLLLILRALLQEKDLIILDETLSSL 501
Cdd:PRK15439 95 PLL--FPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLD-SSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491954606 502 DTarfAEVSRLLRHyvdtfkIKMIL--------ISHKTNRL-HFADHVYGITKGECVYFSKLAD 556
Cdd:PRK15439 172 TP---AETERLFSR------IRELLaqgvgivfISHKLPEIrQLADRISVMRDGTIALSGKTAD 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
333-549 |
2.10e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.53 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNLR------NFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGL----QHQYEGQIDYSKTPISKISASEM 402
Cdd:COG4172 7 LSVEDLSvafgqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 403 ----GANVAYVSvdQ----SL--FHvSIEKSL-------QGFSVNNATQNVWQRLEQLGV--SKARLDYLRTTLSaqvge 463
Cdd:COG4172 87 rrirGNRIAMIF--QepmtSLnpLH-TIGKQIaevlrlhRGLSGAAARARALELLERVGIpdPERRLDAYPHQLS----- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 464 dG------------ANidkladgdrqlllilrallqEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKT 531
Cdd:COG4172 159 -GgqrqrvmiamalAN--------------------EPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL 217
|
250 260
....*....|....*....|
gi 491954606 532 N--RlHFADHVYGITKGECV 549
Cdd:COG4172 218 GvvR-RFADRVAVMRQGEIV 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
344-402 |
2.19e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 52.47 E-value: 2.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEM 402
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAEL 74
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
329-387 |
2.39e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 52.79 E-value: 2.39e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954606 329 PTIRLHISNLR-NF-DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:COG3842 2 AMPALELENVSkRYgDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI 62
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
84-568 |
2.48e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 84 LKMTHRVRKgylnlisfgdeirdseSFQTGDLNDRLTKDIDQCRLFCQQtLIPVWSDVIQvITIICVLFFQSVLIGAAFt 163
Cdd:PLN03232 385 LRLTHEARK----------------NFASGKVTNMITTDANALQQIAEQ-LHGLWSAPFR-IIVSMVLLYQQLGVASLF- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 164 GYLLLSILVlrhvnTSGNDVIPKLRKReakTADFLQ----DVFVNNNDVAPMQaSSRVIAW---FNKQYDKLLPLELhaq 236
Cdd:PLN03232 446 GSLILFLLI-----PLQTLIVRKMRKL---TKEGLQwtdkRVGIINEILASMD-TVKCYAWeksFESRIQGIRNEEL--- 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 237 sfiyrSWI-AALVLIAF---------LEVTSLALGGYSFLRGVIGLGTVYMMIDYATRIQAPLESMqfhANNVQYLKGAF 306
Cdd:PLN03232 514 -----SWFrKAQLLSAFnsfilnsipVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNML---PNLLSQVVNAN 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 307 ANLAELERKFVMQ----SGNSPY-PTKPTIRLHISNLR---NFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVG 378
Cdd:PLN03232 586 VSLQRIEELLLSEerilAQNPPLqPGAPAISIKNGYFSwdsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG 665
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 379 lqhqyegqidysKTPISKISASEMGANVAYVSVDQSLFHVSIEKSLQgFSVNNATQNVWQRLEQLGVsKARLDYLRTTLS 458
Cdd:PLN03232 666 ------------ELSHAETSSVVIRGSVAYVPQVSWIFNATVRENIL-FGSDFESERYWRAIDVTAL-QHDLDLLPGRDL 731
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 459 AQVGEDGANIdklADGDRQLLLILRALLQEKDLIILDETLSSLDTARFAEV-SRLLRHYVDTfKIKMILishkTNRLHFA 537
Cdd:PLN03232 732 TEIGERGVNI---SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKG-KTRVLV----TNQLHFL 803
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 491954606 538 DHV-------YGITKGECVY---------FSKLADWASTYEDEQNVK 568
Cdd:PLN03232 804 PLMdriilvsEGMIKEEGTFaelsksgslFKKLMENAGKMDATQEVN 850
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
331-409 |
2.66e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.11 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 331 IRLHISNLR---NFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEM-GANV 406
Cdd:COG3845 256 VVLEVENLSvrdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrRLGV 335
|
...
gi 491954606 407 AYV 409
Cdd:COG3845 336 AYI 338
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
345-515 |
2.72e-07 |
|
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: 51.85 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEKSL 424
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 425 QgFSVNNATQNVWQRLEQLGVSKARLDYLRTTLSAQVGEDGAnidKLADGDRQLLLILRALLQEKDLIILDETLSSLDTA 504
Cdd:cd03251 97 A-YGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGV---KLSGGQRQRIAIARALLKDPPILILDEATSALDTE 172
|
170
....*....|.
gi 491954606 505 RFAEVSRLLRH 515
Cdd:cd03251 173 SERLVQAALER 183
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
342-402 |
3.98e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 51.21 E-value: 3.98e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEM 402
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREI 74
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
345-540 |
4.41e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.87 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFhvsieksl 424
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 425 qGFSVNNATQNVWQ-RLEQLGVSKARLDYLRTTLSAQVGEDgaNIDKLADGDRQLLLILRALLQEKDLIILDETLSSLDT 503
Cdd:PRK10247 94 -GDTVYDNLIFPWQiRNQQPDPAIFLDDLERFALPDTILTK--NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 491954606 504 ARFAEVSRLLRHYVDTFKIKMILISHKTNRLHFADHV 540
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKV 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
344-535 |
4.44e-07 |
|
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: 51.08 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEKS 423
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 424 LQgFSVNNATQnvwqrlEQL--GVSKARLDYLRTTL----SAQVGEDGAnidKLADGDRQLLLILRALLQEKDLIILDET 497
Cdd:cd03253 95 IR-YGRPDATD------EEVieAAKAAQIHDKIMRFpdgyDTIVGERGL---KLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 491954606 498 LSSLDTARFAEVSRLLRhyvDTFKIK-MILISHktnRLH 535
Cdd:cd03253 165 TSALDTHTEREIQAALR---DVSKGRtTIVIAH---RLS 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
260-556 |
5.77e-07 |
|
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: 52.64 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 260 LGGYSFLRGVIGLGTVYMM-----IDYATRIQAPLESmqfhaNNVQYLKGAFANLAELERKFVMQSGNSPYPTKPTIRLH 334
Cdd:TIGR00957 1212 ISRHSLSAGLVGLSVSYSLqvtfyLNWLVRMSSEMET-----NIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVE 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 335 ISN--LR---NFDHqVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYV 409
Cdd:TIGR00957 1287 FRNycLRyreDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITII 1365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 410 SVDQSLFHVSIEKSLQGFSvNNATQNVWQRLEqLGVSKARLDYLRTTLSAQVGEDGANidkLADGDRQLLLILRALLQEK 489
Cdd:TIGR00957 1366 PQDPVLFSGSLRMNLDPFS-QYSDEEVWWALE-LAHLKTFVSALPDKLDHECAEGGEN---LSVGQRQLVCLARALLRKT 1440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 490 DLIILDETLSSLDTARFAEVSRLLRHYVDTFKIkmILISHKTNRLHFADHVYGITKGECVYFSKLAD 556
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTV--LTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSN 1505
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
349-540 |
8.47e-07 |
|
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: 51.25 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 349 VDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI--------DysktpiskisaSEMGANV-------AYVSVDQ 413
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevlqD-----------SARGIFLpphrrriGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 414 SLF-HVSIEKSLQ-GFSvNNATQNVWQRLEQ----LGVSkARLDYLRTTLSAqvGEdganidK---------LADgdrql 478
Cdd:COG4148 87 RLFpHLSVRGNLLyGRK-RAPRAERRISFDEvvelLGIG-HLLDRRPATLSG--GE------RqrvaigralLSS----- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 479 llilrallqeKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTN---RLhfADHV 540
Cdd:COG4148 152 ----------PRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDevaRL--ADHV 204
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
342-521 |
9.40e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 51.38 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSL-FHVSI 420
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 421 EKSLQ-GFSVNNATQNVWQRLEQLGVSKArLDylRTTLSAQVGEDganIDKLADGDRQLLLILRALLQEKDLIILDETLS 499
Cdd:PRK09536 95 RQVVEmGRTPHRSRFDTWTETDRAAVERA-ME--RTGVAQFADRP---VTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180
....*....|....*....|..
gi 491954606 500 SLDTARFAEVSRLLRHYVDTFK 521
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGK 190
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
341-549 |
9.62e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.89 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 341 FDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI---DYSKTPISK---ISASEMGANVAYVSVDQS 414
Cdd:PRK13643 17 FASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgDIVVSSTSKqkeIKPVRKKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 415 LFHVSIEKSLQ------GFSVNNATQNVWQRLEQLGVSKARLDYLRTTLSaqvgedGANIDKLAdgdrqlllILRALLQE 488
Cdd:PRK13643 97 LFEETVLKDVAfgpqnfGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELS------GGQMRRVA--------IAGILAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 489 KDLIILDETLSSLDTARFAEVSRLLRHYVDTFKiKMILISHKTNRL-HFADHVYGITKGECV 549
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVaDYADYVYLLEKGHII 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
342-546 |
1.10e-06 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 50.03 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMgaNVAYVSVDQSLF-HVSI 420
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 421 EKSLQ-GFSVNNATQN-----VWQRLEQLgVSKARLDYLRTTLSAQvgedganidkLADGDRQLLLILRALLQEKDLIIL 494
Cdd:cd03296 92 FDNVAfGLRVKPRSERppeaeIRAKVHEL-LKLVQLDWLADRYPAQ----------LSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491954606 495 DETLSSLDTARFAEVSRLLRHYVDTFKIKMILISH-KTNRLHFADHVYGITKG 546
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKG 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
325-546 |
1.29e-06 |
|
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: 49.85 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 325 YPTKPtirlhisnlrnfDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAivgLQHQY---EGQIDYSKTPISKISASE 401
Cdd:cd03249 10 YPSRP------------DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSL---LERFYdptSGEILLDGVDIRDLNLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 402 MGANVAYVSVDQSLFHVSIEKSLqGFSVNNATQnvwqrLEQLGVSK-ARLDYLRTTL----SAQVGEDGAnidKLADGDR 476
Cdd:cd03249 75 LRSQIGLVSQEPVLFDGTIAENI-RYGKPDATD-----EEVEEAAKkANIHDFIMSLpdgyDTLVGERGS---QLSGGQK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 477 QLLLILRALLQEKDLIILDETLSSLDTARFAEVSRLLrhyvDTFKIKM--ILISHKTNRLHFADHVYGITKG 546
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL----DRAMKGRttIVIAHRLSTIRNADLIAVLQNG 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
342-473 |
1.32e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.22 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKtpiskisasemGANVAYVSVDQSLFhvsie 421
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLD----- 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 491954606 422 kslQGFSVnnaTQNVWQRLEQLGVSKARLDylrtTLSAQVGEDGANIDKLAD 473
Cdd:COG0488 74 ---DDLTV---LDTVLDGDAELRALEAELE----ELEAKLAEPDEDLERLAE 115
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
342-392 |
1.54e-06 |
|
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: 47.83 E-value: 1.54e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKT 392
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST 62
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
342-540 |
1.56e-06 |
|
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: 49.07 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI--DYSKTPISKISASEMGANVAYVSVDQSLF-HV 418
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiiDGLKLTDDKKNINELRQKVGMVFQQFNLFpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 419 SiekslqgfsvnnATQNVWQRLEQ-LGVSKARLDYLRTTLSAQVG-EDGAN--IDKLADGDRQLLLILRALLQEKDLIIL 494
Cdd:cd03262 92 T------------VLENITLAPIKvKGMSKAEAEERALELLEKVGlADKADayPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491954606 495 DETLSSLDTARFAEVSRLLRHYVDTfKIKMILISHKTNrlhFADHV 540
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMG---FAREV 201
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
342-407 |
1.75e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.63 E-value: 1.75e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVA 407
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
344-402 |
2.04e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.10 E-value: 2.04e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEM 402
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREV 74
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
342-549 |
3.05e-06 |
|
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: 48.29 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLqHQYE---GQIDYSKTPISKISASE---MGANVAyvsvdqsl 415
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEvteGEILFKGEDITDLPPEErarLGIFLA-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 416 fhvsiekslqgfsvnnatqnvWQRLEQL-GVSKArlDYLRttlSAQVGEDGanidkladGDRQLLLILRALLQEKDLIIL 494
Cdd:cd03217 83 ---------------------FQYPPEIpGVKNA--DFLR---YVNEGFSG--------GEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 495 DETLSSLDTARFAEVSRLLRHYVDTfKIKMILISHKTNRLHF--ADHVYGITKGECV 549
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYikPDRVHVLYDGRIV 184
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
343-529 |
3.23e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.70 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 343 HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQhQYEGQIDYSKTPISKISASEMganVAYVSVDQSLFHvsiek 422
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQL---LPVRHRIQVVFQ----- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 423 slQGFSVNNATQNVWQ------RLEQLGVSKARLDYLRTTLSAQVGEDGANIDK----LADGDRQLLLILRALLQEKDLI 492
Cdd:PRK15134 370 --DPNSSLNPRLNVLQiieeglRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRypaeFSGGQRQRIAIARALILKPSLI 447
|
170 180 190
....*....|....*....|....*....|....*..
gi 491954606 493 ILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISH 529
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
325-445 |
3.38e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.63 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 325 YPTKPT----IRLHISNLRnfDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISAS 400
Cdd:COG1129 245 FPKRAAapgeVVLEVEGLS--VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPR 322
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 491954606 401 E-MGANVAYVSVD---QSLFhvsiekslQGFSV-NNATQNVWQRLEQLGV 445
Cdd:COG1129 323 DaIRAGIAYVPEDrkgEGLV--------LDLSIrENITLASLDRLSRGGL 364
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
344-387 |
3.50e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.63 E-value: 3.50e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI 61
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
352-549 |
3.70e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.39 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 352 AIAPGQIIGLSGVSGSGKSTLAKAIVGLQhQYEGQIDYSKTPISKISASEMGANVAYVSVDQS-LFHVSiekslqgfsvn 430
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMP----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 431 natqnVWQRLEQLGVSKARLDYLRTTLS---AQVGED---GANIDKLADGD-------RQLLLILRALLQEKDLIILDET 497
Cdd:PRK03695 86 -----VFQYLTLHQPDKTRTEAVASALNevaEALGLDdklGRSVNQLSGGEwqrvrlaAVVLQVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491954606 498 LSSLDTARFAEVSRLLRHYVDTfKIKMILISHKTNR-LHFADHVYGITKGECV 549
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHtLRHADRVWLLKQGKLL 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
342-546 |
3.77e-06 |
|
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: 47.31 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISAsEMGANVAYVSVDQSLFHVSIE 421
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISVLNQRPYLFDTTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 kslqgfsvnnatQNVWQRLEqlGVSKARLDYLRTTLSaqvgedganidkladgdrqlllilrallqEKDLIILDETLSSL 501
Cdd:cd03247 93 ------------NNLGRRFS--GGERQRLALARILLQ-----------------------------DAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491954606 502 DtaRFAEvSRLLRHYVDTFKIKMIL-ISHKTNRLHFADHVYGITKG 546
Cdd:cd03247 130 D--PITE-RQLLSLIFEVLKDKTLIwITHHLTGIEHMDKILFLENG 172
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
345-514 |
3.90e-06 |
|
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: 47.87 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASeMGANVAYVSVDQSLFHV-SIEKS 423
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 424 LQGFSVNNATQNVWQRLEQLGVSkarldylrttlsaqvGEDGANIDKLADGDRQLLLILRALLQEKDLIILDETLSSLDT 503
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLN---------------GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|.
gi 491954606 504 ARFAEVSRLLR 514
Cdd:cd03231 159 AGVARFAEAMA 169
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
318-549 |
3.93e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.84 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 318 MQSGNSPYPTKPTIRLHISNLRNFDHQ---VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQhQYEGQIDYSKTPI 394
Cdd:PRK11174 335 PQQGEKELASNDPVTIEAEDLEILSPDgktLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIEL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 395 SKISASEMGANVAYVSVDQSLFHVSIEKSLQGFSVNNATQNVWQRLEQLGVSKArLDYLRTTLSAQVGEDGAnidKLADG 474
Cdd:PRK11174 414 RELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEF-LPLLPQGLDTPIGDQAA---GLSVG 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 475 DRQLLLILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYvdTFKIKMILISHKTNRLHFADHVYGITKGECV 549
Cdd:PRK11174 490 QAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
342-547 |
4.54e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.21 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQ-------IDYSKtPISKISA--SEMGANVAYVSVD 412
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTirvgditIDTAR-SLSQQKGliRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 413 QSLF-HVS-IEKSLQGFSVnnatqnVWQRLEQLGVSKARldylrtTLSAQVGEDG---ANIDKLADGDRQLLLILRALLQ 487
Cdd:PRK11264 94 FNLFpHRTvLENIIEGPVI------VKGEPKEEATARAR------ELLAKVGLAGketSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 488 EKDLIILDETLSSLDTARFAEVSRLLRHYVDTfKIKMILISHK-------TNRLHFADHVYGITKGE 547
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEmsfardvADRAIFMDQGRIVEQGP 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-402 |
6.01e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 48.54 E-value: 6.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEM 402
Cdd:COG1135 17 PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEREL 77
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
333-379 |
6.80e-06 |
|
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: 47.50 E-value: 6.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 491954606 333 LHISNLR----NFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGL 379
Cdd:cd03263 1 LQIRNLTktykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGE 51
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
258-425 |
7.43e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.80 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 258 LALGGYSFLRGVIGLGTVYMMIDYATRIQAPLESMqfhannVQYLKGAFANLAELERKFVMQSgnspypTKPTIR----- 332
Cdd:PRK13657 258 LVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQV------VAFINQVFMAAPKLEEFFEVED------AVPDVRdppga 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNLRN---FDH---------QVLKKVDMAIAPGQIIGLSGVSGSGKSTLakaIVGLQHQYE---GQIDYSKTPISKI 397
Cdd:PRK13657 326 IDLGRVKGaveFDDvsfsydnsrQGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRVFDpqsGRILIDGTDIRTV 402
|
170 180
....*....|....*....|....*...
gi 491954606 398 SASEMGANVAYVSVDQSLFHVSIEKSLQ 425
Cdd:PRK13657 403 TRASLRRNIAVVFQDAGLFNRSIEDNIR 430
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
342-540 |
8.79e-06 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 46.46 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLqhqyegqidysKTPISKISASEMGANVAYVsVDQSlfhvSIE 421
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGV-----------LRPTSGTVRRAGGARVAYV-PQRS----EVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 KSLQGFSVNNATQNVWQR------------------LEQLGV---SKARLDYL-----RTTLSAQVgedganidkLAdgd 475
Cdd:NF040873 68 DSLPLTVRDLVAMGRWARrglwrrltrddraavddaLERVGLadlAGRQLGELsggqrQRALLAQG---------LA--- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 476 rqlllilrallQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTfKIKMILISHKTNRLHFADHV 540
Cdd:NF040873 136 -----------QEADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPC 188
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
349-387 |
9.23e-06 |
|
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: 48.26 E-value: 9.23e-06
10 20 30
....*....|....*....|....*....|....*....
gi 491954606 349 VDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
346-546 |
9.84e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.94 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGA----NVAYVSVDQSLFHVSIE 421
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSrnrySVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 KSLQGFSVNNATQnvWQRLEQLGVSKARLDYLRTTLSAQVGEDGANidkLADGDRQLLLILRALLQEKDLIILDETLSSL 501
Cdd:cd03290 97 ENITFGSPFNKQR--YKAVTDACSLQPDIDLLPFGDQTEIGERGIN---LSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491954606 502 DTARFAEVSR--LLRHYVDTfKIKMILISHKTNRLHFADHVYGITKG 546
Cdd:cd03290 172 DIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
335-389 |
1.05e-05 |
|
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: 46.79 E-value: 1.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 335 ISNLRNF--DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQY-----EGQIDY 389
Cdd:cd03260 3 LRDLNVYygDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLL 64
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
342-549 |
1.13e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.09 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIe 421
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTI- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 kslqgfsVNN---ATQNVWQRlEQLgVSKARLDY-------LRTTLSAQVGEDGANidkLADGDRQLLLILRALLQEKDL 491
Cdd:PRK11176 434 -------ANNiayARTEQYSR-EQI-EEAARMAYamdfinkMDNGLDTVIGENGVL---LSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 492 IILDETLSSLDTarfaEVSRLLRHYVDTF-KIKMIL-ISHKTNRLHFADHVYGITKGECV 549
Cdd:PRK11176 502 LILDEATSALDT----ESERAIQAALDELqKNRTSLvIAHRLSTIEKADEILVVEDGEIV 557
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
346-532 |
1.16e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.90 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGL--QHQYEGQIDYSKTPI--SKISASEMG---------ANVAYVSVD 412
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLkaSNIRDTERAgiviihqelTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 413 QSLFhVSIEKSLQGFSVNNATqnVWQRLEQLgVSKARLDYLRTTLSaqVGEDGANIDKLADgdrqlllILRALLQEKDLI 492
Cdd:TIGR02633 97 ENIF-LGNEITLPGGRMAYNA--MYLRAKNL-LRELQLDADNVTRP--VGDYGGGQQQLVE-------IAKALNKQARLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491954606 493 ILDETLSSLDTarfAEVSRLLRHYVD--TFKIKMILISHKTN 532
Cdd:TIGR02633 164 ILDEPSSSLTE---KETEILLDIIRDlkAHGVACVYISHKLN 202
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
343-529 |
1.20e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.18 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 343 HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMganVAYV----SVDQSlFHV 418
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVpqseEVDWS-FPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 419 SIEKSLQgfsVNNATQNVWQRL------EQLGVSKARLDYLRTTlSAQVGEdganidkLADGDRQLLLILRALLQEKDLI 492
Cdd:PRK15056 96 LVEDVVM---MGRYGHMGWLRRakkrdrQIVTAALARVDMVEFR-HRQIGE-------LSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 491954606 493 ILDETLSSLDTARFAEVSRLLRHYVDTFKiKMILISH 529
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTH 200
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
344-380 |
1.48e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.21 E-value: 1.48e-05
10 20 30
....*....|....*....|....*....|....*..
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQ 380
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGIT 57
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
327-547 |
1.72e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 46.93 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 327 TKPTIRL-HIS-NLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGA 404
Cdd:PRK13635 2 KEEIIRVeHISfRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 405 NVAYV--SVDQSLFHVSIEKSLqGFSvnnatqnvwqrLEQLGVSkaRLDYLRTTLSA--QVG-EDGANID--KLADGDRQ 477
Cdd:PRK13635 82 QVGMVfqNPDNQFVGATVQDDV-AFG-----------LENIGVP--REEMVERVDQAlrQVGmEDFLNREphRLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 478 LLLILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRLHFADHVYGITKGE 547
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGE 217
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
344-550 |
1.74e-05 |
|
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: 46.11 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYE---GQIDYSKTPISKisaSEMGANVAYVS-VDQSLFHVS 419
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP---DQFQKCVAYVRqDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 420 IEKSLQgFSVNNATqnvwQRLEQLGVSKARLDYLRTTLSA--QVGedGANIDKLADGDRQLLLILRALLQEKDLIILDET 497
Cdd:cd03234 98 VRETLT-YTAILRL----PRKSSDAIRKKRVEDVLLRDLAltRIG--GNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491954606 498 LSSLDTARFAEVSRLLRHYVDTFKIkmILIS-HK--TNRLHFADHVYGITKGECVY 550
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRI--VILTiHQprSDLFRLFDRILLLSSGEIVY 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
311-528 |
1.77e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 311 ELERKFV-MQSGNSPYPTKPTirLHISNLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDY 389
Cdd:PRK09700 245 ELQNRFNaMKENVSNLAHETV--FEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 390 SK---TPISKISASEMGanVAYVSV---DQSLFH-------VSIEKSLQGFSVNNATQNVWQRLEQLGVSKARLDylrtt 456
Cdd:PRK09700 323 NGkdiSPRSPLDAVKKG--MAYITEsrrDNGFFPnfsiaqnMAISRSLKDGGYKGAMGLFHEVDEQRTAENQREL----- 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 457 LSAQVGEDGANIDKLADGDRQLLLILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILIS 528
Cdd:PRK09700 396 LALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSS 467
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-569 |
1.79e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 46.58 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQY------EGQIDYSKTPISKISASEMGANVAYVSVDQSL 415
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 416 F-HVSIEKSL------QGFSVNNATQNVWQR-LEQLGVSKARLDYLRTTLSaqvgedganidKLADGDRQLLLILRALLQ 487
Cdd:PRK14246 102 FpHLSIYDNIayplksHGIKEKREIKKIVEEcLRKVGLWKEVYDRLNSPAS-----------QLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 488 EKDLIILDETLSSLDTARFAEVSRLLRHYVDtfKIKMILISHKTNRL-HFADHVYGITKGEcvyfskLADWASTYEDEQN 566
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVaRVADYVAFLYNGE------LVEWGSSNEIFTS 242
|
...
gi 491954606 567 VKN 569
Cdd:PRK14246 243 PKN 245
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
342-388 |
1.94e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.15 E-value: 1.94e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQID 388
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW 62
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
344-473 |
2.13e-05 |
|
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: 47.24 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKtpiskisasemGANVAYVSVDQSLfhvsieks 423
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP-----------GIKVGYLPQEPQL-------- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491954606 424 lqgfsvnNATQNVWQRLEQ-LGVSKARLDYLrTTLSAQVGEDGANIDKLAD 473
Cdd:TIGR03719 80 -------DPTKTVRENVEEgVAEIKDALDRF-NEISAKYAEPDADFDKLAA 122
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
333-424 |
2.26e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 46.75 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNL-RNFDHQ-VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVS 410
Cdd:PRK11607 20 LEIRNLtKSFDGQhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQS 99
|
90
....*....|....*
gi 491954606 411 VdqSLF-HVSIEKSL 424
Cdd:PRK11607 100 Y--ALFpHMTVEQNI 112
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
343-530 |
2.39e-05 |
|
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: 46.39 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 343 HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQyEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEK 422
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 423 SLQGFSVNNaTQNVWQRLEQLGVsKARLDYLRTTLSAQVgEDGANIdkLADGDRQLLLILRALLQEKDLIILDETLSSLD 502
Cdd:cd03289 96 NLDPYGKWS-DEEIWKVAEEVGL-KSVIEQFPGQLDFVL-VDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180
....*....|....*....|....*...
gi 491954606 503 TARFAEVSRLLRHYVDTFKIkmILISHK 530
Cdd:cd03289 171 PITYQVIRKTLKQAFADCTV--ILSEHR 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
346-532 |
2.43e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGL--QHQYEGQIDYSKTPI--SKISASEMG---------ANVAYVSVD 412
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqaSNIRDTERAgiaiihqelALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 413 QSLF----------------HVSIEKSLQGFSVNnatQNVWQRLEQLGVSKARLDYLRTTLSAQVgedganidkladgdr 476
Cdd:PRK13549 101 ENIFlgneitpggimdydamYLRAQKLLAQLKLD---INPATPVGNLGLGQQQLVEIAKALNKQA--------------- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491954606 477 qlllilrallqekDLIILDETLSSLdTArfAEVSRLLrHYVDTFK---IKMILISHKTN 532
Cdd:PRK13549 163 -------------RLLILDEPTASL-TE--SETAVLL-DIIRDLKahgIACIYISHKLN 204
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
343-453 |
2.61e-05 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 45.61 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 343 HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI-----DYSKTPISKISASEMGanvaYVSVDQSLFh 417
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqDITKLPMHKRARLGIG----YLPQEASIF- 87
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 491954606 418 vsieKSLqgfSVnnaTQNVWQRLEQLGVSKA----RLDYL 453
Cdd:cd03218 88 ----RKL---TV---EENILAVLEIRGLSKKereeKLEEL 117
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
341-549 |
2.71e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.31 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 341 FDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQID------YSKTPISKISASEMGANVAYVSVDQS 414
Cdd:PRK13646 18 YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTvdditiTHKTKDKYIRPVRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 415 LFHVSIEKSLQ------GFSVNNATQNVWQRLEQLGVSKARLDYLRTTLSaqvgedGANIDKLAdgdrqlllILRALLQE 488
Cdd:PRK13646 98 LFEDTVEREIIfgpknfKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMS------GGQMRKIA--------IVSILAMN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 489 KDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRL-HFADHVYGITKGECV 549
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIV 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-387 |
3.06e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 46.26 E-value: 3.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 333 LHISNL-RNF-DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:COG4152 2 LELKGLtKRFgDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV 58
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
333-540 |
3.47e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISN--LRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQidysktpiskisasemganvaYVS 410
Cdd:PRK10938 4 LQISQgtFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE---------------------RQS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 411 VDQSLFHVSIEKsLQgfsvnNATQNVWQRLEQLGVSKARLDYLRTTlsAQVGEDGAN-------------IDKLAD---- 473
Cdd:PRK10938 63 QFSHITRLSFEQ-LQ-----KLVSDEWQRNNTDMLSPGEDDTGRTT--AEIIQDEVKdparceqlaqqfgITALLDrrfk 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 474 ----GDRQLLLILRALLQEKDLIILDETLSSLDTARFAEVSRLLrHYVDTFKIKMILIShktNRLH----FADHV 540
Cdd:PRK10938 135 ylstGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL-ASLHQSGITLVLVL---NRFDeipdFVQFA 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
342-473 |
3.53e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKtpiskisasemGANVAYVSVDQSLfhvsie 421
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP-----------GIKVGYLPQEPQL------ 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 491954606 422 kslqgfsvnNATQNVWQRLEQlGVS--KARLDYLrTTLSAQVGEDGANIDKLAD 473
Cdd:PRK11819 82 ---------DPEKTVRENVEE-GVAevKAALDRF-NEIYAAYAEPDADFDALAA 124
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
346-549 |
3.85e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 45.75 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI--------DYSKTP-ISKIsasemgANVAYVSVDQSLF 416
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgDFSKLQgIRKL------VGIVFQNPETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 417 HVSIEKSLqGFSVNNAT-------QNVWQRLEQLGVSKARLDYLRTtlsaqvgedganidkLADGDRQLLLILRALLQEK 489
Cdd:PRK13644 92 GRTVEEDL-AFGPENLClppieirKRVDRALAEIGLEKYRHRSPKT---------------LSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 490 DLIILDETLSSLDTARFAEVSRLLRHYVDTFKiKMILISHKTNRLHFADHVYGITKGECV 549
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
342-387 |
3.87e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 45.46 E-value: 3.87e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
341-502 |
4.20e-05 |
|
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: 45.31 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 341 FDHQV-LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVayvsVDQS--LF- 416
Cdd:cd03300 10 YGGFVaLDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNT----VFQNyaLFp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 417 HVSIekslqgfsvnnaTQNVWQRLEQLGVSKARLDYLRTTLSAQVGEDG---ANIDKLADGDRQLLLILRALLQEKDLII 493
Cdd:cd03300 86 HLTV------------FENIAFGLRLKKLPKAEIKERVAEALDLVQLEGyanRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
....*....
gi 491954606 494 LDETLSSLD 502
Cdd:cd03300 154 LDEPLGALD 162
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
345-417 |
4.49e-05 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 45.12 E-value: 4.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKIS----ASEMGANVAYvsVDQSlFH 417
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLRARHVGF--VFQS-FQ 100
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
345-562 |
4.54e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.41 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVG-LQ-HQYEGQIDYSKTPISKISASEMGanvaYVSVDQSLF-HVSIE 421
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQgNNFTGTILANNRKPTKQILKRTG----FVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 422 KSLQGFSV----NNATQNVWQRLEQLGVSKARLDYLRTTLsaqVGEdgANIDKLADGDRQLLLILRALLQEKDLIILDET 497
Cdd:PLN03211 159 ETLVFCSLlrlpKSLTKQEKILVAESVISELGLTKCENTI---IGN--SFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491954606 498 LSSLD-TARFAEVSRL--LRHYVDTFKIKMILISHKTNRLHfaDHVYGITKGECVYFSKLADWASTYE 562
Cdd:PLN03211 234 TSGLDaTAAYRLVLTLgsLAQKGKTIVTSMHQPSSRVYQMF--DSVLVLSEGRCLFFGKGSDAMAYFE 299
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
334-551 |
5.56e-05 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 44.98 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 334 HISNLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQ 413
Cdd:cd03295 5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 414 SLF-HVSIEkslqgfsvnnatQNVWQRLEQLGVSKARLDYLRTTLSAQVGEDGANI-----DKLADGDRQLLLILRALLQ 487
Cdd:cd03295 85 GLFpHMTVE------------ENIALVPKLLKWPKEKIRERADELLALVGLDPAEFadrypHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 488 EKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNR-LHFADHVYGITKGECVYF 551
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEaFRLADRIAIMKNGEIVQV 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
342-397 |
7.16e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 44.67 E-value: 7.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKI 397
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA 79
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
333-549 |
7.61e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.79 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNLRNFDHQ------VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANV 406
Cdd:PRK13652 1 MHLIETRDLCYSysgskeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 407 AYV--SVDQSLFHVSIEKSLQ------GFSVNNATQNVWQRLEQLGVSKarldyLRTTLSAQvgedganidkLADGDRQL 478
Cdd:PRK13652 81 GLVfqNPDDQIFSPTVEQDIAfgpinlGLDEETVAHRVSSALHMLGLEE-----LRDRVPHH----------LSGGEKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 479 LLILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRL-HFADHVYGITKGECV 549
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIV 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
332-549 |
8.74e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.52 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 332 RLHISNLR-NF-DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQY-----EGQIDYSKTPISKISASEMGA 404
Cdd:PRK14247 3 KIEIRDLKvSFgQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 405 NVAYV-SVDQSLFHVSI-EKSLQGFSVN---NATQNVWQRLEQlGVSKARL-DYLRTTLSAQVGedganidKLADGDRQL 478
Cdd:PRK14247 83 RVQMVfQIPNPIPNLSIfENVALGLKLNrlvKSKKELQERVRW-ALEKAQLwDEVKDRLDAPAG-------KLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 479 LLILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIkmILISH-KTNRLHFADHVYGITKGECV 549
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHfPQQAARISDYVAFLYKGQIV 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
332-389 |
9.24e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.18 E-value: 9.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954606 332 RLHISNL--RNFDHQVL-KKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDY 389
Cdd:COG4178 362 ALALEDLtlRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR 422
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
344-379 |
9.31e-05 |
|
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: 44.34 E-value: 9.31e-05
10 20 30
....*....|....*....|....*....|....*.
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGL 379
Cdd:TIGR04520 16 PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL 51
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
326-532 |
9.81e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.79 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 326 PTKPTIRLHISnLRNFD-------HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQ--HQYEGQIDYSKTPIsk 396
Cdd:COG2401 20 VLDLSERVAIV-LEAFGvelrvveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 397 isasemganvayvSVDQSLfhvsIEKSLQGFSVNNATqnvwQRLEQLGVSKARLdYLRT--TLSaqvgeDG----ANIDK 470
Cdd:COG2401 97 -------------GREASL----IDAIGRKGDFKDAV----ELLNAVGLSDAVL-WLRRfkELS-----TGqkfrFRLAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491954606 471 LADGDRqlllilrallqekDLIILDETLSSLD--TARFaeVSRLLRHYVDTFKIKMILISHKTN 532
Cdd:COG2401 150 LLAERP-------------KLLVIDEFCSHLDrqTAKR--VARNLQKLARRAGITLVVATHHYD 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
328-388 |
1.33e-04 |
|
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: 43.68 E-value: 1.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954606 328 KPTIRLHISNLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQID 388
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
346-549 |
1.33e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.64 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMganvayvsvdQSLFHVSIEKSLQ 425
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAEL----------REVRRKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 426 GFSV---NNATQNVWQRLEQLGVSKAR-----LDYLRttlsaQVG-EDGAN--IDKLADGDRQLLLILRALLQEKDLIIL 494
Cdd:PRK10070 114 SFALmphMTVLDNTAFGMELAGINAEErrekaLDALR-----QVGlENYAHsyPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491954606 495 DETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNR-LHFADHVYGITKGECV 549
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEaMRIGDRIAIMQNGEVV 244
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
341-529 |
1.38e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.42 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 341 FDHQVLKkVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI-----DYSKTPISKISasemganvayVSV---D 412
Cdd:PRK10771 11 YHHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtlngqDHTTTPPSRRP----------VSMlfqE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 413 QSLF-HVSIEKSLqGFSVN-----NATQNvwQRLEQLgVSKARLDYLRTTLSAQvgedganidkLADGDRQLLLILRALL 486
Cdd:PRK10771 80 NNLFsHLTVAQNI-GLGLNpglklNAAQR--EKLHAI-ARQMGIEDLLARLPGQ----------LSGGQRQRVALARCLV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491954606 487 QEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISH 529
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
345-410 |
1.38e-04 |
|
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: 43.23 E-value: 1.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTpiskisasemganVAYVS 410
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVS 72
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
327-378 |
1.69e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 1.69e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 327 TKPTIRLHISNLR---NfDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVG 378
Cdd:CHL00131 2 NKNKPILEIKNLHasvN-ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
338-547 |
2.34e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.89 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 338 LRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKIS-ASEMGANVAYVSVDQSLF 416
Cdd:PRK15439 271 VEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEDRQSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 417 HVSIEKSLqGFSVNNATQN---VWQRLEQlgvSKARLDYLRTTLSAQVGEDGANIDKLADGDRQLLLILRALLQEKDLII 493
Cdd:PRK15439 351 GLYLDAPL-AWNVCALTHNrrgFWIKPAR---ENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 494 LDETLSSLDTARFAEVSRLLRHyVDTFKIKMILISHKTNRL-HFADHVYGITKGE 547
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRS-IAAQNVAVLFISSDLEEIeQMADRVLVMHQGE 480
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
346-496 |
2.42e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.81 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEKslQ 425
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGP--E 416
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 426 GFSVNNATQNVWqrLEQLGV-SKARLDYLRTTlsaqvgedgaNIdKLADGDRQLLLILRALLQEKDLIILDE 496
Cdd:PRK10522 417 GKPANPALVEKW--LERLKMaHKLELEDGRIS----------NL-KLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
345-515 |
2.63e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.13 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQyEGQIdySKTPISKISASEMGANVAYVSVDQSLFHVS--IEK 422
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEI--QIDGVSWNSVTLQTWRKAFGVIPQKVFIFSgtFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 423 SLQGFSvNNATQNVWQRLEQLGVsKARLDYLRTTLSAQVgEDGANIdkLADGDRQLLLILRALLQEKDLIILDETLSSLD 502
Cdd:TIGR01271 1311 NLDPYE-QWSDEEIWKVAEEVGL-KSVIEQFPDKLDFVL-VDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
170
....*....|...
gi 491954606 503 TARFAEVSRLLRH 515
Cdd:TIGR01271 1386 PVTLQIIRKTLKQ 1398
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
345-547 |
2.66e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 43.25 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEgqidyskTPISKISASemGANVAYVSVDQSLFHVSI---- 420
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-------NPNSKITVD--GITLTAKTVWDIREKVGIvfqn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 421 -EKSLQGFSVNNatqNVWQRLEQLGVSKARLDYLRTTLSAQVG------EDGANidkLADGDRQLLLILRALLQEKDLII 493
Cdd:PRK13640 93 pDNQFVGATVGD---DVAFGLENRAVPRPEMIKIVRDVLADVGmldyidSEPAN---LSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491954606 494 LDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRLHFADHVYGITKGE 547
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGK 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-438 |
2.77e-04 |
|
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: 43.77 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 341 FDHQVL-KKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIdysktpiskisasEMGANVAYVSVDQSlfhvs 419
Cdd:TIGR03719 332 FGDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-------------EIGETVKLAYVDQS----- 393
|
90
....*....|....*....
gi 491954606 420 iEKSLqgfsvnNATQNVWQ 438
Cdd:TIGR03719 394 -RDAL------DPNKTVWE 405
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
326-402 |
2.92e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 43.16 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 326 PTKPTIRLHISNLR-NFD-----------HQVLKKVD---MAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYS 390
Cdd:PRK15079 2 TEGKKVLLEVADLKvHFDikdgkqwfwqpPKTLKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL 81
|
90
....*....|..
gi 491954606 391 KTPISKISASEM 402
Cdd:PRK15079 82 GKDLLGMKDDEW 93
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
342-389 |
3.32e-04 |
|
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: 41.37 E-value: 3.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDY 389
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM 60
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
333-518 |
3.52e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.10 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNL---RNfDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKiSASEMGANVAYv 409
Cdd:PRK13538 2 LEARNLaceRD-ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRDEYHQDLLY- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 410 svdqsLFHVSIEKSL----------QGFSVNNATQNVWQRLEQLGVSKaRLDYLRTTLSAqvgedG----ANIDKLADGD 475
Cdd:PRK13538 79 -----LGHQPGIKTEltalenlrfyQRLHGPGDDEALWEALAQVGLAG-FEDVPVRQLSA-----GqqrrVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491954606 476 RQlllilrallqekdLIILDETLSSLDTARFAEVSRLLRHYVD 518
Cdd:PRK13538 148 AP-------------LWILDEPFTAIDKQGVARLEALLAQHAE 177
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
333-556 |
3.81e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 42.54 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSktpiSKISASEMGANVAYVSV- 411
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS----GRISFSSQFSWIMPGTIk 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 412 DQSLFHVSIEKsLQGFSVNNATQnvwqrLEQLGVSKARLDYlrTTLsaqvGEDGANidkLADGDRQLLLILRALLQEKDL 491
Cdd:cd03291 116 ENIIFGVSYDE-YRYKSVVKACQ-----LEEDITKFPEKDN--TVL----GEGGIT---LSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491954606 492 IILDETLSSLDTARFAEVSRLLRHYVDTFKIKmILISHKTNRLHFADHVYGITKGECVY---FSKLAD 556
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEIFESCVCKLMANKTR-ILVTSKMEHLKKADKILILHEGSSYFygtFSELQS 247
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
333-396 |
3.97e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.86 E-value: 3.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 333 LHISNLrNFDHQ---VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISK 396
Cdd:PRK13540 2 LDVIEL-DFDYHdqpLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK 67
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
342-380 |
3.98e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 42.39 E-value: 3.98e-04
10 20 30
....*....|....*....|....*....|....*....
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQ 380
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLE 51
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
346-387 |
4.81e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 42.71 E-value: 4.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEI 62
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
346-387 |
5.23e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.48 E-value: 5.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
346-402 |
5.70e-04 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 41.86 E-value: 5.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEM 402
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKEL 96
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
342-374 |
5.82e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 42.88 E-value: 5.82e-04
10 20 30
....*....|....*....|....*....|...
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAK 374
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR 402
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
343-397 |
5.84e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 41.92 E-value: 5.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 343 HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLqhqyegqIDYSKTPISKI 397
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL-------ITGDKSAGSHI 64
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
111-292 |
6.23e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 42.11 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 111 QTGDLNDRLTKDIDQCRLFCQQTLIPVWSDVIQVITIICVLFFQS------VLIGAAFtgyLLLSILVLRhvntsgndvi 184
Cdd:cd18563 98 QTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNwklallVLIPVPL---VVWGSYFFW---------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 185 PKLRK-------REAKTADFLQDVFVNnndvapmqasSRVI----------AWFNKQYDKLLPLELHAQSFIYRSWIAAL 247
Cdd:cd18563 165 KKIRRlfhrqwrRWSRLNSVLNDTLPG----------IRVVkafgqekreiKRFDEANQELLDANIRAEKLWATFFPLLT 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491954606 248 VLIAFLEVTSLALGGYSFLRGVIGLGTVYMMIDYATRIQAPLESM 292
Cdd:cd18563 235 FLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWL 279
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
337-556 |
6.57e-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: 41.55 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 337 NLRNFdhqVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEmgANVAYVSVDQSLF 416
Cdd:cd03299 9 DWKEF---KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 417 -HVSIEKSLQgFSVNNATQN-------VWQRLEQLGVSKArLDYLRTTLSAqvgedganidkladGDRQLLLILRALLQE 488
Cdd:cd03299 84 pHMTVYKNIA-YGLKKRKVDkkeierkVLEIAEMLGIDHL-LNRKPETLSG--------------GEQQRVAIARALVVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491954606 489 KDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHK-TNRLHFADHVYGITKGECVYFSKLAD 556
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
326-390 |
7.26e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 7.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491954606 326 PTKPTIRLHISN-----LRNFDH----QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQY----EGQIDYS 390
Cdd:TIGR00956 48 PTFPNALLKILTrgfrkLKKFRDtktfDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYD 125
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
345-560 |
7.58e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGlqhQYEgqidysktpiskISASEMGA--NVAYVSVDQSLFHVSIEK 422
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS---QFE------------ISEGRVWAerSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 423 SLQGFSVNNAT--QNVwQRLEQLgvsKARLDYLRTTLSAQVGEDGANidkLADGDRQLLLILRALLQEKDLIILDETLSS 500
Cdd:PTZ00243 740 NILFFDEEDAArlADA-VRVSQL---EADLAQLGGGLETEIGEKGVN---LSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 501 LDtarfAEVSRLLRHyvDTFKIKM-----ILISHKTNRLHFADHVYGITKGECVYFSKLADWAST 560
Cdd:PTZ00243 813 LD----AHVGERVVE--ECFLGALagktrVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT 871
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
329-373 |
8.38e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 8.38e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 491954606 329 PTIRLHISNL--RNfdhqvLKKVDMAIAPGQIIGLSGVSGSGKSTLA 373
Cdd:PRK00635 2 PSLPVRLSGItvRN-----LKNISIEFCPREIVLLTGVSGSGKSSLA 43
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
344-550 |
9.22e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 41.37 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPI--SKISASEMGANVAYV--SVDQSLFHVS 419
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMVfqDPDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 420 IEKSLQGFSVN------NATQNVWQRLEQLGVSKARldylrttlsaqvgedganiDK----LADGDRQLLLILRALLQEK 489
Cdd:PRK13636 100 VYQDVSFGAVNlklpedEVRKRVDNALKRTGIEHLK-------------------DKpthcLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 490 DLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRLH-FADHVYGITKGECVY 550
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVIL 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
318-409 |
9.22e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 41.31 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 318 MQsgNSPYPTKPTIRLHISNLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKI 397
Cdd:PRK10575 1 MQ--EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW 78
|
90
....*....|..
gi 491954606 398 SASEMGANVAYV 409
Cdd:PRK10575 79 SSKAFARKVAYL 90
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
344-379 |
1.08e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 1.08e-03
10 20 30
....*....|....*....|....*....|....*.
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGL 379
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV 56
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
343-388 |
1.16e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 1.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 491954606 343 HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQID 388
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD 82
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
344-534 |
1.19e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.69 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKIS---ASEMGANVAY--VSVDQSLfhv 418
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGIGIIYqeLSVIDEL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 419 SIEKSLqgFSVNNATQNVWqrleqlGV---------SKARLDYLRTTLSAQVGEDGANidkLADGDRQLLLILRALLQEK 489
Cdd:PRK09700 96 TVLENL--YIGRHLTKKVC------GVniidwremrVRAAMMLLRVGLKVDLDEKVAN---LSISHKQMLEIAKTLMLDA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491954606 490 DLIILDETLSSLDTARFAEVSRLLRHYVDTFKiKMILISHKTNRL 534
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEI 208
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
338-372 |
1.26e-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: 40.68 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|....*
gi 491954606 338 LRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTL 372
Cdd:cd03271 3 LKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSL 37
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
345-529 |
1.35e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 40.84 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKisaseMGANVAYVSVDQSLFhvsieksl 424
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-----PGAERGVVFQNEGLL-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 425 qgfSVNNATQNVWQRLEQLGVSKARLDYLRTTLSAQVGEDGAN---IDKLADGDRQLLLILRALLQEKDLIILDETLSSL 501
Cdd:PRK11248 83 ---PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEkryIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*....
gi 491954606 502 DT-ARFAEVSRLLRHYVDTFKiKMILISH 529
Cdd:PRK11248 160 DAfTREQMQTLLLKLWQETGK-QVLLITH 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
345-467 |
1.38e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASEMGANVAYVSVDQSLFHVSIEKSL 424
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 491954606 425 QGFSvNNATQNVWQRLEQLGVsKARLDYLRTTLSAQVGEDGAN 467
Cdd:PTZ00243 1405 DPFL-EASSAEVWAALELVGL-RERVASESEGIDSRVLEGGSN 1445
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
343-378 |
1.47e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.58 E-value: 1.47e-03
10 20 30
....*....|....*....|....*....|....*.
gi 491954606 343 HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVG 378
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG 49
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
342-387 |
1.56e-03 |
|
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: 40.32 E-value: 1.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI 57
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
358-377 |
1.57e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 40.21 E-value: 1.57e-03
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
346-373 |
1.57e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 1.57e-03
10 20
....*....|....*....|....*...
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLA 373
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLA 38
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-554 |
1.63e-03 |
|
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: 41.43 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSktpiSKISASEMGANVAYVSV- 411
Cdd:TIGR01271 429 LFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS----GRISFSPQTSWIMPGTIk 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 412 DQSLFHVSIEKsLQGFSVNNATQnvwqrLEQLGVSKARLDylRTTLsaqvGEDGANidkLADGDRQLLLILRALLQEKDL 491
Cdd:TIGR01271 505 DNIIFGLSYDE-YRYTSVIKACQ-----LEEDIALFPEKD--KTVL----GEGGIT---LSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491954606 492 IILDETLSSLDTARFAEV--SRLLRHYVDTFKikmILISHKTNRLHFADHVYGITKGECVY---FSKL 554
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIfeSCLCKLMSNKTR---ILVTSKLEHLKKADKILLLHEGVCYFygtFSEL 634
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
353-529 |
1.77e-03 |
|
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: 40.47 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 353 IAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDyskTPISKISASEMganvaYVSVDQSlfhVSIEKSLQGFSVNNA 432
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIE---IELDTVSYKPQ-----YIKADYE---GTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 433 TQNVWQ-------RLEQLgvskarLDYLRTTLSaqvgedGANIDKLAdgdrqlllILRALLQEKDLIILDETLSSLDTAR 505
Cdd:cd03237 91 THPYFKteiakplQIEQI------LDREVPELS------GGELQRVA--------IAACLSKDADIYLLDEPSAYLDVEQ 150
|
170 180
....*....|....*....|....
gi 491954606 506 FAEVSRLLRHYVDTFKIKMILISH 529
Cdd:cd03237 151 RLMASKVIRRFAENNEKTAFVVEH 174
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
344-550 |
1.81e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.19 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQH---QYEGQIDYSKTPiskISASEMGANVAYVSVDQSLF-HVS 419
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMP---IDAKEMRAISAYVQQDDLFIpTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 420 IEKSLQgFSV-----NNAT-----QNVWQRLEQLGVSKArldylRTTLSAQVGEdganIDKLADGDRQLLLILRALLQEK 489
Cdd:TIGR00955 116 VREHLM-FQAhlrmpRRVTkkekrERVDEVLQALGLRKC-----ANTRIGVPGR----VKGLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491954606 490 DLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRLHFA-DHVYGITKGECVY 550
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELfDKIILMAEGRVAY 247
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
346-373 |
1.85e-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: 1.85e-03
10 20
....*....|....*....|....*...
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLA 373
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSLA 39
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
308-387 |
1.98e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 40.58 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 308 NLAELERKF--VMQSGNSPYPTKPTIRLHISNLRNF--DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQY 383
Cdd:PRK13536 15 ELSPIERKHqgISEAKASIPGSMSTVAIDLAGVSKSygDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD 94
|
....
gi 491954606 384 EGQI 387
Cdd:PRK13536 95 AGKI 98
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
324-410 |
2.03e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 39.83 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 324 PYPTKPTIRLH-ISNLRNfDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKisaSEM 402
Cdd:PRK13543 5 LHTAPPLLAAHaLAFSRN-EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDR 80
|
....*...
gi 491954606 403 GANVAYVS 410
Cdd:PRK13543 81 SRFMAYLG 88
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
345-502 |
2.12e-03 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 39.80 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISAsemgANVAYVSVDQSLFHVSIEKSL 424
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSS----AAKAELRNQKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 425 QGFsvnNATQNVWQRLEQLGVSKARLDYLRTTLSAQVG-EDGAN--IDKLADGDRQLLLILRALLQEKDLIILDETLSSL 501
Cdd:PRK11629 100 PDF---TALENVAMPLLIGKKKPAEINSRALEMLAAVGlEHRANhrPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
.
gi 491954606 502 D 502
Cdd:PRK11629 177 D 177
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
342-387 |
2.21e-03 |
|
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: 40.94 E-value: 2.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 491954606 342 DHQVLKKVD---MAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:TIGR03269 293 DRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
355-387 |
2.22e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 2.22e-03
10 20 30
....*....|....*....|....*....|...
gi 491954606 355 PGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV 33
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
331-391 |
2.42e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 2.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954606 331 IRLHISNLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSK 391
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ 64
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
111-289 |
2.53e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 40.10 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 111 QTGDLNDRLTKDIDQCRLFCQQTLIPVWSDVIQVITIICVLFFQSVLIgaAFTGYLLLSILVLRHVNTSGN-DVIPKLRK 189
Cdd:cd18554 101 RSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKL--TFVSLVIFPFYILAVKYFFGRlRKLTKERS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 190 RE-AKTADFL----QDVFVnnndVAPMQASSRVIAWFNKQYDKLLPLELHAQSFIYRSWIAALVLIAFLEVTSLALGGYS 264
Cdd:cd18554 179 QAlAEVQGFLheriQGMSV----IKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYL 254
|
170 180
....*....|....*....|....*
gi 491954606 265 FLRGVIGLGTVYMMIDYATRIQAPL 289
Cdd:cd18554 255 VIEGNLTVGTLVAFVGYMERMYSPL 279
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
345-387 |
2.87e-03 |
|
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: 39.62 E-value: 2.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV 78
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
342-529 |
3.22e-03 |
|
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: 39.68 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQ------IDYSKTPISKI------SASEMGanvAYV 409
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDVWELrkriglVSPALQ---LRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 410 SVDQSLFHVsiekSLQGFsvnNATQNVWQRLEQLGVSKAR--LDYLRttlsaqvgedganIDKLAD--------Gdrqll 479
Cdd:COG1119 92 PRDETVLDV----VLSGF---FDSIGLYREPTDEQRERARelLELLG-------------LAHLADrpfgtlsqG----- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491954606 480 lilrallqEK-------------DLIILDETLSSLD-TARFaEVSRLLRHYVDTFKIKMILISH 529
Cdd:COG1119 147 --------EQrrvliaralvkdpELLILDEPTAGLDlGARE-LLLALLDKLAAEGAPTLVLVTH 201
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
346-372 |
3.23e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 3.23e-03
10 20
....*....|....*....|....*..
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTL 372
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
333-387 |
3.29e-03 |
|
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: 39.10 E-value: 3.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 491954606 333 LHISNL-RNFDHQ-VLKKVDMAIAPGqIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:cd03264 1 LQLENLtKRYGKKrALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI 56
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
342-387 |
3.66e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 39.70 E-value: 3.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 491954606 342 DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI 63
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
358-376 |
3.97e-03 |
|
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.
Pssm-ID: 238982 [Multi-domain] Cd Length: 187 Bit Score: 38.85 E-value: 3.97e-03
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
333-549 |
3.99e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 333 LHISNLRNF--DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGlQHQYE---GQIDYSKTPISKISASEMGANVA 407
Cdd:PRK09580 2 LSIKDLHVSveDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG-REDYEvtgGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 408 YVSVDqslFHVSIEKSLQGFSVNNATQNVWQRLEQLGV----------SKARL-----DYLrtTLSAQVGEDGanidkla 472
Cdd:PRK09580 81 FMAFQ---YPVEIPGVSNQFFLQTALNAVRSYRGQEPLdrfdfqdlmeEKIALlkmpeDLL--TRSVNVGFSG------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491954606 473 dGDRQLLLILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTfKIKMILISHKTNRLHF--ADHVYGITKGECV 549
Cdd:PRK09580 149 -GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYikPDYVHVLYQGRIV 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
326-420 |
4.23e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 39.55 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 326 PTKPTIRLHISNLRNF-----DHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISAS 400
Cdd:PRK09452 5 NKQPSSLSPLVELRGIsksfdGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE 84
|
90 100
....*....|....*....|...
gi 491954606 401 EMGANvayvSVDQS--LF-HVSI 420
Cdd:PRK09452 85 NRHVN----TVFQSyaLFpHMTV 103
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
345-389 |
4.39e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 38.70 E-value: 4.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 491954606 345 VLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDY 389
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKL 61
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
297-569 |
4.46e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 4.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 297 NNVQYLKG--AFANLAEL-ERKFVMQSGNSPYPTKPTIRLHISNLR-----NFDHQVLKKVDMAIAPGQIIGLSGVSGSG 368
Cdd:PTZ00265 344 NITEYMKSleATNSLYEIiNRKPLVENNDDGKKLKDIKKIQFKNVRfhydtRKDVEIYKDLNFTLTEGKTYAFVGESGCG 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 369 KSTLAKAIVGLQHQYEGQIDYSKT-PISKISASEMGANVAYVSVDQSLFHVSIE----------KSLQGFS--VNNATQN 435
Cdd:PTZ00265 424 KSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKnnikyslyslKDLEALSnyYNEDGND 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 436 VWQRLEQLGVSKARL-----DYLRTTLSA---------QVGED---------------------------GANIDKLADG 474
Cdd:PTZ00265 504 SQENKNKRNSCRAKCagdlnDMSNTTDSNeliemrknyQTIKDsevvdvskkvlihdfvsalpdkyetlvGSNASKLSGG 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 475 DRQLLLILRALLQEKDLIILDETLSSLDTARFAEVSRLLRHYVDTFKIKMILISHKTNRLHFADHVYGIT---KGECVYF 551
Cdd:PTZ00265 584 QKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSnreRGSTVDV 663
|
330
....*....|....*...
gi 491954606 552 SKLADWASTYEDEQNVKN 569
Cdd:PTZ00265 664 DIIGEDPTKDNKENNNKN 681
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
112-300 |
4.77e-03 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 39.29 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 112 TGDLNDRLTKDIDQCRLFCQQTLIPVWSDVIQVITIICVLFFQSV---LIGAAFTGYLLLSILVLRHVNTSGNDVIpklR 188
Cdd:cd18544 97 VGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWrlaLISLLVLPLLLLATYLFRKKSRKAYREV---R 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 189 KREAKTADFLQDvfvnnnDVAPMqassRVI------AWFNKQYDKLLplELHAQSFIYRSWIAALV--LIAFLEVTSLAL 260
Cdd:cd18544 174 EKLSRLNAFLQE------SISGM----SVIqlfnreKREFEEFDEIN--QEYRKANLKSIKLFALFrpLVELLSSLALAL 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491954606 261 ----GGYSFLRGVIGLGTVYMMIDYATRIQAPLE--SMQFhaNNVQ 300
Cdd:cd18544 242 vlwyGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRdlAEKF--NILQ 285
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
344-379 |
5.07e-03 |
|
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: 38.50 E-value: 5.07e-03
10 20 30
....*....|....*....|....*....|....*.
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGL 379
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL 54
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
335-388 |
5.77e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 5.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 491954606 335 ISNLRNFDHQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQID 388
Cdd:PRK13546 29 IPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
346-372 |
5.95e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 5.95e-03
10 20
....*....|....*....|....*..
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTL 372
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTL 651
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
333-401 |
6.22e-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: 38.57 E-value: 6.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491954606 333 LHISNL-RNFD-HQVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASE 401
Cdd:cd03219 1 LEVRGLtKRFGgLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE 71
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
300-372 |
6.44e-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: 39.61 E-value: 6.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491954606 300 QYLKGAFanlaELERKFVMQSGNspyptKPTIRLHISNLRNfdhqvLKKVDMAIAPGQIIGLSGVSGSGKSTL 372
Cdd:TIGR00630 592 QYLSGRK----KIEVPAERRPGN-----GKFLTLKGARENN-----LKNITVSIPLGLFTCITGVSGSGKSTL 650
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
338-545 |
6.51e-03 |
|
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: 37.72 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 338 LRNFDHqVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAI---VGLQHQYEGQIDYSKTpiskisasemGANVAYVSVDqs 414
Cdd:cd03227 4 LGRFPS-YFVPNDVTFGEGSLTIITGPNGSGKSTILDAIglaLGGAQSATRRRSGVKA----------GCIVAAVSAE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491954606 415 lFHVSIEKSLQGFSvnnatqnvwqrleqlgvSKARLdylrttlsaqvgedgANIDKLADgdrqlllilralLQEKDLIIL 494
Cdd:cd03227 71 -LIFTRLQLSGGEK-----------------ELSAL---------------ALILALAS------------LKPRPLYIL 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491954606 495 DE---TLSSLDTARFAEVsrLLRHYVDTFkiKMILISHKTNRLHFADHVYGITK 545
Cdd:cd03227 106 DEidrGLDPRDGQALAEA--ILEHLVKGA--QVIVITHLPELAELADKLIHIKK 155
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
346-373 |
6.58e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 6.58e-03
10 20
....*....|....*....|....*...
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLA 373
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSLA 43
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
111-174 |
6.87e-03 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 38.92 E-value: 6.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491954606 111 QTGDLNDRLTKDIDQCRLFCQQTLIPVWSDVIQVITIICVLFFQSVLIGAAFTGYLLLSILVLR 174
Cdd:cd18547 100 SHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTK 163
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
341-414 |
7.83e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 7.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491954606 341 FDHQVL-KKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIdysktpiskisasEMGANVAYVSVDQS 414
Cdd:PRK11819 334 FGDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-------------KIGETVKLAYVDQS 395
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
346-401 |
8.92e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 8.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491954606 346 LKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDYSKTPISKISASE 401
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE 69
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
344-387 |
9.39e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 38.17 E-value: 9.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 491954606 344 QVLKKVDMAIAPGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQI 387
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI 61
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
355-389 |
9.39e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 37.98 E-value: 9.39e-03
10 20 30
....*....|....*....|....*....|....*
gi 491954606 355 PGQIIGLSGVSGSGKSTLAKAIVGLQHQYEGQIDY 389
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY 65
|
|
| |
