|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-582 |
1.17e-169 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 495.45 E-value: 1.17e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 1 MESVDSAAARRtYLRLIEPVKGRIIGNVAIAALSSACEFVPYLAIARVaqlsITEGVPPSDV-LAMWVLVAVAGAAAGRM 79
Cdd:COG1132 1 MSKSPRKLLRR-LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRI----IDALLAGGDLsALLLLLLLLLGLALLRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 80 LFSMATGRC-HYADADFRVHVRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVY 158
Cdd:COG1132 76 LLSYLQRYLlARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 159 LFTVDVRFALLLVAYFVVVIGVAWpFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELA 238
Cdd:COG1132 156 LFVIDWRLALIVLLVLPLLLLVLR-LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 239 KACYVWTKRNGNAFSWVSALFSPGAMLVVLLAATLafVANGVLPLERCVPFLVLGVGIPAGLVNLFRSIRMLQMSLQAAD 318
Cdd:COG1132 235 RANLRAARLSALFFPLMELLGNLGLALVLLVGGLL--VLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 319 HLASVLNVAP-LAEPERPRPAAEGPVCMEFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWD 397
Cdd:COG1132 313 RIFELLDEPPeIPDPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 398 PVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLG 477
Cdd:COG1132 392 PTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 478 SEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGK 557
Cdd:COG1132 472 ERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGR 551
|
570 580
....*....|....*....|....*
gi 506241759 558 VVERGVHEELLAADGHYAALWRSQQ 582
Cdd:COG1132 552 IVEQGTHEELLARGGLYARLYRLQF 576
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
103-582 |
1.21e-112 |
|
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: 352.98 E-value: 1.21e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 103 LIEHLGKIPLGWFNDNSSAQVkQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVVIGVAW 182
Cdd:COG2274 235 FFRHLLRLPLSFFESRSVGDL-ASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 183 pFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKACYVWTKRNGNAFSWVSALFSPG 262
Cdd:COG2274 314 -LFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 263 AMLVVLLAATLafVANGVLPLERCVPFLVLGVGIPAGLVNLFRSIRMLQMSLQAADHLASVLNVAPLAEPER---PRPAA 339
Cdd:COG2274 393 TVALLWLGAYL--VIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRsklSLPRL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 340 EGPVcmEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVL 419
Cdd:COG2274 471 KGDI--ELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 SRVAVVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQ 499
Cdd:COG2274 549 RQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLR 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 500 DAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALWR 579
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
...
gi 506241759 580 SQQ 582
Cdd:COG2274 709 QQL 711
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-572 |
5.84e-98 |
|
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: 310.54 E-value: 5.84e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 7 AAARRTYLRLIEPVKGRIIGNVAIAALSSACEFVPYLAIARVAQLSITEGVPPSDVLamWVLVAVAGAAAGRMLFSMATG 86
Cdd:COG4988 2 KPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALL--PLLGLLLAVLLLRALLAWLRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 87 RC-HYADADFRVHVRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVR 165
Cdd:COG4988 80 RAaFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 166 FALLLVAyFVVVIgvawPFMMRDFG----PLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAc 241
Cdd:COG4988 160 SGLILLV-TAPLI----PLFMILVGkgaaKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKR- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 242 yvwT----KRngnAF--SWVSALFSPGAMLVVLLAATLAFVaNGVLPLERCVPFLVLGVgipaglvNLFRSIRML----- 310
Cdd:COG4988 234 ---TmkvlRV---AFlsSAVLEFFASLSIALVAVYIGFRLL-GGSLTLFAALFVLLLAP-------EFFLPLRDLgsfyh 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 311 --QMSLQAADHLASVLNVAPLAEPERPRPA-AEGPVCMEFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTT 387
Cdd:COG4988 300 arANGIAAAEKIFALLDAPEPAAPAGTAPLpAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKST 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 388 LARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVME 467
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 468 LPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHA 547
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
570 580
....*....|....*....|....*
gi 506241759 548 DQILVLVGGKVVERGVHEELLAADG 572
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
346-581 |
1.99e-97 |
|
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: 297.60 E-value: 1.99e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:cd03253 2 EFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILV 505
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 506 LDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALWRSQ 581
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
92-579 |
1.00e-95 |
|
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: 304.77 E-value: 1.00e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 92 DADFRV--HVRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVlnlhQSVGHAPVDV----TAALLSPLIPLVYLFTVDVR 165
Cdd:COG4987 81 DATLRLlaDLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV----DALDNLYLRVllplLVALLVILAAVAFLAFFSPA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 166 FALLLVAYFVVVIGVAWPFMMRdfgpLNKRFNEAMV----EVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAc 241
Cdd:COG4987 157 LALVLALGLLLAGLLLPLLAAR----LGRRAGRRLAaaraALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAA- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 242 yvwTKRNGNAFSWVSAL--FSPGAMLVVLLAATLAFVANGVLPlercVPFLVLGVGIPAGLVNLF----RSIRMLQMSLQ 315
Cdd:COG4987 232 ---QRRLARLSALAQALlqLAAGLAVVAVLWLAAPLVAAGALS----GPLLALLVLAALALFEALaplpAAAQHLGRVRA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 316 AADHLASVLNVAP-LAEPERPRPAAEGPVcMEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPR 394
Cdd:COG4987 305 AARRLNELLDAPPaVTEPAEPAPAPGGPS-LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 395 FWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDT 474
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDT 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 475 VLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLV 554
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
490 500
....*....|....*....|....*
gi 506241759 555 GGKVVERGVHEELLAADGHYAALWR 579
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
156-593 |
3.88e-93 |
|
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: 299.04 E-value: 3.88e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 156 LVYLFtvDVRFALL----LVAYFVVVIGVA-WPFMMRdfgplnKRFNEAMVEVSSAAV------EMVegiaviKTFGSRS 224
Cdd:COG5265 173 LLVKY--DWWFALItlvtVVLYIAFTVVVTeWRTKFR------REMNEADSEANTRAVdsllnyETV------KYFGNEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 225 RAGARYRAATEELAKAcyvwTKRNGNAFSWV----SALFSPGAMLVVLLAA--------TLA-FVANGVLPLERCVPFLV 291
Cdd:COG5265 239 REARRYDEALARYERA----AVKSQTSLALLnfgqALIIALGLTAMMLMAAqgvvagtmTVGdFVLVNAYLIQLYIPLNF 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 292 LGV---GIPAGLVNLFRSIRMLQMSLQAADhlasvlnvAPLAEPERPRPAAegpvcMEFEGVAFAYGENLPfVLQDVDVA 368
Cdd:COG5265 315 LGFvyrEIRQALADMERMFDLLDQPPEVAD--------APDAPPLVVGGGE-----VRFENVSFGYDPERP-ILKGVSFE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 369 LEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGAT 448
Cdd:COG5265 381 VPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDAS 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 449 DEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNAL 528
Cdd:COG5265 461 EEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV 540
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 529 AKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALWRSQQVDALEKALLVE 593
Cdd:COG5265 541 ARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALAA 605
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
346-578 |
2.00e-92 |
|
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: 284.89 E-value: 2.00e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILV 505
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241759 506 LDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALW 578
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
99-581 |
1.49e-90 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 291.24 E-value: 1.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 99 VRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVVI 178
Cdd:TIGR02203 89 IRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 179 GVAWPFMMRdFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKACYVWTKrNGNAFSWVSAL 258
Cdd:TIGR02203 169 ILMRRVSKR-LRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTS-AGSISSPITQL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 259 FSPGAMLVVLLAAtLAFVANGVLPLERCVPFLVLGVGIPAGLVNLFRSIRMLQMSLQAADHLASVLNVAP-LAEPERPRP 337
Cdd:TIGR02203 247 IASLALAVVLFIA-LFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPeKDTGTRAIE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 338 AAEGPVcmEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGE 417
Cdd:TIGR02203 326 RARGDV--EFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 418 VLSRVAVVFQDSMLLRASIADNIRLGRPG-ATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARA 496
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARA 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 497 IVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAA 576
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQ 563
|
....*
gi 506241759 577 LWRSQ 581
Cdd:TIGR02203 564 LHNMQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
346-572 |
9.85e-90 |
|
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: 277.57 E-value: 9.85e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:cd03254 4 EFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILV 505
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 506 LDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADG 572
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
346-581 |
3.22e-87 |
|
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: 271.34 E-value: 3.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGE--NLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVA 423
Cdd:cd03249 2 EFKNVSFRYPSrpDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPI 503
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 504 LVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALWRSQ 581
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
345-581 |
3.40e-75 |
|
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: 240.08 E-value: 3.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAV 424
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPIL 504
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 505 VLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALWRSQ 581
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-581 |
5.56e-73 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 245.26 E-value: 5.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 25 IGNVAIAALSSAcefVPYLaIARVAQlSITEGVPPSDVLAMWVLVAvagaaagrmLFSMATGRCHYADADFRVHVR--TV 102
Cdd:PRK13657 26 VANVLLAAATFA---EPIL-FGRIID-AISGKGDIFPLLAAWAGFG---------LFNIIAGVLVARHADRLAHRRrlAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 103 LIEHLGKI---PLGWFNDNSSAQVKQA---ATDDVLNL-------HQSvghapvdvTAALLSPLIPLVylFTVDVRFALL 169
Cdd:PRK13657 92 LTEYFERIiqlPLAWHSQRGSGRALHTllrGTDALFGLwlefmreHLA--------TLVALVVLLPLA--LFMNWRLSLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 170 LVAyFVVVIGVAWPFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFgSRSRAGAR-YRAATEELAKACYvwtkrn 248
Cdd:PRK13657 162 LVV-LGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSY-NRIEAETQaLRDIADNLLAAQM------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 249 gNAFSW---VSAL---FSPGAMLVVLLAATlAFVANGVLPLERCVPFLvlgvgipaGLVNLFRSiRMLQMS------LQA 316
Cdd:PRK13657 234 -PVLSWwalASVLnraASTITMLAILVLGA-ALVQKGQLRVGEVVAFV--------GFATLLIG-RLDQVVafinqvFMA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 317 ADHLASVLN----VAPLAEPERPRPAA--EGPVcmEFEGVAFAYGENLPFVlQDVDVALEPGTVTALVGDSGSGKTTLAR 390
Cdd:PRK13657 303 APKLEEFFEvedaVPDVRDPPGAIDLGrvKGAV--EFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 391 LIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQ 470
Cdd:PRK13657 380 LLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPD 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 471 GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQI 550
Cdd:PRK13657 460 GYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRI 539
|
570 580 590
....*....|....*....|....*....|.
gi 506241759 551 LVLVGGKVVERGVHEELLAADGHYAALWRSQ 581
Cdd:PRK13657 540 LVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
345-557 |
2.85e-72 |
|
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: 229.96 E-value: 2.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAV 424
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRASIADNIrlgrpgatdeqvqaaarqaqihdrvmelpqgydtvlgsegsdLSGGEAQRVAIARAIVQDAPIL 504
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506241759 505 VLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGK 557
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
98-581 |
1.95e-69 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 235.68 E-value: 1.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 98 HVRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVT---AALLSPLIPLVYlFTVDVRFALLLVAyf 174
Cdd:PRK11176 99 TMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVregASIIGLFIMMFY-YSWQLSLILIVIA-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 175 vVVIGVAWPFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELakacyvwtKRNGNAFSW 254
Cdd:PRK11176 176 -PIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRM--------RQQGMKMVS 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 255 VSALFSPG-------AMLVVLLAATLAFVANGVLPLERCVPFlvlgvgipAGLVNLFRSIRML-------QMSLQAADHL 320
Cdd:PRK11176 247 ASSISDPIiqliaslALAFVLYAASFPSVMDTLTAGTITVVF--------SSMIALMRPLKSLtnvnaqfQRGMAACQTL 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 321 ASVLNVaplaEPERPRPA-----AEGPVcmEFEGVAFAY-GENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPR 394
Cdd:PRK11176 319 FAILDL----EQEKDEGKrvierAKGDI--EFRNVTFTYpGKEVP-ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTR 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 395 FWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGA-TDEQVQAAARQAQIHDRVMELPQGYD 473
Cdd:PRK11176 392 FYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLD 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 474 TVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVL 553
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV 551
|
490 500
....*....|....*....|....*...
gi 506241759 554 VGGKVVERGVHEELLAADGHYAALWRSQ 581
Cdd:PRK11176 552 EDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-577 |
1.47e-63 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 222.68 E-value: 1.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 14 LRLIEPVKGRIIGNVAIAALSSACE-FVPYLaIARVAQLSITEGVPPSDVLAMWVLVAVAGAAAgrmLFSMATGRCH-YA 91
Cdd:TIGR00958 153 LGLSGRDWPWLISAFVFLTLSSLGEmFIPFY-TGRVIDTLGGDKGPPALASAIFFMCLLSIASS---VSAGLRGGSFnYT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 92 DADFRVHVRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLV 171
Cdd:TIGR00958 229 MARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 172 AYFVVVIgvawpFMMRDFGP----LNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKacyVWTKR 247
Cdd:TIGR00958 309 INLPLVF-----LAEKVFGKryqlLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQ---LNKRK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 248 N--GNAFSWVSALFSPGaMLVVLLAATLAFVANGVLPLERCVPFLVLGVGIPAGLVNLFRSIRMLQMSLQAADHLASVLN 325
Cdd:TIGR00958 381 AlaYAGYLWTTSVLGML-IQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLD 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 326 VAPLAEPE---RPRPAaEGPVcmEFEGVAFAYGE--NLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVS 400
Cdd:TIGR00958 460 RKPNIPLTgtlAPLNL-EGLI--EFQDVSFSYPNrpDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 401 GSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEG 480
Cdd:TIGR00958 536 GQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 481 SDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNalAKGRTTVVIAHRLDTIVHADQILVLVGGKVVE 560
Cdd:TIGR00958 616 SQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
570
....*....|....*..
gi 506241759 561 RGVHEELLAADGHYAAL 577
Cdd:TIGR00958 694 MGTHKQLMEDQGCYKHL 710
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
111-583 |
3.38e-61 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 213.81 E-value: 3.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 111 PLGWFNDNSSAQVKQAATDD---VLNLHQSVgHAPVDVTAALLSPLipLVYLFTVDVRFALLLVAYFVVVIGVAWPFMmR 187
Cdd:PRK10790 112 PLSAFDTQPVGQLISRVTNDtevIRDLYVTV-VATVLRSAALIGAM--LVAMFSLDWRMALVAIMIFPAVLVVMVIYQ-R 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 188 DFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAcyvwtkrngnafsWVSALFSPGAMLVV 267
Cdd:PRK10790 188 YSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMA-------------RMQTLRLDGFLLRP 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 268 LLAATLAFVANGVLPLERCVPFLVLGVGIPAGLVN-----------LFRSIRMLQMSLQAADHLASVLNVAPLAEPERPR 336
Cdd:PRK10790 255 LLSLFSALILCGLLMLFGFSASGTIEVGVLYAFISylgrlneplieLTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 337 PAAEGPVcmEFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASG 416
Cdd:PRK10790 335 PLQSGRI--DIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 417 EVLSRVAVVFQDSMLLRASIADNIRLGRPgATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARA 496
Cdd:PRK10790 412 VLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 497 IVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAA 576
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQ 570
|
....*..
gi 506241759 577 LWRSQQV 583
Cdd:PRK10790 571 MYQLQLA 577
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
45-553 |
6.62e-61 |
|
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: 211.38 E-value: 6.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 45 IARVAQLSITEGVPPSDVLamWVLVAVAGAAAGRMLFSMATGR-CHYADADFRVHVRTVLIEHLGKIPLGWFNDNSSAQV 123
Cdd:TIGR02857 26 LARVVDGLISAGEPLAELL--PALGALALVLLLRALLGWLQERaAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 124 KQAATDDVLNLhqsVGHA----PVDVTAALLsPLIPLVYLFTVDVRFALLLVAYFVVVIGvawpFMM---RDFGPLNKRF 196
Cdd:TIGR02857 104 ATLALEGVEAL---DGYFarylPQLVLAVIV-PLAILAAVFPQDWISGLILLLTAPLIPI----FMIligWAAQAAARKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 197 NEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKACyVWTKRNgnAF--SWVSALFSpgAMLVVLLAATLA 274
Cdd:TIGR02857 176 WAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERT-MRVLRI--AFlsSAVLELFA--TLSVALVAVYIG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 275 F-VANGVLPLERCVPFLVLGVGIPAGLVNLFRSIRMLQMSLQAADHLASVLNVAPLAEPE-RPRPAAEGPVcMEFEGVAF 352
Cdd:TIGR02857 251 FrLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGkAPVTAAPASS-LEFSGVSV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 353 AYgENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLL 432
Cdd:TIGR02857 330 AY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 RASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAH 512
Cdd:TIGR02857 409 AGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 506241759 513 ADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVL 553
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
92-580 |
1.62e-59 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 208.97 E-value: 1.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 92 DADFRVHVR--TVLIEHLGKI---PLGWFNDNSSAQVKQA---ATDDVLNLHQSVGHAPVDVTAALLSpLIPLVylFTVD 163
Cdd:TIGR01192 79 EADRLAHGRraTLLTEAFGRIismPLSWHQQRGTSNALHTllrATETLFGLWLEFMRQHLATFVALFL-LIPTA--FAMD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 164 VRFALLLVAYFVVVIGVAWPFMMRdfgplnKRFNEAMVE-----VSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELA 238
Cdd:TIGR01192 156 WRLSIVLMVLGILYILIAKLVMQR------TKNGQAAVEhhyhnVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 239 KACYV----WTKRNGnafswVSALFSPGAMLVVLLAATLaFVANGVLPLERCVPFLvlgvgipaGLVNLF--RSIRMLQM 312
Cdd:TIGR01192 230 SAQYPvldwWALASG-----LNRMASTISMMCILVIGTV-LVIKGELSVGEVIAFI--------GFANLLigRLDQMSGF 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 313 SLQAADHLASVLNVAPLAEP--ERPRPAAEGPV-----CMEFEGVAFAYGENLPFVlQDVDVALEPGTVTALVGDSGSGK 385
Cdd:TIGR01192 296 ITQIFEARAKLEDFFDLEDSvfQREEPADAPELpnvkgAVEFRHITFEFANSSQGV-FDVSFEAKAGQTVAIVGPTGAGK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 386 TTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRV 465
Cdd:TIGR01192 375 TTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFI 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 466 MELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIV 545
Cdd:TIGR01192 455 LKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVR 534
|
490 500 510
....*....|....*....|....*....|....*
gi 506241759 546 HADQILVLVGGKVVERGVHEELLAADGHYAALWRS 580
Cdd:TIGR01192 535 NADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
192-590 |
3.41e-59 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 208.03 E-value: 3.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 192 LNKRFNEAMVEVSS---AAVEMVEGIAVIKTFGSRSRAGARYRA-ATEELAKACYVwtkrngnafSWVSALFSPGAMLVV 267
Cdd:PRK10789 161 LHERFKLAQAAFSSlndRTQESLTSIRMIKAFGLEDRQSALFAAdAEDTGKKNMRV---------ARIDARFDPTIYIAI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 268 LLAATLA------FVANGVLPLERCVPFLV-LGVGIPAGLVnLFRSIRMLQMSLQAADHLASVLNVAP-LAEPERPRPAA 339
Cdd:PRK10789 232 GMANLLAigggswMVVNGSLTLGQLTSFVMyLGLMIWPMLA-LAWMFNIVERGSAAYSRIRAMLAEAPvVKDGSEPVPEG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 340 EGPVCMEFEgvAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVL 419
Cdd:PRK10789 311 RGELDVNIR--QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 SRVAVVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQ 499
Cdd:PRK10789 389 SRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 500 DAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALWR 579
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
410
....*....|.
gi 506241759 580 SQQvdaLEKAL 590
Cdd:PRK10789 549 YQQ---LEAAL 556
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
140-579 |
9.99e-59 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 209.41 E-value: 9.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 140 HAPVDVTAALLSPLIPLVYL---FTVDVRFALLLVAyFVVVIGVAWPFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAV 216
Cdd:TIGR03796 266 FLSGQLATTALDAVMLVFYAllmLLYDPVLTLIGIA-FAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIET 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 217 IKTFGSRSRAGAR---YRAATEELAKACYVWTKRNGNAFSWVSALfspGAMLVVLLAATLafVANGVLPLERCVPFLVLG 293
Cdd:TIGR03796 345 LKASGLESDFFSRwagYQAKLLNAQQELGVLTQILGVLPTLLTSL---NSALILVVGGLR--VMEGQLTIGMLVAFQSLM 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 294 VGIPA---GLVNLFRSIRMLQMSLqaaDHLASVLN--VAPLAEPERPRPAAEGPVC-----MEFEGVAFAYGENLPFVLQ 363
Cdd:TIGR03796 420 SSFLEpvnNLVGFGGTLQELEGDL---NRLDDVLRnpVDPLLEEPEGSAATSEPPRrlsgyVELRNITFGYSPLEPPLIE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 364 DVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLG 443
Cdd:TIGR03796 497 NFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLW 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 444 RPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQK 523
Cdd:TIGR03796 577 DPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDD 656
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 524 ALNAlaKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALWR 579
Cdd:TIGR03796 657 NLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
346-558 |
1.17e-57 |
|
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: 193.46 E-value: 1.17e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYgENLP--FVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVA 423
Cdd:cd03248 13 KFQNVTFAY-PTRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPI 503
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 504 LVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKV 558
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-541 |
7.06e-56 |
|
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: 197.97 E-value: 7.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 11 RTYLRLIEPVKGRIIGNVAIAALSS----ACEFVPYLAIARVAQLsitegvPPsdvlamwVLVAVAGAAAGRMlFSMATG 86
Cdd:TIGR02868 2 LRILPLLKPRRRRLALAVLLGALALgsavALLGVSAWLISRAAEM------PP-------VLYLSVAAVAVRA-FGIGRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 87 RCHYA------DADFRV--HVRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVY 158
Cdd:TIGR02868 68 VFRYLerlvghDAALRSlgALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 159 LFTVDVRFALLLVAYFVVVIGVAWPFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELA 238
Cdd:TIGR02868 148 IAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 239 KAcyvwTKRNGNAFSWVSALFSPGAMLVVLLAATLAfvANGVLPLERCVPFLVLGVGIPAGLVNLFR----SIRMLQMSL 314
Cdd:TIGR02868 228 RA----ERRAAAATALGAALTLLAAGLAVLGALWAG--GPAVADGRLAPVTLAVLVLLPLAAFEAFAalpaAAQQLTRVR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 315 QAADHLASVLNVA-PLAEPERPRPAAEGP--VCMEFEGVAFAYGENlPFVLQDVDVALEPGTVTALVGDSGSGKTTLARL 391
Cdd:TIGR02868 302 AAAERIVEVLDAAgPVAEGSAPAAGAVGLgkPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 392 IPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQG 471
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDG 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 472 YDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRL 541
Cdd:TIGR02868 461 LDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
104-577 |
6.90e-55 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 198.81 E-value: 6.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 104 IEHLGKIPLGWFNDNSSAQVKQAATDdvlnlHQSVGHAPVDVTAALLSPLIPLVYLFTVDVR-----FALLLVA---YFV 175
Cdd:TIGR01193 236 IKHLFELPMSFFSTRRTGEIVSRFTD-----ASSIIDALASTILSLFLDMWILVIVGLFLVRqnmllFLLSLLSipvYAV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 176 VVigvaWPFMmRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSragARYRAATEE----LAKA-CYVWTKRNGN 250
Cdd:TIGR01193 311 II----ILFK-RTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEA---ERYSKIDSEfgdyLNKSfKYQKADQGQQ 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 251 AFSWVSALfspgAMLVVLLAATLAFVANGVLPLERCVPFLVLgvgiPAGLVNLFRSIRMLQMSLQAADHLASVLNVAPLA 330
Cdd:TIGR01193 383 AIKAVTKL----ILNVVILWTGAYLVMRGKLTLGQLITFNAL----LSYFLTPLENIINLQPKLQAARVANNRLNEVYLV 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 331 EPE----RPRPAAEGPVC-MEFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRM 405
Cdd:TIGR01193 455 DSEfinkKKRTELNNLNGdIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 406 NGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLG-RPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLS 484
Cdd:TIGR01193 534 NGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSIS 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 485 GGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALaKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVH 564
Cdd:TIGR01193 614 GGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSH 692
|
490
....*....|...
gi 506241759 565 EELLAADGHYAAL 577
Cdd:TIGR01193 693 DELLDRNGFYASL 705
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
149-581 |
1.45e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 192.35 E-value: 1.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 149 LLSPL------IPLVYLFT--VDVRFALLLVAyFVVVIGVAWPFMmrdFGPLNKRFNEAMVEVSS----AAVEMVEGIAV 216
Cdd:PRK11160 137 LISPLvaalvvILVLTIGLsfFDLTLALTLGG-ILLLLLLLLPLL---FYRLGKKPGQDLTHLRAqyrvQLTEWLQGQAE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 217 IKTFGsrsrAGARYRAATEELAKACYVWTKRNGNafswVSALfSPGAMLV---VLLAATLAFVANGVLplercvpflvlG 293
Cdd:PRK11160 213 LTLFG----AEDRYRQQLEQTEQQWLAAQRRQAN----LTGL-SQALMILangLTVVLMLWLAAGGVG-----------G 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 294 VGIPAGLVNLF-----RSIRMLqMSLQAA-DHLASVLNVAP------LAEPERPRPAAEGP----VCMEFEGVAFAYGEN 357
Cdd:PRK11160 273 NAQPGALIALFvfaalAAFEAL-MPVAGAfQHLGQVIASARrineitEQKPEVTFPTTSTAaadqVSLTLNNVSFTYPDQ 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 358 LPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIA 437
Cdd:PRK11160 352 PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLR 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 438 DNIRLGRPGATDEQVQAAARQAQIhDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPEN 517
Cdd:PRK11160 432 DNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506241759 518 ETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALWRSQ 581
Cdd:PRK11160 511 ERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
308-570 |
1.57e-53 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 192.27 E-value: 1.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 308 RMLQMSLQAADHLASVLNVAPLAEPERPRPAAEGPVcmEFEGVAFAY-GENLPfVLQDVDVALEPGTVTALVGDSGSGKT 386
Cdd:COG4618 296 KQFVSARQAYRRLNELLAAVPAEPERMPLPRPKGRL--SVENLTVVPpGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 387 TLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNI-RLGrpGATDEQVQAAARQAQIHDRV 465
Cdd:COG4618 373 TLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMI 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 466 MELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNAL-AKGRTTVVIAHRLDTI 544
Cdd:COG4618 451 LRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLL 530
|
250 260
....*....|....*....|....*.
gi 506241759 545 VHADQILVLVGGKVVERGVHEELLAA 570
Cdd:COG4618 531 AAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
316-584 |
1.04e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 185.05 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 316 AADHLASVLNvAPLAEPERPR--PAAEGPVCMEFEG-VAFAY-GENLpfvLQDVDVALEPGTVTALVGDSGSGKTTLARL 391
Cdd:PRK11174 320 AAESLVTFLE-TPLAHPQQGEkeLASNDPVTIEAEDlEILSPdGKTL---AGPLNFTLPAGQRIALVGPSGAGKTSLLNA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 392 IPRFWdPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQG 471
Cdd:PRK11174 396 LLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 472 YDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQIL 551
Cdd:PRK11174 475 LDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIW 554
|
250 260 270
....*....|....*....|....*....|...
gi 506241759 552 VLVGGKVVERGVHEELLAADGHYAALWRSQQVD 584
Cdd:PRK11174 555 VMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
346-562 |
5.73e-50 |
|
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: 172.77 E-value: 5.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:cd03245 4 EFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILV 505
Cdd:cd03245 84 PQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 506 LDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERG 562
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
346-558 |
8.25e-48 |
|
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: 165.08 E-value: 8.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLLRASIADNIrlgrpgatdeqvqaaarqaqihdrvmelpqgydtvlgsegsdLSGGEAQRVAIARAIVQDAPILV 505
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 506 LDEATAHADPENETAIQKALNAL-AKGRTTVVIAHRLDTIVHADQILVLVGGKV 558
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
152-570 |
4.78e-47 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 173.69 E-value: 4.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 152 PLIP--LVYLFTVDVRFALLLVAYFVVVIGVAWpfmmrdfgpLNKRFN-----EAMVEVSSA---AVEMVEGIAVIKTFG 221
Cdd:TIGR01842 127 PWMPiyLLVCFLLHPWIGILALGGAVVLVGLAL---------LNNRATkkplkEATEASIRAnnlADSALRNAEVIEAMG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 222 SRSRAGARYRAATEELAKACYVWTKRNG--NAFSWV------SALFSPGAMLVVLLAATLAFVANGVLPLERCV-PFlvl 292
Cdd:TIGR01842 198 MMGNLTKRWGRFHSKYLSAQSAASDRAGmlSNLSKYfrivlqSLVLGLGAYLAIDGEITPGMMIAGSILVGRALaPI--- 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 293 gvgipAGLVNLFRSIrmlQMSLQAADHLASVLNVAPLAEPERPRPAAEGPVcmEFEGVAFAYGENLPFVLQDVDVALEPG 372
Cdd:TIGR01842 275 -----DGAIGGWKQF---SGARQAYKRLNELLANYPSRDPAMPLPEPEGHL--SVENVTIVPPGGKKPTLRGISFSLQAG 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 373 TVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGATDEQV 452
Cdd:TIGR01842 345 EALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKI 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 453 QAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNAL-AKG 531
Cdd:TIGR01842 425 IEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARG 504
|
410 420 430
....*....|....*....|....*....|....*....
gi 506241759 532 RTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAA 570
Cdd:TIGR01842 505 ITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
345-562 |
7.61e-47 |
|
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: 164.20 E-value: 7.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAV 424
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRASIADNIR-LGRpgATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPI 503
Cdd:cd03244 83 IPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 504 LVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERG 562
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
346-569 |
3.01e-41 |
|
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: 149.40 E-value: 3.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:COG1122 2 ELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQ--DSMLLRASIADNI-----RLGRPGATdeqvqaaarqaqIHDRVME-LpqgydTVLGSEG------SDLSGGEAQRV 491
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVafgpeNLGLPREE------------IRERVEEaL-----ELVGLEHladrppHELSGGQKQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 492 AIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIA-HRLDTIV-HADQILVLVGGKVVERGVHEELLA 569
Cdd:COG1122 144 AIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAeLADRVIVLDDGRIVADGTPREVFS 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
345-571 |
2.41e-40 |
|
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: 147.50 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAV 424
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSML-LRASIADNIRLGR---------PGATDEQVQaaarqaqihDRVMELpqgydtvLGSEG------SDLSGGEA 488
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAV---------EEALER-------TGLEHladrpvDELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 489 QRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLD-TIVHADQILVLVGGKVVERGVHE 565
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPE 223
|
....*.
gi 506241759 566 ELLAAD 571
Cdd:COG1120 224 EVLTPE 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
346-557 |
7.15e-40 |
|
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: 144.92 E-value: 7.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQ--DSMLLRASIADNI-----RLGRPGATdeqvqaaarqaqIHDRVMELPQgydtVLGSEG------SDLSGGEAQRVA 492
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVafgleNLGLPEEE------------IEERVEEALE----LVGLEGlrdrspFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 493 IARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIA-HRLDTIV-HADQILVLVGGK 557
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLeLADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
314-573 |
7.72e-40 |
|
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: 152.75 E-value: 7.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 314 LQAADHLASVLNVAPLAEPERPRPAAEGPVcMEFEGVAFAYGENLP---FVLQDVDVALEPGTVTALVGDSGSGKTTLAR 390
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPL-LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 391 LIPRFWDPVSGSVRMNGTELPQMASGEVL---SRVAVVFQD--SML-----LRASIADNIRLGRPGATDEqvqaaarqaq 460
Cdd:COG1123 310 LLLGLLRPTSGSILFDGKDLTKLSRRSLRelrRRVQMVFQDpySSLnprmtVGDIIAEPLRLHGLLSRAE---------- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 461 IHDRVME------LPQGYDTVLGSEgsdLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GR 532
Cdd:COG1123 380 RRERVAEllervgLPPDLADRYPHE---LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGL 456
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 506241759 533 TTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH 573
Cdd:COG1123 457 TYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
345-562 |
2.20e-39 |
|
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: 142.45 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTElPQMASGEVLSRVAV 424
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP-VSDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRASIADNirLGRPgatdeqvqaaarqaqihdrvmelpqgydtvlgsegsdLSGGEAQRVAIARAIVQDAPIL 504
Cdd:cd03247 80 LNQRPYLFDTTLRNN--LGRR-------------------------------------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 505 VLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERG 562
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
346-557 |
2.03e-38 |
|
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: 138.92 E-value: 2.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQdsmllrasiadnirlgrpgatdeqvqaaarqaqihdrvmelpqgydtvlgsegsdLSGGEAQRVAIARAIVQDAPILV 505
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 506 LDEATAHADPENETAIQKALNALA-KGRTTVVIAHRLDTIVHA-DQILVLVGGK 557
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
345-567 |
2.18e-38 |
|
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: 141.55 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWD-----PVSGSVRMNGTEL--PQMASGE 417
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 418 VLSRVAVVFQDSMLLRASIADNIRLG-------RPGATDEQVQAAARQAQIHDRVMElpqgydtvlGSEGSDLSGGEAQR 490
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKD---------RLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 491 VAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAH------RLdtivhADQILVLVGGKVVERGVH 564
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFGPT 224
|
...
gi 506241759 565 EEL 567
Cdd:cd03260 225 EQI 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
346-571 |
5.66e-38 |
|
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: 140.50 E-value: 5.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGE---VLSRV 422
Cdd:COG1127 7 EVRNLTKSFGDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQ-----DSMllraSIADNIRLG---RPGATDEQvqaaarqaqIHDRVME------LPqgydtvlGSEG---SDLSG 485
Cdd:COG1127 85 GMLFQggalfDSL----TVFENVAFPlreHTDLSEAE---------IRELVLEklelvgLP-------GAADkmpSELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 486 GEAQRVAIARAIVQDAPILVLDEATAHADPENETAI-------QKALNAlakgrTTVVIAHRLDTIVH-ADQILVLVGGK 557
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITSAVIdelirelRDELGL-----TSVVVTHDLDSAFAiADRVAVLADGK 219
|
250
....*....|....
gi 506241759 558 VVERGVHEELLAAD 571
Cdd:COG1127 220 IIAEGTPEELLASD 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
346-558 |
6.67e-37 |
|
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: 136.85 E-value: 6.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLP--FVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEvLSR-- 421
Cdd:cd03255 2 ELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE-LAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 ---VAVVFQDSMLL-RASIADNIRL-----GRPGATDeqvqaaarqaqiHDRVMELPqgydTVLGSEG------SDLSGG 486
Cdd:cd03255 81 rrhIGFVFQSFNLLpDLTALENVELplllaGVPKKER------------RERAEELL----ERVGLGDrlnhypSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506241759 487 EAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVHADQILVLVGGKV 558
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
350-570 |
1.26e-36 |
|
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: 137.24 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 350 VAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDS 429
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 430 ML-------LRASIADNIRL-GRPGATDEQVQAAarqaqihDRVmELPQGYdtvLGSEGSDLSGGEAQRVAIARAIVQDA 501
Cdd:COG1124 89 YAslhprhtVDRILAEPLRIhGLPDREERIAELL-------EQV-GLPPSF---LDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 502 PILVLDEATAHADPENETAIQKALNAL--AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAA 570
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLreERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
346-562 |
2.80e-36 |
|
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: 134.10 E-value: 2.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQdsMLLRASIADnirlgrpgatdeqvqaaarqaqIHDRVMelpqgydtvlgsegSDLSGGEAQRVAIARAIVQDAPILV 505
Cdd:cd03214 79 PQ--ALELLGLAH----------------------LADRPF--------------NELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 506 LDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIV-HADQILVLVGGKVVERG 562
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNLAArYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
346-571 |
5.88e-36 |
|
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: 134.94 E-value: 5.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS---RV 422
Cdd:cd03261 2 ELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQDSMLLRA-SIADNI--RLGRPGATDEqvqaaarqAQIHDRVMElpqGYDTVlGSEG------SDLSGGEAQRVAI 493
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVafPLREHTRLSE--------EEIREIVLE---KLEAV-GLRGaedlypAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 494 ARAIVQDAPILVLDEATAHADPENETAIQKALNAL--AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAA 570
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
.
gi 506241759 571 D 571
Cdd:cd03261 228 D 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
349-562 |
6.23e-36 |
|
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: 134.56 E-value: 6.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 349 GVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR---VAVV 425
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRrkeIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSML-------LRASIADNIRLGRPGATDEQVQAAARQAQIHdrvMELPqgyDTVLGSEGSDLSGGEAQRVAIARAIV 498
Cdd:cd03257 88 FQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLLVG---VGLP---EEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 499 QDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
346-560 |
2.35e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.87 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS---RV 422
Cdd:COG2884 3 RFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQDSMLL--RaSIADNIRL-----GRPGAtdeqvqaaarqaQIHDRVMElpqgydtVLGSEG---------SDLSGG 486
Cdd:COG2884 82 GVVFQDFRLLpdR-TVYENVALplrvtGKSRK------------EIRRRVRE-------VLDLVGlsdkakalpHELSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 487 EAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIA-HRLDtIVHA--DQILVLVGGKVVE 560
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
362-511 |
6.32e-35 |
|
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: 129.30 E-value: 6.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLL-RASIADNI 440
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 441 RLGRPGATDEQVQAAARQAQIHDRVmELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATA 511
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
346-577 |
1.37e-34 |
|
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: 137.73 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDP---VSGSVRMNGTELPQMASGEVLSRV 422
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQDSM--LLRASIADNIRLGrpgatdeQVQAAARQAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIV 498
Cdd:COG1123 86 GMVFQDPMtqLNPVTVGDQIAEA-------LENLGLSRAEARARVLELLEavGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 499 QDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGHYA 575
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQALA 238
|
..
gi 506241759 576 AL 577
Cdd:COG1123 239 AV 240
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
346-558 |
2.62e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 129.55 E-value: 2.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:COG4619 2 ELEGLSFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLLRASIADNIRlgRPGATDEQVQAAARQAQIHDRVmELPqgyDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILV 505
Cdd:COG4619 80 PQEPALWGGTVRDNLP--FPFQLRERKFDRERALELLERL-GLP---PDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 506 LDEATAHADPENETAIQKALNALA--KGRTTVVIAHRLDTIVH-ADQILVLVGGKV 558
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
290-553 |
3.05e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 139.78 E-value: 3.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 290 LVLGVGIPAGLVNL-FRSIRMLQMSLQAADHLASVLNVAPLAEPERPRPAAEGPVCMEFEGVAFAYGENLPF-VLQDVDV 367
Cdd:PTZ00265 327 ILLGVLISMFMLTIiLPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVeIYKDLNF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 368 ALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTE-LPQMASGEVLSRVAVVFQDSMLLRASIADNIR----- 441
Cdd:PTZ00265 407 TLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslys 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 442 ----------LGRPGAT------------------------------------------DEQVQAAARQAQIHDRVMELP 469
Cdd:PTZ00265 487 lkdlealsnyYNEDGNDsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVSALP 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 470 QGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALA--KGRTTVVIAHRLDTIVHA 547
Cdd:PTZ00265 567 DKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYA 646
|
....*.
gi 506241759 548 DQILVL 553
Cdd:PTZ00265 647 NTIFVL 652
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
345-562 |
1.16e-33 |
|
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: 127.53 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAV 424
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRASIADNI-RLGRpgATDEqvqaaarqaqihdrvmelpQGYDTVLGSE-GSDLSGGEAQRVAIARAIVQDAP 502
Cdd:cd03369 87 IPQDPTLFSGTIRSNLdPFDE--YSDE-------------------EIYGALRVSEgGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 503 ILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERG 562
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
346-571 |
2.81e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.90 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELpqmasGEVLSRVAVV 425
Cdd:COG1121 8 ELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLLR---ASIADNIRLG---------RPGATDeqvqaaarqaqiHDRVME-LpqgyDTVlGSEG------SDLSGG 486
Cdd:COG1121 81 PQRAEVDWdfpITVRDVVLMGrygrrglfrRPSRAD------------REAVDEaL----ERV-GLEDladrpiGELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 487 EAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIV-HADQILVLVGGKVVErGVH 564
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPP 222
|
....*..
gi 506241759 565 EELLAAD 571
Cdd:COG1121 223 EEVLTPE 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
345-560 |
5.83e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 126.31 E-value: 5.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAY--GENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEV---- 418
Cdd:COG1136 5 LELRNLTKSYgtGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 419 LSRVAVVFQDSMLL-RASIADNIRL-----GRPGATDEqvqaaarqaqihDRVMELpqgydtvLGSEG---------SDL 483
Cdd:COG1136 85 RRHIGFVFQFFNLLpELTALENVALplllaGVSRKERR------------ERAREL-------LERVGlgdrldhrpSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 484 SGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVHADQILVLVGGKVVE 560
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
143-579 |
6.17e-33 |
|
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: 135.84 E-value: 6.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 143 VDVTAALLSPLIPLVY--LFTVDVRFALLLVA--YFVVVI---GVAWPFMMRdFGPLNKRFNEAMVEVSSAAV-----EM 210
Cdd:TIGR00957 1072 LDTVDSMIPPVIKMFMgsLFNVIGALIVILLAtpIAAVIIpplGLLYFFVQR-FYVASSRQLKRLESVSRSPVyshfnET 1150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 211 VEGIAVIKTFGSRSRAGARYRAATEELAKACYVWTKRNgnafSWVSALFSPGAMLVVLLAATLAFVANGVLPlercvPFL 290
Cdd:TIGR00957 1151 LLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVAN----RWLAVRLECVGNCIVLFAALFAVISRHSLS-----AGL 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 291 VlGVGIPAGLVNLFRSIRMLQMSLQAADHLASVLNVAPLAEPER--------PRPAAEGPVC--MEFEGVAFAYGENLPF 360
Cdd:TIGR00957 1222 V-GLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKeapwqiqeTAPPSGWPPRgrVEFRNYCLRYREDLDL 1300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNI 440
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 441 RlgrPGA--TDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENE 518
Cdd:TIGR00957 1381 D---PFSqySDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 519 TAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALWR 579
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
345-562 |
9.14e-32 |
|
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: 122.63 E-value: 9.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEvlSRVAV 424
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLL-RASIADNIRLG-RPGATDEqvqaaarqAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQD 500
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFGlKLRGVPK--------AEIRARVRELLElvGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 501 APILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
346-570 |
1.40e-31 |
|
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: 122.69 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFV--LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVL---S 420
Cdd:cd03258 3 ELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRkarR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 RVAVVFQDSMLLRA-SIADNIRL-----GRPGAtdeqvqaaarqaQIHDRVMELPQgydtVLGSEG------SDLSGGEA 488
Cdd:cd03258 83 RIGMIFQHFNLLSSrTVFENVALpleiaGVPKA------------EIEERVLELLE----LVGLEDkadaypAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 489 QRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHE 565
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 506241759 566 ELLAA 570
Cdd:cd03258 227 EVFAN 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
345-557 |
2.75e-31 |
|
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: 120.65 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGEN---LPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGtelpqmasgevlsR 421
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 VAVVFQDSMLLRASIADNIRLGRPgaTDEQVqaaarqaqiHDRVME----------LPQGYDTVLGSEGSDLSGGEAQRV 491
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP--FDEER---------YEKVIKacalepdleiLPDGDLTEIGEKGINLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 492 AIARAIVQDAPILVLDEATAHADPENETAI-QKALN-ALAKGRTTVVIAHRLDTIVHADQILVLVGGK 557
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
346-570 |
6.19e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 120.94 E-value: 6.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASgEVLSRVAVV 425
Cdd:COG1131 2 EVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSML-LRASIADNIRL-----GRPGATDEqvqaaarqaqihDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAI 497
Cdd:COG1131 79 PQEPALyPDLTVRENLRFfarlyGLPRKEAR------------ERIDELLElfGLTDAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 498 VQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIA-HRLDTIVH-ADQILVLVGGKVVERGVHEELLAA 570
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
348-559 |
8.13e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 119.67 E-value: 8.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 348 EGVAFAYGENlPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGtelPQMASGEVLSRVAVVFQ 427
Cdd:cd03226 3 ENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 428 DS--MLLRASIADNIRLGRPGATDEQVQAAAR--QAQIHDRVMELPQgydtvlgsegsDLSGGEAQRVAIARAIVQDAPI 503
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVlkDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 504 LVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIVH-ADQILVLVGGKVV 559
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
346-553 |
1.84e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 118.79 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELpqmasGEVLSRVAVV 425
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLLR---ASIADNIRLGR---------PGATDEqvqaaarqaqihDRVMELpqgYDTVLGSEGSD-----LSGGEA 488
Cdd:cd03235 74 PQRRSIDRdfpISVRDVVLMGLyghkglfrrLSKADK------------AKVDEA---LERVGLSELADrqigeLSGGQQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 489 QRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNAL-AKGRTTVVIAHRLDTIV-HADQILVL 553
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLeYFDRVLLL 205
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
354-582 |
1.90e-30 |
|
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: 120.01 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 354 YGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLR 433
Cdd:cd03288 29 YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 434 ASIADNIRLGRPgATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHA 513
Cdd:cd03288 109 GSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 514 DPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLA-ADGHYAALWRSQQ 582
Cdd:cd03288 188 DMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGVFASLVRTDK 257
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
345-557 |
3.50e-30 |
|
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: 116.90 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR--V 422
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRrrI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQDSMLL-RASIADNIRLGrpgatdeqvqaaarqaqihdrvmelpqgydtvlgsegsdLSGGEAQRVAIARAIVQDA 501
Cdd:cd03229 79 GMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 502 PILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGK 557
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
346-589 |
5.88e-30 |
|
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: 119.07 E-value: 5.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTE------LPqmasgEVL 419
Cdd:TIGR04520 2 EVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtldeenLW-----EIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 SRVAVVFQ--DSMLLRASIADNI-----RLGRPgaTDEqvqaaarqaqIHDRV--------MElpqGYdtvLGSEGSDLS 484
Cdd:TIGR04520 77 KKVGMVFQnpDNQFVGATVEDDVafgleNLGVP--REE----------MRKRVdealklvgME---DF---RDREPHLLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 485 GGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVHADQILVLVGGKVVERG 562
Cdd:TIGR04520 139 GGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
|
250 260
....*....|....*....|....*..
gi 506241759 563 VHEELLAadghyaalwrsqQVDALEKA 589
Cdd:TIGR04520 219 TPREIFS------------QVELLKEI 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
345-574 |
1.40e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 125.14 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAY--GENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWD------------------------- 397
Cdd:PTZ00265 1166 IEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 398 -----------------------------PVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIRLGRPGAT 448
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 449 DEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNAL 528
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 529 AK--GRTTVVIAHRLDTIVHADQILVL-----VGGKVVERGVHEELLAA-DGHY 574
Cdd:PTZ00265 1405 KDkaDKTIITIAHRIASIKRSDKIVVFnnpdrTGSFVQAHGTHEELLSVqDGVY 1458
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
345-561 |
5.08e-29 |
|
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: 114.88 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPF--VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPqmasgEVLSRV 422
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQDSMLL--RaSIADNIRLG---RPGATDEqvqaaarqaqIHDRVMELpqgYDTV--LGSEG---SDLSGGEAQRVA 492
Cdd:cd03293 76 GYVFQQDALLpwL-TVLDNVALGlelQGVPKAE----------ARERAEEL---LELVglSGFENaypHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506241759 493 IARAIVQDAPILVLDEATAHADPENETAIQKAL-NALAKGRTTVV-IAHRLDTIVH-ADQILVL--VGGKVVER 561
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELlDIWRETGKTVLlVTHDIDEAVFlADRVVVLsaRPGRIVAE 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
345-558 |
1.34e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 113.66 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEV--LSR- 421
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpyLRRk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 VAVVFQDSMLL-RASIADNIRL-----GRPGatdeqvqaaarqAQIHDRVMELPQgydtVLGSEG------SDLSGGEAQ 489
Cdd:cd03292 80 IGVVFQDFRLLpDRNVYENVAFalevtGVPP------------REIRKRVPAALE----LVGLSHkhralpAELSGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 490 RVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIV--HADQILVLVGGKV 558
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVdtTRHRVIALERGKL 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
346-568 |
2.02e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.70 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQ--DSMLLRASIADNIRLGrpgatdeQVQAAARQAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDA 501
Cdd:PRK13632 89 FQnpDNQFIGATVEDDIAFG-------LENKKVPPKKMKDIIDDLAKkvGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 502 PILVLDEATAHADPENETAIQKALNALAKGRTTVVIA--HRLDTIVHADQILVLVGGKVVERGVHEELL 568
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
361-562 |
2.95e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.95 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVL---SRVAVVFQDSMLLRA-SI 436
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 ADNIRL-----GRPGATdeqvqaaarqaqIHDRVMELpqgYDTVlGSEG------SDLSGGEAQRVAIARAIVQDAPILV 505
Cdd:COG1135 100 AENVALpleiaGVPKAE------------IRKRVAEL---LELV-GLSDkadaypSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241759 506 LDEATAHADPENETAIqkaLNALAK-----GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:COG1135 164 CDEATSALDPETTRSI---LDLLKDinrelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
345-567 |
2.97e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.51 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGS---VRMNGTELPQMASGEVLSR 421
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 VAVVFQ--DSMLLRASIADNIRLGrpgATDEQVQAAARQAQIHDRVMELpqGYDTVLGSEGSDLSGGEAQRVAIARAIVQ 499
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFG---LENRAVPRPEMIKIVRDVLADV--GMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 500 DAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEEL 567
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
346-559 |
5.25e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 112.84 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVL---SRV 422
Cdd:COG3638 4 ELRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQDSMLL-RASIADNI---RLGRPGA--------TDEQVQAAARQAqihDRVMELPQGYDTVlgsegSDLSGGEAQR 490
Cdd:COG3638 83 GMIFQQFNLVpRLSVLTNVlagRLGRTSTwrsllglfPPEDRERALEAL---ERVGLADKAYQRA-----DQLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 491 VAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIV-HADQILVLVGGKVV 559
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARrYADRIIGLRDGRVV 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
346-567 |
6.01e-28 |
|
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: 112.66 E-value: 6.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGE---VLSRV 422
Cdd:cd03256 2 EVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQDSMLL-RASIADNIRLGRPGATDEQVQAAARQAQIH--------DRVmelpqGYDTVLGSEGSDLSGGEAQRVAI 493
Cdd:cd03256 81 GMIFQQFNLIeRLSVLENVLSGRLGRRSTWRSLFGLFPKEEkqralaalERV-----GLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 494 ARAIVQDAPILVLDEATAHADPENETAIQKALNALA--KGRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEEL 567
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
346-569 |
7.65e-28 |
|
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: 111.76 E-value: 7.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR-VAV 424
Cdd:cd03224 2 EVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLL-RASIADNIRLGRPGATDEQVQAAArqaqihDRVMEL-PQgYDTVLGSEGSDLSGGEAQRVAIARAIVQDAP 502
Cdd:cd03224 80 VPEGRRIFpELTVEENLLLGAYARRRAKRKARL------ERVYELfPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 503 ILVLDEATAHADPENETAIQKALNALAKGRTTVVIA-HRLDTIV-HADQILVLVGGKVVERGVHEELLA 569
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVeQNARFALeIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
346-558 |
9.37e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 109.79 E-value: 9.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQmASGEVLSRVAVV 425
Cdd:cd03230 2 EVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLL-RASIADNIRLgrpgatdeqvqaaarqaqihdrvmelpqgydtvlgsegsdlSGGEAQRVAIARAIVQDAPIL 504
Cdd:cd03230 79 PEEPSLYeNLTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 505 VLDEATAHADPENETAIQKALNALAKGRTTVVIA-HRLDTIVH-ADQILVLVGGKV 558
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
346-569 |
9.94e-28 |
|
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: 112.01 E-value: 9.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENlPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVV 425
Cdd:cd03295 2 EFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLL-RASIADNIRL-----GRPGATdeqvqaaarqaqIHDRVMEL-------PQGYdtvLGSEGSDLSGGEAQRVA 492
Cdd:cd03295 81 IQQIGLFpHMTVEENIALvpkllKWPKEK------------IRERADELlalvgldPAEF---ADRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 493 IARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLD-TIVHADQILVLVGGKVVERGVHEELLA 569
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
346-573 |
1.68e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 111.00 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGEnLPFvlqDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEvlsR-VAV 424
Cdd:COG3840 3 RLDDLTYRYGD-FPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSML---LraSIADNIRLG-RPG----ATDeqvqaaarqaqiHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIA 494
Cdd:COG3840 76 LFQENNLfphL--TVAQNIGLGlRPGlkltAEQ------------RAQVEQALErvGLAGLLDRLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 495 RAIVQDAPILVLDEATAHADPenetaiqkAL--------NALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGV 563
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDP--------ALrqemldlvDELCRerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
|
250
....*....|
gi 506241759 564 HEELLAADGH 573
Cdd:COG3840 214 TAALLDGEPP 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
345-571 |
2.00e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.03 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAV 424
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQ--DSMLLRASIADNIRLG---RPGATDEqvqaaaRQAQIHDRVMELpqGYDTVLGSEGSDLSGGEAQRVAIARAIVQ 499
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGlenIGVPREE------MVERVDQALRQV--GMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506241759 500 DAPILVLDEATAHADPENETAIQKALNAL-AKGRTTVV-IAHRLDTIVHADQILVLVGGKVVERGVHEELLAAD 571
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLkEQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
265-572 |
1.10e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 116.38 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 265 LVVLLAATLAFVANGvlPLERCVPF-------LVLGVGIPAGLVNLFRSIRMLQMSLQAADHLASVLNV---APLA-EPE 333
Cdd:PLN03130 1149 LMIWLTASFAVMQNG--RAENQAAFastmgllLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLpseAPLViENN 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 334 RPRPAAEGPVCMEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQM 413
Cdd:PLN03130 1227 RPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF 1306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 414 ASGEVLSRVAVVFQDSMLLRASIADNIRlgrPGA--TDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRV 491
Cdd:PLN03130 1307 GLMDLRKVLGIIPQAPVLFSGTVRFNLD---PFNehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLL 1383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 492 AIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAAD 571
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNE 1463
|
.
gi 506241759 572 G 572
Cdd:PLN03130 1464 G 1464
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
265-572 |
2.63e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 115.07 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 265 LVVLLAATLAFVANGvlPLERCVPF-------LVLGVGIPAGLVNLFRSIRMLQMSLQAADHLASVLNVAPLAEP--ERP 335
Cdd:PLN03232 1146 VMIWLTATFAVLRNG--NAENQAGFastmgllLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAiiENN 1223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 336 RPAAEGPV--CMEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQM 413
Cdd:PLN03232 1224 RPVSGWPSrgSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF 1303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 414 ASGEVLSRVAVVFQDSMLLRASIADNIRlgrPGA--TDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRV 491
Cdd:PLN03232 1304 GLTDLRRVLSIIPQSPVLFSGTVRFNID---PFSehNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLL 1380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 492 AIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAAD 571
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
.
gi 506241759 572 G 572
Cdd:PLN03232 1461 T 1461
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
361-568 |
1.49e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.97 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMaSGEVLSRV-AVVFQDSMLLRA-SIAD 438
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAW-SPWELARRrAVLPQHSSLAFPfTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRLGR-PGATDEQVQAAarqaqIHDRVMELPQgydtVLGSEGSD---LSGGEAQRVAIARAIVQ-------DAPILVLD 507
Cdd:COG4559 95 VVALGRaPHGSSAAQDRQ-----IVREALALVG----LAHLAGRSyqtLSGGEQQRVQLARVLAQlwepvdgGPRWLFLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 508 EATAHADPENETAIQKALNALAKGRTTVVIahrldtIVH--------ADQILVLVGGKVVERGVHEELL 568
Cdd:COG4559 166 EPTSALDLAHQHAVLRLARQLARRGGGVVA------VLHdlnlaaqyADRILLLHQGRLVAQGTPEEVL 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
361-580 |
1.54e-25 |
|
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: 107.45 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDP---VSGSVRMNGTELPQMaSGEVL-----SRVAVVFQDSM-- 430
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKL-SEKELrkirgREIQMIFQDPMts 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 431 ---LLR--ASIADNIRLGRPGATDEqvqaaarqaqIHDRVME------LPQGYDtVLGS---EgsdLSGGEAQRVAIARA 496
Cdd:COG0444 99 lnpVMTvgDQIAEPLRIHGGLSKAE----------ARERAIEllervgLPDPER-RLDRyphE---LSGGMRQRVMIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 497 IVQDAPILVLDEATahadpeneTA----IQKA-LNALAK-----GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHE 565
Cdd:COG0444 165 LALEPKLLIADEPT--------TAldvtIQAQiLNLLKDlqrelGLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVE 236
|
250
....*....|....*..
gi 506241759 566 ELLAADGH-Y-AALWRS 580
Cdd:COG0444 237 ELFENPRHpYtRALLSS 253
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
362-569 |
3.07e-25 |
|
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: 105.42 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS----RVAVVFQDSMLL-RASI 436
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 ADNIRL-----GRPGATDEQVQAaarqaqihdRVMELP--QGYDTVLGSEgsdLSGGEAQRVAIARAIVQDAPILVLDEA 509
Cdd:cd03294 120 LENVAFglevqGVPRAEREERAA---------EALELVglEGWEHKYPDE---LSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241759 510 TAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLA 569
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAelQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
346-553 |
3.41e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.17 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAY---GENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPqmasgEVLSRV 422
Cdd:COG1116 9 ELRGVSKRFptgGGGVT-ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQDSMLL--RaSIADNIRLGRPGATdeqvqaaARQAQIHDRVMELpqgYDTV--LGSEG---SDLSGGEAQRVAIAR 495
Cdd:COG1116 83 GVVFQEPALLpwL-TVLDNVALGLELRG-------VPKAERRERAREL---LELVglAGFEDaypHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 496 AIVQDAPILVLDEATAHADPENETAIQKALNAL--AKGRTTVVIAHRLDTIVH-ADQILVL 553
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFlADRVVVL 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
346-567 |
5.23e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.72 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEvlsR-VAV 424
Cdd:COG3842 7 ELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK---RnVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSML---LraSIADNI-----RLGRPGATdeqvqaaarqaqIHDRVMELpqgYDTV-LGSEG----SDLSGGEAQRV 491
Cdd:COG3842 82 VFQDYALfphL--TVAENVafglrMRGVPKAE------------IRARVAEL---LELVgLEGLAdrypHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 492 AIARAIVQDAPILVLDEATAHADPE--NET-----AIQKALnalakGRTTVVIAH-RLDTIVHADQILVLVGGKVVERGV 563
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKlrEEMreelrRLQREL-----GITFIYVTHdQEEALALADRIAVMNDGRIEQVGT 219
|
....
gi 506241759 564 HEEL 567
Cdd:COG3842 220 PEEI 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
360-568 |
1.66e-24 |
|
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: 102.41 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 360 FVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEvlSRVAVVFQDSMLL-RASIAD 438
Cdd:cd03299 13 FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFpHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRLGrpgatdeQVQAAARQAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPE 516
Cdd:cd03299 91 NIAYG-------LKKRKVDKKEIERKVLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 517 NETAIQKALNALAKGRTTVVI--AHRLDTI-VHADQILVLVGGKVVERGVHEELL 568
Cdd:cd03299 164 TKEKLREELKKIRKEFGVTVLhvTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
345-562 |
1.90e-24 |
|
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: 101.42 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGEnLPFvlqDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTElpqMASGEVLSR-VA 423
Cdd:cd03298 1 VRLDKIRFSYGE-QPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD---VTAAPPADRpVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQDSMLL-RASIADNIRLGRPGATDEQVQAAARQAQIHDRVmelpqGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAP 502
Cdd:cd03298 74 MLFQENNLFaHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARV-----GLAGLEKRLPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241759 503 ILVLDEATAHADPENETAIQKALNAL--AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-573 |
2.88e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.30 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWD-----PVSGSVRMNGTELPQMASGEVLSRVAVVFQ-DSMLLRA 434
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 435 SIADNIRLGRpgatdEQVQAAARQAQIHDRV---MELPQGYDTV---LGSEGSDLSGGEAQRVAIARAIVQDAPILVLDE 508
Cdd:PRK14247 98 SIFENVALGL-----KLNRLVKSKKELQERVrwaLEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 509 ATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH 573
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
346-570 |
5.60e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 100.84 E-value: 5.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL--PQMASGEVLSRVA 423
Cdd:COG1126 3 EIENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQD-----SMllraSIADNIRLG----RPGATDEqvqaaarqaqIHDRVMELpqgydtvLGSEG---------SDLSG 485
Cdd:COG1126 81 MVFQQfnlfpHL----TVLENVTLApikvKKMSKAE----------AEERAMEL-------LERVGladkadaypAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 486 GEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLD---TIvhADQILVLVGGKVVER 561
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKeGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEE 217
|
....*....
gi 506241759 562 GVHEELLAA 570
Cdd:COG1126 218 GPPEEFFEN 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
361-569 |
6.24e-24 |
|
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: 100.59 E-value: 6.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR-VAVVFQDSMLLRA-SIAD 438
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRLGRPGATDEQVQAAARQAQ---IHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHA 513
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREereARERAEELLErvGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 514 DPENETAIQKALNALA-KGRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEELLA 569
Cdd:cd03219 175 NPEETEELAELIRELReRGITVLLVEHDMDVVMsLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
346-562 |
9.44e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 102.96 E-value: 9.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFV--LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS--- 420
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 RVAVVFQDSMLLRA-SIADNIRL-----GRPGAtdeqvqaaarqaQIHDRVMELpqgYDTVLGSEGSD-----LSGGEAQ 489
Cdd:PRK11153 83 QIGMIFQHFNLLSSrTVFDNVALplelaGTPKA------------EIKARVTEL---LELVGLSDKADrypaqLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 490 RVAIARAIVQDAPILVLDEATAHADPENETAIqkaLNALAK-----GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSI---LELLKDinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
150-590 |
9.69e-24 |
|
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: 106.95 E-value: 9.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 150 LSPLIPLVYLFTVDVRFALllvaYFV-------VVIGVAWPFMMRdfgPLN-------KRFNEAMVEVSSAAV----EMV 211
Cdd:TIGR00957 431 LATYINMIWSAPLQVILAL----YFLwlnlgpsVLAGVAVMVLMV---PLNavmamktKTYQVAHMKSKDNRIklmnEIL 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 212 EGIAVIKTFGSRSRAGARYRAATEE----LAKACYVWTKrngNAFSWVSalfSPGAMLVVLLAATLAFVANGVLPLERCV 287
Cdd:TIGR00957 504 NGIKVLKLYAWELAFLDKVEGIRQEelkvLKKSAYLHAV---GTFTWVC---TPFLVALITFAVYVTVDENNILDAEKAF 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 288 PFLVLG--VGIPAGLV-NLFRSIRMLQMSLQAADHLASVLNVAPLAEPERPRPAAEGpVCMEFEGVAFAYGENLPFVLQD 364
Cdd:TIGR00957 578 VSLALFniLRFPLNILpMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEG-NSITVHNATFTWARDLPPTLNG 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 365 VDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTelpqmasgevlsrVAVVFQDSMLLRASIADNIRLGR 444
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGK 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 445 PGATDEQVQAAARQAQIHDRVMeLPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKA 524
Cdd:TIGR00957 724 ALNEKYYQQVLEACALLPDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 525 L---NALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYAALWRSQQVDALEKAL 590
Cdd:TIGR00957 803 VigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHL 871
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
361-571 |
1.38e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.23 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRA-SIADN 439
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPfTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 440 IRLGR-PGATDEqvqaaARQAQIHDRVMELPQgydtVLGSEGSD---LSGGEAQRVAIARAIVQ------DAPILVLDEA 509
Cdd:PRK13548 97 VAMGRaPHGLSR-----AEDDALVAAALAQVD----LAHLAGRDypqLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 510 TAHADPENETAIQKALNALAKGRTTVVIA--HRLD-TIVHADQILVLVGGKVVERGVHEELLAAD 571
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHERGLAVIVvlHDLNlAARYADRIVLLHQGRLVADGTPAEVLTPE 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
336-567 |
2.39e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.73 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 336 RPAAEGPVCMEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWD--P---VSGSVRMNGTEL 410
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 411 --PQMASGEVLSRVAVVFQDSMLLRASIADNI----RLGrpGATDEQVqaaarqaqIHDRVMELPQG---YDTV---LGS 478
Cdd:COG1117 81 ydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVayglRLH--GIKSKSE--------LDEIVEESLRKaalWDEVkdrLKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 479 EGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALaKGRTTVVI-------AHRLdtivhADQIL 551
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIvthnmqqAARV-----SDYTA 224
|
250
....*....|....*.
gi 506241759 552 VLVGGKVVERGVHEEL 567
Cdd:COG1117 225 FFYLGELVEFGPTEQI 240
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
361-568 |
5.17e-23 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 99.11 E-value: 5.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQM--ASGEVLSR-VAVVFQDS-------M 430
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrKQRRAFRRdVQLVFQDSpsavnprM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 431 LLRASIADNIR-LGRPGATDEQVQAAARQaqihdRVMELPqgyDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEA 509
Cdd:TIGR02769 106 TVRQIIGEPLRhLTSLDESEQKARIAELL-----DMVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 510 TAHADPENETAIQKALNAL--AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELL 568
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLqqAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLL 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
345-569 |
6.88e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.32 E-value: 6.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPF---VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVL-- 419
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 --SRVAVVFQ--DSMLLRASIADNIRLGrP---GATDEQVQAAArqaqihDRVMELPQGYDTVLGSEGSDLSGGEAQRVA 492
Cdd:PRK13634 83 lrKKVGIVFQfpEHQLFEETVEKDICFG-PmnfGVSEEDAKQKA------REMIELVGLPEELLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 493 IARAIVQDAPILVLDEATAHADPENETAIQKALNAL--AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
345-553 |
7.34e-23 |
|
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: 96.78 E-value: 7.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQmASGEVLSRVAV 424
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRA-SIADNIRL-----GRPGATDEQvqaaarqaqihDRVMEL--PQGYDTVLGSEgsdLSGGEAQRVAIARA 496
Cdd:COG4133 80 LGHADGLKPElTVRENLRFwaalyGLRADREAI-----------DEALEAvgLAGLADLPVRQ---LSAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 497 IVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVL 553
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDL 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
361-567 |
8.85e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.02 E-value: 8.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR-VAVVFQDSMLLRA-SIAD 438
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRLGRPGATdeqvqaaarQAQIHDRVM---------ELpqGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEA 509
Cdd:COG1129 99 NIFLGREPRR---------GGLIDWRAMrrrarellaRL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 510 TAhADPENETAI-QKALNAL-AKGRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEEL 567
Cdd:COG1129 168 TA-SLTEREVERlFRIIRRLkAQGVAIIYISHRLDEVFeIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
331-567 |
1.42e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 103.32 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 331 EPERPRPAAEGPV---CMEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNG 407
Cdd:PTZ00243 1292 EPASPTSAAPHPVqagSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 408 TELPQMASGEVLSRVAVVFQDSMLLRASIADNIrlgRP--GATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSG 485
Cdd:PTZ00243 1372 REIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSV 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 486 GEAQRVAIARAIVQ-DAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVH 564
Cdd:PTZ00243 1449 GQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSP 1528
|
...
gi 506241759 565 EEL 567
Cdd:PTZ00243 1529 REL 1531
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
353-568 |
1.71e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.01 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 353 AYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQ----- 427
Cdd:PRK11231 11 GYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQhhltp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 428 DSMLLRASIA-----DNIRLGRPGATDEQVQaaarqaqihDRVMELPQgYDTVLGSEGSDLSGGEAQRVAIARAIVQDAP 502
Cdd:PRK11231 89 EGITVRELVAygrspWLSLWGRLSAEDNARV---------NQAMEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 503 ILVLDEATAHADPENETAIQKALNAL-AKGRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEELL 568
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASrYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
348-588 |
2.52e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.43 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 348 EGVAFAYGENLPF---VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL--PQMASGEVLSRV 422
Cdd:PRK13637 6 ENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQ--DSMLLRASIADNIRLG--RPGATDEQvqaaarqaqIHDRV---MELPQ-GYDTVLGSEGSDLSGGEAQRVAIA 494
Cdd:PRK13637 86 GLVFQypEYQLFEETIEKDIAFGpiNLGLSEEE---------IENRVkraMNIVGlDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 495 RAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLaad 571
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVF--- 233
|
250
....*....|....*..
gi 506241759 572 ghyaalwrsQQVDALEK 588
Cdd:PRK13637 234 ---------KEVETLES 241
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
346-559 |
3.20e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.61 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENlpFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEvlsR-VAV 424
Cdd:COG3839 5 ELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---RnIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQD-----SMllraSIADNI----RL-GRPGATdeqvqaaarqaqIHDRVMELPQgydtVLGSEG------SDLSGGEA 488
Cdd:COG3839 80 VFQSyalypHM----TVYENIafplKLrKVPKAE------------IDRRVREAAE----LLGLEDlldrkpKQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 489 QRVAIARAIVQDAPILVLDEATAHADPE--NET-----AIQKALNAlakgrTTVVIAHrlD-----TIvhADQILVLVGG 556
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDAKlrVEMraeikRLHRRLGT-----TTIYVTH--DqveamTL--ADRIAVMNDG 210
|
...
gi 506241759 557 KVV 559
Cdd:COG3839 211 RIQ 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
346-569 |
3.25e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 95.82 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR-VAV 424
Cdd:COG0410 5 EVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRA-SIADNIRLGRPGATDEQVQAAARqaqihDRVMEL-PqgydtVL----GSEGSDLSGGEAQRVAIARAIV 498
Cdd:COG0410 83 VPEGRRIFPSlTVEENLLLGAYARRDRAEVRADL-----ERVYELfP-----RLkerrRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 499 QDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVI----AHR-LDtivHADQILVLVGGKVVERGVHEELLA 569
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLveqnARFaLE---IADRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
345-567 |
4.01e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 96.36 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAV 424
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSmllrasiaDNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTV-----LGSEGSDLSGGEAQRVAIARAIVQ 499
Cdd:PRK13648 88 VFQNP--------DNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVdmlerADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 500 DAPILVLDEATAHADPENETAIQKALNALA--KGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEEL 567
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
360-562 |
4.26e-22 |
|
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: 94.15 E-value: 4.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 360 FVLQDVDVALEPGTVTALVGDSGSGKTTLARLIP--RFWDPVSGSVRMNGTELPQMASGevlSRVAVVFQDSMLLrasia 437
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRSFR---KIIGYVPQDDILH----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 438 dnirlgrpgatdeqvqaaarqaqihdrvmelpqGYDTV-----LGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAH 512
Cdd:cd03213 95 ---------------------------------PTLTVretlmFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506241759 513 ADPENETAIQKALNALAK-GRTTVVIAHRLDTIVHA--DQILVLVGGKVVERG 562
Cdd:cd03213 142 LDSSSALQVMSLLRRLADtGRTIICSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
346-559 |
5.55e-22 |
|
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: 92.88 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPqmasgevlsrvavv 425
Cdd:cd03216 2 ELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 fqdsmllRASIADNIRLGrpgatdeqvqaaarQAQIHdrvmelpQgydtvlgsegsdLSGGEAQRVAIARAIVQDAPILV 505
Cdd:cd03216 66 -------FASPRDARRAG--------------IAMVY-------Q------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 506 LDEATAHADPENETAIQKALNAL-AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVV 559
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLrAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
348-562 |
8.86e-22 |
|
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: 93.80 E-value: 8.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 348 EGVAFAYGENLpfVLQDVDVALEPGtVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASgEVLSRVAVVFQ 427
Cdd:cd03264 4 ENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 428 D-----SMLLRASIADNIRLGRPGATDEQVQAaarqaqihDRVMELPQGYDtVLGSEGSDLSGGEAQRVAIARAIVQDAP 502
Cdd:cd03264 80 EfgvypNFTVREFLDYIAWLKGIPSKEVKARV--------DEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 503 ILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTI-VHADQILVLVGGKVVERG 562
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
345-571 |
1.24e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.38 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTL----ARLIPrfwdPVSGSVRMNGTELPQMASGEVLS 420
Cdd:COG4604 2 IEIKNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLlsmiSRLLP----PDSGEVLVDGLDVATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 RVAVvfqdsmlLRASIADNIRL---------------GRPGATDEQvqaaarqaqIHDRVME------LPQGY-DTvlgs 478
Cdd:COG4604 76 RLAI-------LRQENHINSRLtvrelvafgrfpyskGRLTAEDRE---------IIDEAIAyldledLADRYlDE---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 479 egsdLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALA--KGRTTVVIAHRLD-TIVHADQILVLVG 555
Cdd:COG4604 136 ----LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKD 211
|
250
....*....|....*.
gi 506241759 556 GKVVERGVHEELLAAD 571
Cdd:COG4604 212 GRVVAQGTPEEIITPE 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
346-558 |
1.27e-21 |
|
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: 93.36 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQ--MASGEVLSRVA 423
Cdd:cd03262 2 EIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQDSMLL-RASIADNIRL------GRPGATDEqvqaaarqaqihDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIA 494
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLapikvkGMSKAEAE------------ERALELLEkvGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 495 RAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIVH-ADQILVLVGGKV 558
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
362-573 |
1.88e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 95.57 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS---RVAVVFQDS-------ML 431
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDPyaslnprMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 432 LRASIADNIRLGRPGATDEQVqaaarqaqihDRVMELpqgYDTV-LGSEGSD-----LSGGEAQRVAIARAIVQDAPILV 505
Cdd:COG4608 114 VGDIIAEPLRIHGLASKAERR----------ERVAEL---LELVgLRPEHADrypheFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 506 LDEATAHADpeneTAIQ-KALNALAK-----GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH 573
Cdd:COG4608 181 CDEPVSALD----VSIQaQVLNLLEDlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARPLH 251
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
346-567 |
1.96e-21 |
|
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: 93.46 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEvlSRVAVV 425
Cdd:cd03300 2 ELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLL-RASIADNI-----RLGRPGATdeqvqaaarqaqIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAI 497
Cdd:cd03300 78 FQNYALFpHLTVFENIafglrLKKLPKAE------------IKERVAEALDlvQLEGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241759 498 VQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAH-RLDTIVHADQILVLVGGKVVERGVHEEL 567
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
330-570 |
2.22e-21 |
|
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: 97.83 E-value: 2.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 330 AEPER--PRPAAEGPVCMEFEG--VAFAYGENL------PFV-LQDVDVALEPGTVTALVGDSGSGKTTLA----RLIPR 394
Cdd:COG4172 259 AEPRGdpRPVPPDAPPLLEARDlkVWFPIKRGLfrrtvgHVKaVDGVSLTLRRGETLGLVGESGSGKSTLGlallRLIPS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 395 fwdpvSGSVRMNGTELPQMASGEVL---SRVAVVFQD---SMLLRASIADNI----RLGRPGATDEQvqaaarqaqIHDR 464
Cdd:COG4172 339 -----EGEIRFDGQDLDGLSRRALRplrRRMQVVFQDpfgSLSPRMTVGQIIaeglRVHGPGLSAAE---------RRAR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 465 VMElpqgydtVLGSEGSD----------LSGGEAQRVAIARAIVQDAPILVLDEATAHADpeneTAIQKA-LNALAK--- 530
Cdd:COG4172 405 VAE-------ALEEVGLDpaarhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDLLRDlqr 473
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 506241759 531 --GRTTVVIAHRLdTIVHA--DQILVLVGGKVVERGVHEELLAA 570
Cdd:COG4172 474 ehGLAYLFISHDL-AVVRAlaHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
346-567 |
2.29e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 93.36 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR-VAV 424
Cdd:TIGR03410 2 EVSNLNVYYGQSH--ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLL-RASIADNIRLG---RPGATDEqvqaaarqaqIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQD 500
Cdd:TIGR03410 80 VPQGREIFpRLTVEENLLTGlaaLPRRSRK----------IPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 501 APILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEEL 567
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
361-560 |
2.30e-21 |
|
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: 93.27 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQM---ASGEVLSR-VAVVFQDSMLLRASI 436
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARhVGFVFQSFQLLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 A-DNIRL-----GRPGATDEQVQAAarqaqihDRVmelpqGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEAT 510
Cdd:COG4181 107 AlENVMLplelaGRRDARARARALL-------ERV-----GLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506241759 511 AHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVHADQILVLVGGKVVE 560
Cdd:COG4181 175 GNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
361-553 |
3.05e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTelpqmasgevlSRVAVVFQDSML---LRASIA 437
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEVpdsLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 438 DNIRLGRPGATDEQVQAAARQAQIHDRVMElPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPEN 517
Cdd:NF040873 76 DLVAMGRWARRGLWRRLTRDDRAAVDDALE-RVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 506241759 518 ETAIQKALNAL-AKGRTTVVIAHRLDTIVHADQILVL 553
Cdd:NF040873 155 RERIIALLAEEhARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
128-570 |
3.17e-21 |
|
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: 97.56 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 128 TDDVLNLHQSVGHAPVDVTAALLSpLIPLVYLFTVDVRFALLLVAYFVVVIGVAWPFMMRdfgpLNKRFNEAMVEVSS-- 205
Cdd:COG4615 112 TEDVRTISQAFVRLPELLQSVALV-LGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRR----ARRHLRRAREAEDRlf 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 206 AAVE-MVEGIAVIKtfGSRSRagaRYRAATEELAKACYVWTKRNGNAFSWVSALFSPGAMLVVLLAATLAFVANGVLPLE 284
Cdd:COG4615 187 KHFRaLLEGFKELK--LNRRR---RRAFFDEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWAD 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 285 RCVPFLVLGVGI----P-AGLVNLFRSIRMLQMSLQAADHLASVL-NVAPLAEPERPRPAAEGPVCMEFEGVAFAY---G 355
Cdd:COG4615 262 PAVLSGFVLVLLflrgPlSQLVGALPTLSRANVALRKIEELELALaAAEPAAADAAAPPAPADFQTLELRGVTYRYpgeD 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 356 ENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRas 435
Cdd:COG4615 342 GDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-- 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 436 iadniRL-GRPGATDEqvqaaarqaqihDRV------MELpqgyDTVLGSEG-----SDLSGGEAQRVAIARAIVQDAPI 503
Cdd:COG4615 420 -----RLlGLDGEADP------------ARArellerLEL----DHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPI 478
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 504 LVLDEATAHADPEN-ETAIQKALNAL-AKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAA 570
Cdd:COG4615 479 LVFDEWAADQDPEFrRVFYTELLPELkARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
364-582 |
4.58e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 95.18 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 364 DVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS----RVAVVFQDSMLL-RASIAD 438
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpekrRIGYVFQEARLFpHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRLGRPGATDEQVQAAArqaqihDRVMELpQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENE 518
Cdd:TIGR02142 95 NLRYGMKRARPSERRISF------ERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 519 TAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEElLAADGHYAALWRSQQ 582
Cdd:TIGR02142 168 YEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAE-VWASPDLPWLAREDQ 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
345-568 |
5.21e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.64 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFV---LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGE---- 417
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 418 VLSRVAVVFQ--DSMLLRASIADNIRLGRP--GATDEQVQAaarqaqIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAI 493
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQnfGIPKEKAEK------IAAEKLEMVGLADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 494 ARAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEELL 568
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDVF 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
362-559 |
8.99e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 8.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL----PQ--MASGevlsrVAVVFQDSMLLRA- 434
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirsPRdaIALG-----IGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 435 SIADNIRLGRPGAtdeqVQAAARQAQIHDRVMELPQGY------DTVLGsegsDLSGGEAQRVAIARAIVQDAPILVLDE 508
Cdd:COG3845 96 TVAENIVLGLEPT----KGGRLDRKAARARIRELSERYgldvdpDAKVE----DLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 509 ATAHADPEnETAI-QKALNALAK-GRTTVVIAHRLDTIV-HADQILVLVGGKVV 559
Cdd:COG3845 168 PTAVLTPQ-EADElFEILRRLAAeGKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
345-562 |
1.13e-20 |
|
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: 90.78 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNG---TELPQMASGevlsr 421
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvTDLPPKDRD----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 VAVVFQDSMLL-RASIADNIRLG---RPGATDEqvqaaarqaqIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIAR 495
Cdd:cd03301 74 IAMVFQNYALYpHMTVYDNIAFGlklRKVPKDE----------IDERVREVAEllQIEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 496 AIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAH-RLDTIVHADQILVLVGGKVVERG 562
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
307-560 |
1.64e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 307 IRMLQ-MSLQAADHLASVLNVApLAEPERPrpaaeGPVCMEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGK 385
Cdd:COG0488 283 IKALEkLEREEPPRRDKTVEIR-FPPPERL-----GKKVLELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 386 TTLARLIPRFWDPVSGSVRMnGTELpqmasgevlsRVAVVFQDSMLLR--ASIADNIRLGRPGATDeqvqaaarqaqIHD 463
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKL-GETV----------KIGYFDQHQEELDpdKTVLDELRDGAPGGTE-----------QEV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 464 RvmelpqgydTVLGSEG----------SDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALaKGrT 533
Cdd:COG0488 413 R---------GYLGRFLfsgddafkpvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-T 481
|
250 260 270
....*....|....*....|....*....|
gi 506241759 534 TVVIAH-R--LDTIvhADQILVLVGGKVVE 560
Cdd:COG0488 482 VLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
360-587 |
1.91e-20 |
|
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: 93.24 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 360 FVLqDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS----RVAVVFQDSMLL-RA 434
Cdd:COG4148 14 FTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPphrrRIGYVFQEARLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 435 SIADNIRLGRPGATDEQVQAAarqaqiHDRVMELpqgydtvLGSEG------SDLSGGEAQRVAIARAIVQDAPILVLDE 508
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRIS------FDEVVEL-------LGIGHlldrrpATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 509 ATAHADPENETAIQKALNALAK-GRTTVV-IAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGHYAALWRSQQVDA 585
Cdd:COG4148 160 PLAALDLARKAEILPYLERLRDeLDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSV 239
|
..
gi 506241759 586 LE 587
Cdd:COG4148 240 LE 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
343-562 |
2.56e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 90.87 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 343 VCMEFEGVAfaygenlpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR- 421
Cdd:COG0411 10 LTKRFGGLV---------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 VAVVFQDSMLLRA-SIADNIRLGRPGATDEQVQAAARQAQ--------IHDRVMELPQ--GYDTVLGSEGSDLSGGEAQR 490
Cdd:COG0411 81 IARTFQNPRLFPElTVLENVLVAAHARLGRGLLAALLRLPrarreereARERAEELLErvGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 491 VAIARAIVQDAPILVLDEATAHADPEnETA-IQKALNALAK--GRTTVVIAHRLDTIV-HADQILVLVGGKVVERG 562
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPE-ETEeLAELIRRLRDerGITILLIEHDMDLVMgLADRIVVLDFGRVIAEG 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
345-569 |
3.00e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 91.33 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLP-FVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVA 423
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQ--DSMLLRASIADNIRLGrpgatdeQVQAAARQAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQ 499
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFG-------LENKGIPHEEMKERVNEALElvGMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 500 DAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
361-571 |
4.86e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSML-LRASIADN 439
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 440 IRLGRPGATDEQVQAAARQAQIHDRVMElPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENET 519
Cdd:PRK09536 98 VEMGRTPHRSRFDTWTETDRAAVERAME-RTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 520 AIQKALNALAK-GRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEELLAAD 571
Cdd:PRK09536 177 RTLELVRRLVDdGKTAVAAIHDLDLAArYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
352-556 |
8.43e-20 |
|
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: 88.54 E-value: 8.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 352 FAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGT--ELPQMASGEVLSRVAVVF--Q 427
Cdd:cd03290 8 FSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKneSEPSFEATRSRNRYSVAYaaQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 428 DSMLLRASIADNIRLGRPgATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLD 507
Cdd:cd03290 87 KPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506241759 508 EATAHADPE-NETAIQKALNALAKG--RTTVVIAHRLDTIVHADQILVLVGG 556
Cdd:cd03290 166 DPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
361-568 |
1.20e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 90.59 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELP-QMASGEvlSRVAVVFQDSMLLR-ASIAD 438
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE--RRVGFVFQHYALFPhMTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRLG---RPGATDEqvqaaarqaqIHDRVMEL-------------PqgydtvlgsegSDLSGGEAQRVAIARAIVQDAP 502
Cdd:COG1118 95 NIAFGlrvRPPSKAE----------IRARVEELlelvqlegladryP-----------SQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 503 ILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELL 568
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVY 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
361-569 |
1.21e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.37 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASG--EVLSRVAVVFQ--DSMLLRASI 436
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVGIVFQnpDDQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 ADNIRLGrP---GATDEQvqaaarqaqIHDRVMELPQGydtvLGSEGSD------LSGGEAQRVAIARAIVQDAPILVLD 507
Cdd:PRK13639 97 EEDVAFG-PlnlGLSKEE---------VEKRVKEALKA----VGMEGFEnkpphhLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506241759 508 EATAHADPENETAIQKALNALAKGRTTVVIA-HRLDTI-VHADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
345-591 |
1.25e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPF---VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGE---- 417
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 418 VLSRVAVVFQ--DSMLLRASIADNIRLGrP---GATDEQVQAAARQAqihdrvMELPQGYDTVLGSEGSDLSGGEAQRVA 492
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG-PqnfGVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 493 IARAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEELLaa 570
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDIF-- 233
|
250 260
....*....|....*....|.
gi 506241759 571 dghyaalwrsQQVDALEKALL 591
Cdd:PRK13649 234 ----------QDVDFLEEKQL 244
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
345-569 |
1.47e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.00 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAY-GENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVA 423
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQ--DSMLLRASIADNIRLG--RPGATDEQVQAAARQAQIHDRVMELPQgydtvlgSEGSDLSGGEAQRVAIARAIVQ 499
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGmeNQGIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 500 DAPILVLDEATAHADPENETAIQKALNALAKGR--TTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
335-562 |
1.54e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.69 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 335 PRPAAEGPVCMEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLAR-------LIPRFwdPVSGSVRMNG 407
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 408 TEL--PQMASGEVLSRVAVVFQDSMLLRASIADNIR-----LGRPGATDEQVQAAARQAQIHDRVMElpqgydtVLGSEG 480
Cdd:PRK14243 77 KNLyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAygariNGYKGDMDELVERSLRQAALWDEVKD-------KLKQSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 481 SDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVE 560
Cdd:PRK14243 150 LSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTE 229
|
..
gi 506241759 561 RG 562
Cdd:PRK14243 230 GG 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
345-567 |
2.07e-19 |
|
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: 87.78 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGEnlpFV-LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEvlSRVA 423
Cdd:cd03296 3 IEVRNVSKRFGD---FVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQDSMLLR-ASIADNIRLG---RPGATdeqvqaAARQAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAI 497
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFGlrvKPRSE------RPPEAEIRAKVHELLKlvQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 498 VQDAPILVLDEATAHADpeneTAIQKALNALAK------GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEEL 567
Cdd:cd03296 152 AVEPKVLLLDEPFGALD----AKVRKELRRWLRrlhdelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
362-569 |
2.27e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.75 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASG--EVLSRVAVVFQ--DSMLLRASIA 437
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVGMVFQdpDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 438 DNIRLGrpgatdeQVQAAARQAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADP 515
Cdd:PRK13636 102 QDVSFG-------AVNLKLPEDEVRKRVDNALKrtGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 516 ENETAIQKALNALAK--GRTTVVIAHRLDTI-VHADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK13636 175 MGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
345-578 |
2.96e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.30 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPF---VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVL-- 419
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 --SRVAVVFQ--DSMLLRASIADNIRLgrpGATDEQVQAAARQAQIHDRVMELpqGYD-TVLGSEGSDLSGGEAQRVAIA 494
Cdd:PRK13646 83 vrKRIGMVFQfpESQLFEDTVEREIIF---GPKNFKMNLDEVKNYAHRLLMDL--GFSrDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 495 RAIVQDAPILVLDEATAHADPENETAIQKALNALA--KGRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEELLaAD 571
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELF-KD 236
|
....*..
gi 506241759 572 GHYAALW 578
Cdd:PRK13646 237 KKKLADW 243
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
345-569 |
7.11e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.19 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFV---LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS- 420
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 ---RVAVVFQ--DSMLLRASIADNIRLGrP---GATDEQVQAAARQAQihdRVMELPqgyDTVLGSEGSDLSGGEAQRVA 492
Cdd:PRK13641 83 lrkKVSLVFQfpEAQLFENTVLKDVEFG-PknfGFSEDEAKEKALKWL---KKVGLS---EDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 493 IARAIVQDAPILVLDEATAHADPEN-ETAIQKALNALAKGRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
358-568 |
1.13e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 358 LPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS----RVAVVFQDSMLL- 432
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMp 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 RASIADNIRLGR--PGATDEQVQAAARQAQIHDRVMELPQGYDtvlgsegSDLSGGEAQRVAIARAIVQDAPILVLDEAT 510
Cdd:PRK10070 120 HMTVLDNTAFGMelAGINAEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 511 AHADPENETAIQKALNALAKG--RTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELL 568
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
362-569 |
1.17e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 90.57 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLarliprfwdpVSGsvrMNGtELPQMASGEVLSR--VAVVFQDSMLLRASIADN 439
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSL----------ISA---MLG-ELPPRSDASVVIRgtVAYVPQVSWIFNATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 440 IRLGRPGATDEQVQAAARQAQIHDRVMeLPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPEN-- 517
Cdd:PLN03130 699 ILFGSPFDPERYERAIDVTALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgr 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 518 ---ETAIQKALnalaKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLA 569
Cdd:PLN03130 778 qvfDKCIKDEL----RGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
361-567 |
2.73e-18 |
|
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: 85.68 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGtelpqmasgevlsRVAVVFQDSMLLRASIADNI 440
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 441 RLGRpgATDEQVQAAARQA-QIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENET 519
Cdd:cd03291 119 IFGV--SYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506241759 520 AI-QKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEEL 567
Cdd:cd03291 197 EIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
361-562 |
2.79e-18 |
|
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: 83.96 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQmASGEVLSRVAVVFqDSMLL--RASIAD 438
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVS-DSTGLydRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRL-----GRPGAtdeqvqaaarqaQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATA 511
Cdd:cd03266 98 NLEYfaglyGLKGD------------ELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506241759 512 HADPENETAIQKALNAL-AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:cd03266 166 GLDVMATRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
361-560 |
3.45e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS---RVAVVFQDSM------- 430
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 431 LLRASIADNIR-LGRPGATDEQVQAAARQaqihdRVMELPqgyDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEA 509
Cdd:PRK10419 107 TVREIIREPLRhLLSLDKAERLARASEML-----RAVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 510 TAHADPENETAIQKALNALAKGRTT--VVIAHRLDTIVH-ADQILVLVGGKVVE 560
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
362-562 |
3.70e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.44 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWD-----PVSGSVRMNGTEL--PQMASGEVLSRVAVVFQDSMLLRA 434
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 435 SIADNIRLG-------RPGATDEQVQAAARQAQIHDRVMElpQGYDTVLGsegsdLSGGEAQRVAIARAIVQDAPILVLD 507
Cdd:PRK14239 101 SIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 508 EATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYN 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
360-573 |
4.61e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 84.50 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 360 FVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELpqmASGEVLSR---VAVVFQDSmllRASI 436
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL---EYGDYKYRckhIRMIFQDP---NTSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 ADNIRLGRpgatdeqvqaaarqaqihdrVMELPQGYDTVLGSEG-----------------------SDLSGGEAQRVAI 493
Cdd:COG4167 101 NPRLNIGQ--------------------ILEEPLRLNTDLTAEEreerifatlrlvgllpehanfypHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 494 ARAIVQDAPILVLDEATAHADPENETAI-------QKALnalakGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHE 565
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIinlmlelQEKL-----GISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTA 235
|
....*...
gi 506241759 566 ELLAADGH 573
Cdd:COG4167 236 EVFANPQH 243
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
364-587 |
6.25e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 364 DVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS----RVAVVFQDSMLL-RASIAD 438
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPpekrRIGYVFQDARLFpHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRLGRPGATDEQvqaaarqaqiHDRVMELpQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENE 518
Cdd:PRK11144 96 NLRYGMAKSMVAQ----------FDKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 519 TAIQKALNALAKGRTT--VVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGHYAALWRSQQVDALE 587
Cdd:PRK11144 165 RELLPYLERLAREINIpiLYVSHSLDEILRlADRVVVLEQGKVKAFGPLEEVWASSAMRPWLPKEEQSSILK 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
348-571 |
6.27e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.27 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 348 EGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQ 427
Cdd:PRK10253 11 EQLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 428 DS----------MLLRASIADNIRLGRPGATDEQVQAaarqaqihdRVMElPQGYDTVLGSEGSDLSGGEAQRVAIARAI 497
Cdd:PRK10253 89 NAttpgditvqeLVARGRYPHQPLFTRWRKEDEEAVT---------KAMQ-ATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 498 VQDAPILVLDEATAHADPENETAIQKALNAL--AKGRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEELLAAD 571
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACrYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
364-562 |
6.61e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 82.73 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 364 DVDVALE-PGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLS----RVAVVFQDSMLL-RASIA 437
Cdd:cd03297 14 TLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPpqqrKIGLVFQQYALFpHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 438 DNIRLGRPGATDeqvqaaarqAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADP 515
Cdd:cd03297 94 ENLAFGLKRKRN---------REDRISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506241759 516 ENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:cd03297 165 ALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
346-568 |
8.46e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.22 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR--VA 423
Cdd:PRK09493 3 EFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRqeAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQDSMLLRASIA-DNIRLGrP----GATDEQVqaaarqaqiHDRVMELpqgydtvLGSEG---------SDLSGGEAQ 489
Cdd:PRK09493 81 MVFQQFYLFPHLTAlENVMFG-PlrvrGASKEEA---------EKQAREL-------LAKVGlaerahhypSELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 490 RVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALA-KGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEEL 567
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVL 223
|
.
gi 506241759 568 L 568
Cdd:PRK09493 224 I 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
361-567 |
2.51e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.98 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEvlSRVAVVFQDSMLLR-ASIADN 439
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 440 IRLG--------RPGAtdeqvqaaarqAQIHDRVMELpqgYDTVLGSE-----GSDLSGGEAQRVAIARAIVQDAPILVL 506
Cdd:PRK10851 95 IAFGltvlprreRPNA-----------AAIKAKVTQL---LEMVQLAHladryPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506241759 507 DEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEEL 567
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
361-573 |
2.82e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.72 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL--------PQMASGEVLSRVAVVFQDSMLL 432
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 -RASIADNIRLGRPGATDEQvqaaarqaqiHDRVMELPQGYDTVLGSEGSD------LSGGEAQRVAIARAIVQDAPILV 505
Cdd:PRK11264 98 pHRTVLENIIEGPVIVKGEP----------KEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241759 506 LDEATAHADPENETAIQKALNALAK-GRTTVVIAHRL----DTivhADQILVLVGGKVVERGVHEELLAADGH 573
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMsfarDV---ADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
361-558 |
3.71e-17 |
|
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: 79.78 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR-VAVV----FQDSMLLRAS 435
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 436 IADNIRLGRpgatdeqvqaaarqaqihdrvmelpqgydtvlgsegsDLSGGEAQRVAIARAIVQDAPILVLDEATAHADP 515
Cdd:cd03215 95 VAENIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 506241759 516 ENETAIQKALNALA-KGRTTVVIAHRLDTIVH-ADQILVLVGGKV 558
Cdd:cd03215 138 GAKAEIYRLIRELAdAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-573 |
3.96e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.43 E-value: 3.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 354 YGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWD-----PVSGSVRMNGTEL--PQMASGEVLSRVAVVF 426
Cdd:PRK14267 14 YGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 427 Q-DSMLLRASIADNIRLG--------RPGATDEQVQAAARQAQIHDRVMELPQGYdtvlgseGSDLSGGEAQRVAIARAI 497
Cdd:PRK14267 92 QyPNPFPHLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRLNDY-------PSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 498 VQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH 573
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
356-568 |
4.09e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.71 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 356 ENLPFVLQDVDVAL-------EPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQD 428
Cdd:PRK13647 8 EDLHFRYKDGTKALkglslsiPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 429 --SMLLRASIADNIRLG------RPGATDEQVQAAARQAQIHDRVMELPQgydtvlgsegsDLSGGEAQRVAIARAIVQD 500
Cdd:PRK13647 88 pdDQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 501 APILVLDEATAHADPENETAIQKALNALAKGRTTVVIA-HRLDTIVH-ADQILVLVGGKVVERGVHEELL 568
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
361-567 |
4.15e-17 |
|
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: 85.73 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGtelpqmasgevlsRVAVVFQDSMLLRASIADNI 440
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 441 RLGRpgATDEQVQAAARQA-QIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENET 519
Cdd:TIGR01271 508 IFGL--SYDEYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506241759 520 AI-QKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEEL 567
Cdd:TIGR01271 586 EIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
24-323 |
4.65e-17 |
|
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: 81.83 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 24 IIGNVAIAALSSACEFVPYLAIARVaqlsITEGVPPSDV-LAMWVLVAVAGAAAGRMLFSMATGRCH-YADADFRVHVRT 101
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLL----IDDVIPAGDLsLLLWIALLLLLLALLRALLSYLRRYLAaRLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 102 VLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVVIGVA 181
Cdd:cd07346 77 DLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 182 WPFMMRdFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAcyvwTKRNGNAFSWVSA---L 258
Cdd:cd07346 157 RYFRRR-IRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDA----NLRAARLSALFSPligL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 259 FSPGAMLVVLLAATLaFVANGVLPLERCVPFLvlgvgipAGLVNLFRSIRML-QMSLQAADHLASV 323
Cdd:cd07346 232 LTALGTALVLLYGGY-LVLQGSLTIGELVAFL-------AYLGMLFGPIQRLaNLYNQLQQALASL 289
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
345-553 |
5.44e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.53 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAV 424
Cdd:PRK10247 8 LQLQNVGYLAGDAK--ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRASIADN------IRLGRPgatDEQVQAAARQAqihdrvMELPqgyDTVLGSEGSDLSGGEAQRVAIARAIv 498
Cdd:PRK10247 86 CAQTPTLFGDTVYDNlifpwqIRNQQP---DPAIFLDDLER------FALP---DTILTKNIAELSGGEKQRISLIRNL- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 499 QDAP-ILVLDEATAHADPENETAIQKALNALAKGRTTVVI--AHRLDTIVHADQILVL 553
Cdd:PRK10247 153 QFMPkVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITL 210
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-570 |
5.58e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWD------PVSGSVRMNGTELPQMASGEVLSRVAVVFQD-SMLLR 433
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQpNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 434 ASIADNIR--LGRPGATDEQVQAAARQAQIHdRVMELPQGYDTvLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATA 511
Cdd:PRK14246 105 LSIYDNIAypLKSHGIKEKREIKKIVEECLR-KVGLWKEVYDR-LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 512 HADPENETAIQKALNALAKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAA 570
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
354-559 |
7.14e-17 |
|
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: 79.86 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 354 YGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL-PQMAsgEVLSRVAVVFQDSMLL 432
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRK--AARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 RA-SIADNIRL-----GRPGATDEQVQAAARqaqihdRVMELPQGYDTvlgsEGSDLSGGEAQRVAIARAIVQDAPILVL 506
Cdd:cd03263 88 DElTVREHLRFyarlkGLPKSEIKEEVELLL------RVLGLTDKANK----RARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 507 DEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTI-VHADQILVLVGGKVV 559
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLR 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
361-541 |
7.72e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.24 E-value: 7.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASG---EVLSR-VAVVFQDSMLLRASI 436
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 A-DNIRL------GRPGATDEQVQAAARQAQIHDRVMELPqgydtvlgsegSDLSGGEAQRVAIARAIVQDaPILVL-DE 508
Cdd:PRK11629 104 AlENVAMplligkKKPAEINSRALEMLAAVGLEHRANHRP-----------SELSGGERQRVAIARALVNN-PRLVLaDE 171
|
170 180 190
....*....|....*....|....*....|....*
gi 506241759 509 ATAHADPENETAIQKALNAL--AKGRTTVVIAHRL 541
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDL 206
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
362-568 |
8.20e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.94 E-value: 8.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPrFWDP----VSGSVRMNGT--ELPQMASgevlsRVAVVFQDSMLLRAS 435
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMpiDAKEMRA-----ISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 436 IADN-------IRLGRPGATDEQVQaaarqaqihdRVMELPQGY------DTVLGSEGS--DLSGGEAQRVAIARAIVQD 500
Cdd:TIGR00955 115 TVREhlmfqahLRMPRRVTKKEKRE----------RVDEVLQALglrkcaNTRIGVPGRvkGLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 501 APILVLDEATAHADPENETAIQKALNALA-KGRTTVVIAHRLDTIVHA--DQILVLVGGKVVERGVHEELL 568
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAV 255
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
335-562 |
8.41e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 335 PRPAAEGPVcMEFEGVAFAYGENLP---FVLQDVDVALEPGTVTALVGDSGSGKTTLAR-----LIPRFWDPVSGSVRMN 406
Cdd:PRK13631 13 PNPLSDDII-LRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 407 GTELPQMASGEVLSR-----------VAVVFQ--DSMLLRASIADNIRLGrPGATDEQVQAAARQAQIHDRVMELPQGYd 473
Cdd:PRK13631 92 DKKNNHELITNPYSKkiknfkelrrrVSMVFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSY- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 474 tvLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETA-IQKALNALAKGRTTVVIAHRLDTIVH-ADQIL 551
Cdd:PRK13631 170 --LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVI 247
|
250
....*....|.
gi 506241759 552 VLVGGKVVERG 562
Cdd:PRK13631 248 VMDKGKILKTG 258
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
345-569 |
8.85e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.80 E-value: 8.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMAS-GEVLSRVA 423
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQ--DSMLLRASIADNIRLGRPGATdeqvqaaARQAQIHDRV-MELPQ-GYDTVLGSEGSDLSGGEAQRVAIARAIVQ 499
Cdd:PRK13644 81 IVFQnpETQFVGRTVEEDLAFGPENLC-------LPPIEIRKRVdRALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 500 DAPILVLDEATAHADPENETAIQKALNAL-AKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
318-556 |
1.03e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 318 DHLASVLNVAPLAEPERPRPAAEGPVCMEFEGVAFAygenLP---FVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPR 394
Cdd:COG4178 336 AGFEEALEAADALPEAASRIETSEDGALALEDLTLR----TPdgrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 395 FWDPVSGSVRMNGTE----LPQ---MASG---EVLS--RVAVVFQDSMLLRASIAdnIRLGRpgatdeqvqaaarqaqIH 462
Cdd:COG4178 412 LWPYGSGRIARPAGArvlfLPQrpyLPLGtlrEALLypATAEAFSDAELREALEA--VGLGH----------------LA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 463 DRvMELPQGYDTVLgsegsdlSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLD 542
Cdd:COG4178 474 ER-LDEEADWDQVL-------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRST 545
|
250
....*....|....
gi 506241759 543 TIVHADQILVLVGG 556
Cdd:COG4178 546 LAAFHDRVLELTGD 559
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
366-577 |
1.09e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.63 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 366 DVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNG---TELPQmasgevlSR--VAVVFQDSMLL-RASIADN 439
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPP-------SRrpVSMLFQENNLFsHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 440 IRLG-RPG-----ATDEQVQAAARQAQIHDRVMELPqgydtvlgsegSDLSGGEAQRVAIARAIVQDAPILVLDEATAHA 513
Cdd:PRK10771 92 IGLGlNPGlklnaAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 514 DPENETAIQKALNALAKGR--TTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGHYAAL 577
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
96-292 |
1.79e-16 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 79.99 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 96 RVHVRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFV 175
Cdd:pfam00664 73 SRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 176 VVIGVAWPFMMRdFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAcyvWTKRNG--NAFS 253
Cdd:pfam00664 153 LYILVSAVFAKI-LRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKA---GIKKAVanGLSF 228
|
170 180 190
....*....|....*....|....*....|....*....
gi 506241759 254 WVSALFSPGAMLVVLLAATlAFVANGVLPLERCVPFLVL 292
Cdd:pfam00664 229 GITQFIGYLSYALALWFGA-YLVISGELSVGDLVAFLSL 266
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
347-569 |
1.95e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.05 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 347 FEGVAFAYGENLPF---VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELP----QMASGEVL 419
Cdd:PRK13645 9 LDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 SR-VAVVFQ--DSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVmELPQGYdtvLGSEGSDLSGGEAQRVAIARA 496
Cdd:PRK13645 89 RKeIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 497 IVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
346-565 |
2.65e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.90 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL-----PQMASGEVLS 420
Cdd:COG4161 4 QLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 R-VAVVFQDSMLL-RASIADNIrLGRP----GATDEQVQaaarqaqihDRVMELpqgYDTVLGSEGSD-----LSGGEAQ 489
Cdd:COG4161 82 QkVGMVFQQYNLWpHLTVMENL-IEAPckvlGLSKEQAR---------EKAMKL---LARLRLTDKADrfplhLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 490 RVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHE 565
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
354-569 |
2.92e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 354 YGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELP---------QMASGEVL----S 420
Cdd:PRK10619 15 YGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLrllrT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 RVAVVFQD-SMLLRASIADNIR------LGRPGA-TDEQVQAAARQAQIHDRVMelpqgydtvlGSEGSDLSGGEAQRVA 492
Cdd:PRK10619 93 RLTMVFQHfNLWSHMTVLENVMeapiqvLGLSKQeARERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 493 IARAIVQDAPILVLDEATAHADPENETAIQKALNALA-KGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
350-567 |
2.96e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 350 VAFAYGEN----LPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMAS-GEVLSRVAV 424
Cdd:PRK13633 10 VSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlWDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQ--DSMLLRASIADNI-----RLGRPgaTDEqvqaaarqaqIHDRVMElpqGYDTVLGSEGSD-----LSGGEAQRVA 492
Cdd:PRK13633 90 VFQnpDNQIVATIVEEDVafgpeNLGIP--PEE----------IRERVDE---SLKKVGMYEYRRhaphlLSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 493 IARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEEL 567
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
362-573 |
3.60e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.01 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR---VAVVFQD---------- 428
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkIQIVFQNpygslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 429 -SMLLRASIADNIRLGRPgatdeqvqaaarqaqihDRVMELPQGYDTV-LGSEGSD-----LSGGEAQRVAIARAIVQDA 501
Cdd:PRK11308 111 vGQILEEPLLINTSLSAA-----------------ERREKALAMMAKVgLRPEHYDryphmFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 502 PILVLDEATAHADpeneTAIQ-KALNALAK-----GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH 573
Cdd:PRK11308 174 DVVVADEPVSALD----VSVQaQVLNLMMDlqqelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPRH 248
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
345-567 |
5.21e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 78.65 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFvlQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASG---EVLSR 421
Cdd:PRK11831 8 VDMRGVSFTRGNRCIF--DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 VAVVFQDSMLLR-ASIADNIrlgrpgATDEQVQAAARQAQIHDRVMELPQGydtvLGSEG------SDLSGGEAQRVAIA 494
Cdd:PRK11831 86 MSMLFQSGALFTdMNVFDNV------AYPLREHTQLPAPLLHSTVMMKLEA----VGLRGaaklmpSELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 495 RAIVQDAPILVLDEATAHADPENETAIQKALNAL--AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEEL 567
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
330-573 |
5.71e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.90 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 330 AEPE-RPRPAAEG-PVCMEFEGVAFAY-----------GENlpFVLQDVDVALEPGTVTALVGDSGSGKTT----LARLI 392
Cdd:PRK15134 259 SEPSgDPVPLPEPaSPLLDVEQLQVAFpirkgilkrtvDHN--VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 393 PRfwdpvSGSVRMNGTELPQMASGEVL---SRVAVVFQD---SMLLRAS----IADNIRLGRPGATDEQVqaaarqaqiH 462
Cdd:PRK15134 337 NS-----QGEIWFDGQPLHNLNRRQLLpvrHRIQVVFQDpnsSLNPRLNvlqiIEEGLRVHQPTLSAAQR---------E 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 463 DRVMELPQ--GYDTVLGSE-GSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGR--TTVVI 537
Cdd:PRK15134 403 QQVIAVMEevGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFI 482
|
250 260 270
....*....|....*....|....*....|....*...
gi 506241759 538 AHRLDtIVHA--DQILVLVGGKVVERGVHEELLAADGH 573
Cdd:PRK15134 483 SHDLH-VVRAlcHQVIVLRQGEVVEQGDCERVFAAPQQ 519
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
345-538 |
6.64e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.22 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAY--GENlpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEV--LS 420
Cdd:PRK10908 2 IRFEHVSKAYlgGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 R-VAVVFQD-SMLLRASIADN--IRLGRPGATDEQVQAAARQAQihDRVMELPQGYDTVLgsegsDLSGGEAQRVAIARA 496
Cdd:PRK10908 79 RqIGMIFQDhHLLMDRTVYDNvaIPLIIAGASGDDIRRRVSAAL--DKVGLLDKAKNFPI-----QLSGGEQQRVGIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 506241759 497 IVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIA 538
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMA 193
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
354-562 |
1.12e-15 |
|
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: 76.10 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 354 YGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMAsgEVLSRVAVV-----FQD 428
Cdd:cd03268 10 YGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGALieapgFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 429 SMLLRasiaDNIRLGR--PGATDEqvqaaarqaqIHDRVMelpqgyDTV-LGSEGSD----LSGGEAQRVAIARAIVQDA 501
Cdd:cd03268 86 NLTAR----ENLRLLArlLGIRKK----------RIDEVL------DVVgLKDSAKKkvkgFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241759 502 PILVLDEATAHADPENETAIQKALNALAKGRTTVVIA-HRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
346-557 |
1.27e-15 |
|
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: 74.02 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIprfwdpvsgsvrmNGTELPQmaSGEVlsrvavv 425
Cdd:cd03221 2 ELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------------AGELEPD--EGIV------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 fqdsmllraSIADNIRLGRpgatdeqvqaaarqaqihdrvmeLPQgydtvlgsegsdLSGGEAQRVAIARAIVQDAPILV 505
Cdd:cd03221 58 ---------TWGSTVKIGY-----------------------FEQ------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 506 LDEATAHADPENETAIQKALNALaKGrTTVVIAH-R--LDTIvhADQILVLVGGK 557
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY-PG-TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
350-573 |
1.70e-15 |
|
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: 79.73 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 350 VAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGK--TTLA--RLIPRFWDPVSGSVRMNGTELPQmASGEVL-----S 420
Cdd:COG4172 14 VAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKsvTALSilRLLPDPAAHPSGSILFDGQDLLG-LSERELrrirgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 RVAVVFQDSM-----LLR--ASIADNIRL--GRPGAtdeqvqaaarqaQIHDRVMEL--------PQgydTVLGSEGSDL 483
Cdd:COG4172 93 RIAMIFQEPMtslnpLHTigKQIAEVLRLhrGLSGA------------AARARALELlervgipdPE---RRLDAYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 484 SGGEAQRVAIARAIVQDAPILVLDEATahadpeneTA----IQKA-LNALAK-----GRTTVVIAHRLdTIV--HADQIL 551
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPT--------TAldvtVQAQiLDLLKDlqrelGMALLLITHDL-GVVrrFADRVA 228
|
250 260
....*....|....*....|..
gi 506241759 552 VLVGGKVVERGVHEELLAADGH 573
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAAPQH 250
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
335-564 |
1.81e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 335 PRPAAEGPVCMEFEGVAFAYGEnlpFVLqdvDValEPGT-----VTALVGDSGSGKTTLARLIPRFWDPVSGSVrmnGTE 409
Cdd:PRK13409 331 PRDESERETLVEYPDLTKKLGD---FSL---EV--EGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 410 L-----PQ-------MASGEVLSRVAVVFQDSMLlRASIADNIRLgrpgatdeqvqaaarqaqihDRVMElpqgydtvlg 477
Cdd:PRK13409 400 LkisykPQyikpdydGTVEDLLRSITDDLGSSYY-KSEIIKPLQL--------------------ERLLD---------- 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 478 SEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGR--TTVVIAHRL---DTIvhADQILV 552
Cdd:PRK13409 449 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIymiDYI--SDRLMV 526
|
250
....*....|..
gi 506241759 553 LVGgkvvERGVH 564
Cdd:PRK13409 527 FEG----EPGKH 534
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-573 |
1.87e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.06 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGsVRMNGTELPQMAS-------GEVLSRVAVVFQDSMLLR 433
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSifnyrdvLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 434 ASIADNIRLGRP-----------GATDEQVQAAARQAQIHDRVMELPqgydtvlgsegSDLSGGEAQRVAIARAIVQDAP 502
Cdd:PRK14271 115 MSIMDNVLAGVRahklvprkefrGVAQARLTEVGLWDAVKDRLSDSP-----------FRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 503 ILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH 573
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
337-571 |
1.91e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.54 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 337 PAAEGPVcmEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASg 416
Cdd:PRK13537 2 PMSVAPI--DFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 417 EVLSRVAVVFQ-DSMLLRASIADNIRL-----GRPGATDEQVQAAARqaqihdRVMELPQGYDTVLGsegsDLSGGEAQR 490
Cdd:PRK13537 77 HARQRVGVVPQfDNLDPDFTVRENLLVfgryfGLSAAAARALVPPLL------EFAKLENKADAKVG----ELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 491 VAIARAIVQDAPILVLDEATAHADPENETAIQKALNAL-AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELL 568
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
...
gi 506241759 569 AAD 571
Cdd:PRK13537 227 ESE 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
345-591 |
2.38e-15 |
|
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: 79.95 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDpVSGSVRMNGTELPQMASGEVLSRVAV 424
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRASIADNIRlgrPGA--TDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAP 502
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLD---PYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 503 ILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHYaalwrSQQ 582
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF-----KQA 1448
|
....*....
gi 506241759 583 VDALEKALL 591
Cdd:TIGR01271 1449 MSAADRLKL 1457
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
361-559 |
2.72e-15 |
|
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: 75.39 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIP---RFWDPVSGSVRMNGTElpqMASGEVLSRVAVVFQDSMLL----- 432
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQP---RKPDQFQKCVAYVRQDDILLpgltv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 RASI--ADNIRLGRPGATDEQVQAaarqaqihDRVMELPQGYDTVLGSEG-SDLSGGEAQRVAIARAIVQDAPILVLDEA 509
Cdd:cd03234 99 RETLtyTAILRLPRKSSDAIRKKR--------VEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506241759 510 TAHADPENETAIQKALNALAKGRTTVVIA-H--RLDTIVHADQILVLVGGKVV 559
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
362-567 |
2.82e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.02 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLarliprfwdpVSGsvrMNGtELPQMASGEVLSR--VAVVFQDSMLLRASIADN 439
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSL----------ISA---MLG-ELSHAETSSVVIRgsVAYVPQVSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 440 IRLGRPGATDEQVQAAARQAQIHDrvMELPQGYD-TVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPE-N 517
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHD--LDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506241759 518 ETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEEL 567
Cdd:PLN03232 777 HQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
355-560 |
3.26e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 355 GENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQM---ASGEVLSR-VAVVFQDSM 430
Cdd:PRK10584 19 GEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhVGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 431 LLRASIA-DNIRL------GRPGATDEQVQAAARQAQIHDRVMELPqgydtvlgsegSDLSGGEAQRVAIARAIVQDAPI 503
Cdd:PRK10584 99 LIPTLNAlENVELpallrgESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 504 LVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVHADQILVLVGGKVVE 560
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
364-573 |
4.82e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.67 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 364 DVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASG---EVLSRVAVVFQD---SMLLRASIA 437
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDplaSLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 438 DNI----RLGRPGATDEqvqaaarqaQIHDRVME-------LPQgydtVLGSEGSDLSGGEAQRVAIARAIVQDAPILVL 506
Cdd:PRK15079 119 EIIaeplRTYHPKLSRQ---------EVKDRVKAmmlkvglLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 507 DEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH 573
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLH 255
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
345-555 |
7.78e-15 |
|
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: 72.57 E-value: 7.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTE----LPQ---MASGe 417
Cdd:cd03223 1 IELENLSLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEdllfLPQrpyLPLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 418 vlsrvavvfqdsmLLRASIAdnirlgrpgatdeqvqaaarqaqihdrvmeLPqgYDTVLgsegsdlSGGEAQRVAIARAI 497
Cdd:cd03223 79 -------------TLREQLI------------------------------YP--WDDVL-------SGGEQQRLAFARLL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 498 VQDAPILVLDEATAHADPENETAIQKALNALakgRTTVV-IAHRLDTIVHADQILVLVG 555
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
346-571 |
8.97e-15 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 74.35 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSV------RMNGTELPqmasgEVL 419
Cdd:COG1119 5 ELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgeRRGGEDVW-----ELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 SRVAVV---FQDSMLLRASIADNIR------LGRPGATDEQVQAAArqaqihDRVMELpqgydtvLGSEG------SDLS 484
Cdd:COG1119 78 KRIGLVspaLQLRFPRDETVLDVVLsgffdsIGLYREPTDEQRERA------RELLEL-------LGLAHladrpfGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 485 GGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVV-IAHRLDTIVHA-DQILVLVGGKVVER 561
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
250
....*....|
gi 506241759 562 GVHEELLAAD 571
Cdd:COG1119 225 GPKEEVLTSE 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
362-586 |
9.34e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 74.04 E-value: 9.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVlsrvaVVFQD-SMLLRASIADNI 440
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNySLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 441 RLgrpgATDEQVQAAARQaqihDRVMELPQGYDTVLGSEGSD-----LSGGEAQRVAIARAIVQDAPILVLDEATAHADP 515
Cdd:TIGR01184 76 AL----AVDRVLPDLSKS----ERRAIVEEHIALVGLTEAADkrpgqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 516 ENETAIQKALNALAK--GRTTVVIAHRLD-TIVHADQILVLVGGKV----------VERGVHEELLAADGHYAALwRSQQ 582
Cdd:TIGR01184 148 LTRGNLQEELMQIWEehRVTVLMVTHDVDeALLLSDRVVMLTNGPAanigqilevpFPRPRDRLEVVEDPSYYDL-RNEA 226
|
....
gi 506241759 583 VDAL 586
Cdd:TIGR01184 227 LYFL 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
312-571 |
9.80e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 77.32 E-value: 9.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 312 MSLQAA-DHLASvLNVAPLaEPERPRPAAeGPVC--MEFEGVAFAYGENlPFVLQDVDVALEPGTVTALVGDSGSGKTTL 388
Cdd:PRK10522 290 LSAQVAfNKLNK-LALAPY-KAEFPRPQA-FPDWqtLELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 389 ARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRasiadniRLGRPG---ATDEQVQAAARQAQIHDRV 465
Cdd:PRK10522 366 AMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD-------QLLGPEgkpANPALVEKWLERLKMAHKL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 466 mELPQGYDTVLgsegsDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPE-NETAIQKALNAL-AKGRTTVVIAHRLDT 543
Cdd:PRK10522 439 -ELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfRREFYQVLLPLLqEMGKTIFAISHDDHY 512
|
250 260
....*....|....*....|....*....
gi 506241759 544 IVHADQILVLVGGKVVE-RGVHEELLAAD 571
Cdd:PRK10522 513 FIHADRLLEMRNGQLSElTGEERDAASRD 541
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
361-571 |
1.04e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.84 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQ--DSMLLRASIAD 438
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRLGRPG-ATDEQVQAAARQAQIHdrvmelPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPEN 517
Cdd:PRK13652 99 DIAFGPINlGLDEETVAHRVSSALH------MLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 518 ETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAAD 571
Cdd:PRK13652 173 VKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
335-564 |
1.27e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 77.13 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 335 PRPAAEGPVCMEFEGVAFAYGEnlpFVLqDVDVA-LEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMngtEL--- 410
Cdd:COG1245 332 PRREKEEETLVEYPDLTKSYGG---FSL-EVEGGeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE---DLkis 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 411 --PQMASG-------EVLSRVAVVFQDSMLLRASIADNIRLgrpgatdeqvqaaarqaqihDRVMElpqgydtvlgSEGS 481
Cdd:COG1245 405 ykPQYISPdydgtveEFLRSANTDDFGSSYYKTEIIKPLGL--------------------EKLLD----------KNVK 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 482 DLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALA--KGRTTVVIAHRL---DTIvhADQILVLVGg 556
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDIyliDYI--SDRLMVFEG- 531
|
....*...
gi 506241759 557 kvvERGVH 564
Cdd:COG1245 532 ---EPGVH 536
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
361-508 |
1.36e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 74.13 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTelPQMASGevlSRVAVVFQDSMLLR-ASIADN 439
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV--PVTGPG---ADRGVVFQKDALLPwLNVLDN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 440 IRL-----GRPGATdeqvqaaarqaqIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDE 508
Cdd:COG4525 97 VAFglrlrGVPKAE------------RRARAEELLAlvGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
361-569 |
1.55e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 73.35 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTE----------------LPQMASgevlsrvav 424
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklpmhkrarlgigyLPQEAS--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQdsmllRASIADNIRLGRPGATDeqvqaaaRQAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAP 502
Cdd:cd03218 86 IFR-----KLTVEENILAVLEIRGL-------SKKEREEKLEELLEefHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 503 ILVLDEATAHADPENETAIQKALNALAKGRTTVVIA-HRL-DTIVHADQILVLVGGKVVERGVHEELLA 569
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
362-571 |
1.64e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.72 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTL----ARLIPRfwdpvSGSVRMNGTELPQMaSGEVLSRV-AVVFQDSMLLrASI 436
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLlarmAGLLPG-----QGEILLNGRPLSDW-SAAELARHrAYLSQQQSPP-FAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 A--DNIRLGRPGATDEQVqaaarqaqIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQ-------DAPILV 505
Cdd:COG4138 85 PvfQYLALHQPAGASSEA--------VEQLLAQLAEalGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 506 LDEATAHADPENETAIQKALNALA-KGRTTVVIAHRLD-TIVHADQILVLVGGKVVERGVHEELLAAD 571
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPE 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-565 |
1.92e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.87 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 335 PRPAAEGPVCMEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMA 414
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 415 SGeVLSRVAVVFQ-DSMLLRASIADNIRL-GRpgatdeqvqaaarQAQIHDRVME-----------LPQGYDTVLgsegS 481
Cdd:PRK13536 110 RL-ARARIGVVPQfDNLDLEFTVRENLLVfGR-------------YFGMSTREIEavipsllefarLESKADARV----S 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 482 DLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNA-LAKGRTTVVIAHRLDTIVH-ADQILVLVGG-KV 558
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGrKI 251
|
....*..
gi 506241759 559 VERGVHE 565
Cdd:PRK13536 252 AEGRPHA 258
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
345-562 |
2.10e-14 |
|
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: 72.31 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL-------------- 410
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLdiaarnrigylpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 411 ----PQMASGEVLSRVAvvfQDSMLLRASIADNIR--LGRPGATDEQvqaaarqaqihDRVMElpqgydtvlgsegsDLS 484
Cdd:cd03269 79 rglyPKMKVIDQLVYLA---QLKGLKKEEARRRIDewLERLELSEYA-----------NKRVE--------------ELS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 485 GGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALA-KGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:cd03269 131 KGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
346-572 |
2.23e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.99 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL--------------- 410
Cdd:COG4152 3 ELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdpedrrrigylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 411 ---PQMASGEVLSRVAvvfqdsmllrasiadniRL-GRPGATdeqvqaaarqaqIHDRVMEL-------PQGYDTVlgse 479
Cdd:COG4152 81 glyPKMKVGEQLVYLA-----------------RLkGLSKAE------------AKRRADEWlerlglgDRANKKV---- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 480 gSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALA-KGRTTVVIAHRLDTI-VHADQILVLVGGK 557
Cdd:COG4152 128 -EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVeELCDRIVIINKGR 206
|
250
....*....|....*
gi 506241759 558 VVERGVHEELLAADG 572
Cdd:COG4152 207 KVLSGSVDEIRRQFG 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
329-559 |
2.62e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 329 LAEPERPRPAAEGPVCMEFEGVafaygeNLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLI----PrfwdPVSGSVR 404
Cdd:COG1129 241 LEDLFPKRAAAPGEVVLEVEGL------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALfgadP----ADSGEIR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 405 MNGTEL----PQ--MASGevlsrVAVV----FQDSMLLRASIADNI------RLGRPGATDEQVQAAARQAQIHDrvMEL 468
Cdd:COG1129 311 LDGKPVrirsPRdaIRAG-----IAYVpedrKGEGLVLDLSIRENItlasldRLSRGGLLDRRRERALAEEYIKR--LRI 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 469 -PQGYDTVLGSegsdLSGGEAQRVAIARAIVQDAPILVLDEAT------AHADpenetaIQKALNALAK-GRTTVVIAHR 540
Cdd:COG1129 384 kTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTrgidvgAKAE------IYRLIRELAAeGKAVIVISSE 453
|
250 260
....*....|....*....|
gi 506241759 541 LDTIVH-ADQILVLVGGKVV 559
Cdd:COG1129 454 LPELLGlSDRILVMREGRIV 473
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
345-574 |
3.03e-14 |
|
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: 73.35 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDpVSGSVRMNGTELPQMASGEVLSRVAV 424
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRASIADNIRlgrPGA--TDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAP 502
Cdd:cd03289 82 IPQKVFIFSGTFRKNLD---PYGkwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 503 ILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAADGHY 574
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
332-566 |
3.25e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.60 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 332 PERPRPAAEGPVCMEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNG---T 408
Cdd:PRK09452 2 KKLNKQPSSLSPLVELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqdiT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 409 ELPQMASgevlsRVAVVFQDSMLL-RASIADNIRLG-----RPGAtdeqvqaaarqaQIHDRVME---LPQgYDTVLGSE 479
Cdd:PRK09452 80 HVPAENR-----HVNTVFQSYALFpHMTVFENVAFGlrmqkTPAA------------EITPRVMEalrMVQ-LEEFAQRK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 480 GSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAH-RLDTIVHADQILVLVGG 556
Cdd:PRK09452 142 PHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDG 221
|
250
....*....|....
gi 506241759 557 KVVERG----VHEE 566
Cdd:PRK09452 222 RIEQDGtpreIYEE 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
361-571 |
3.58e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQ-----DSMLLRAS 435
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQqlpaaEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 436 IAD-----NIRLGRPGATDeqvqaaarqaqiHDRVMEL-------PQGYDTVlgsegSDLSGGEAQRVAIARAIVQDAPI 503
Cdd:PRK10575 106 VAIgrypwHGALGRFGAAD------------REKVEEAislvglkPLAHRLV-----DSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 504 LVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHA---DQILVLVGGKVVERGVHEELLAAD 571
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArycDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
361-561 |
3.74e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.81 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGtelpQMASGEVLSRvAVVFQDSMLLR-ASIADN 439
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG----KPVEGPGAER-GVVFQNEGLLPwRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 440 IRLGRPGATDEQVQAAARQAQIHDRVmelpqgydtvlGSEGSD------LSGGEAQRVAIARAIVQDAPILVLDEATAHA 513
Cdd:PRK11248 91 VAFGLQLAGVEKMQRLEIAHQMLKKV-----------GLEGAEkryiwqLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 506241759 514 DPENETAIQKALNAL--AKGRTTVVIAHRLDTIVHADQILVLVG---GKVVER 561
Cdd:PRK11248 160 DAFTREQMQTLLLKLwqETGKQVLLITHDIEEAVFMATELVLLSpgpGRVVER 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
348-562 |
7.31e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 348 EGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL-----PQMASGEVLSR- 421
Cdd:PRK11124 6 NGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktPSDKAIRELRRn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 VAVVFQDSMLL-RASIADNI--------RLGRPGAtdeqvqaaarqaqiHDRVMELpqgYDTVLGSEGSD-----LSGGE 487
Cdd:PRK11124 84 VGMVFQQYNLWpHLTVQQNLieapcrvlGLSKDQA--------------LARAEKL---LERLRLKPYADrfplhLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 488 AQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
349-576 |
7.44e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 7.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 349 GVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSV-----RMNgtELPQMASGevlsrVA 423
Cdd:PRK11000 8 NVTKAYGDVV--ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekRMN--DVPPAERG-----VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQDSMLL-RASIADNIRLGRPGAtdeqvqaAARQAQIHDRV---MELPQgYDTVLGSEGSDLSGGEAQRVAIARAIVQ 499
Cdd:PRK11000 79 MVFQSYALYpHLSVAENMSFGLKLA-------GAKKEEINQRVnqvAEVLQ-LAHLLDRKPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 500 DAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAH-RLDTIVHADQILVLVGGKVVERGVHEELLaadgHYAA 576
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELY----HYPA 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
348-558 |
9.98e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.63 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 348 EGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELpqmasGEVLSRVAVVFQ 427
Cdd:PRK11247 16 NAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 428 DSMLLR-ASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPqgydtvlgsegSDLSGGEAQRVAIARAIVQDAPILVL 506
Cdd:PRK11247 89 DARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 507 DEATAHADPENETAIQKALNAL--AKGRTTVVIAHRL-DTIVHADQILVLVGGKV 558
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
354-555 |
1.42e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.69 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 354 YGEN------LPfvlqdvdvALEPGTVTALVGDSGSGKTTLAR-----LIPRF--------WDPVSGSVRmnGTEL---- 410
Cdd:PRK13409 83 YGVNgfklygLP--------IPKEGKVTGILGPNGIGKTTAVKilsgeLIPNLgdyeeepsWDEVLKRFR--GTELqnyf 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 411 PQMASGEVlsRVAV----VFQDSMLLRASIADNIRlgrpgATDEQVQAaarqaqihDRVMELpQGYDTVLGSEGSDLSGG 486
Cdd:PRK13409 153 KKLYNGEI--KVVHkpqyVDLIPKVFKGKVRELLK-----KVDERGKL--------DEVVER-LGLENILDRDISELSGG 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 487 EAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHR---LDTIvhADQILVLVG 555
Cdd:PRK13409 217 ELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDlavLDYL--ADNVHIAYG 286
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
361-569 |
1.63e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.19 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR--VAVVFQDS------MLL 432
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRqqVATVFQDPeqqifyTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 RASIADNIR-LGRPGATdeqvqaaarqaqIHDRVMELPqgydTVLGSEG------SDLSGGEAQRVAIARAIVQDAPILV 505
Cdd:PRK13638 96 DSDIAFSLRnLGVPEAE------------ITRRVDEAL----TLVDAQHfrhqpiQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 506 LDEATAHADPENET---AIQKALnaLAKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK13638 160 LDEPTAGLDPAGRTqmiAIIRRI--VAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
361-562 |
1.73e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.48 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLI---PRFwDPVSGSVRMNGTELPQMASGEvlsR----VAVVFQD----- 428
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPKY-EVTSGSILLDGEDILELSPDE---RaragIFLAFQYpveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 429 ----SMLLRASIaDNIRLGRPGATDEQVQAAARQaqihdRVMELPQGYdtvLGSE-GSDLSGGEAQRVAIARAIVQDAPI 503
Cdd:COG0396 91 gvsvSNFLRTAL-NARRGEELSAREFLKLLKEKM-----KELGLDEDF---LDRYvNEGFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 504 LVLDEATAHADPENETAIQKALNALA-KGRTTVVIAH--RLDTIVHADQILVLVGGKVVERG 562
Cdd:COG0396 162 AILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
362-562 |
2.14e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.81 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRF--WDPVSGS-VRMNGTELP---QMASGEVLSR--VAVVFQDSMLL- 432
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGShIELLGRTVQregRLARDIRKSRanTGYIFQQFNLVn 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 RASIADNIRLGRPGATD------------------EQVQAAARQAQIHDRVmelpqgydtvlgsegSDLSGGEAQRVAIA 494
Cdd:PRK09984 100 RLSVLENVLIGALGSTPfwrtcfswftreqkqralQALTRVGMVHFAHQRV---------------STLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 495 RAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLD-TIVHADQILVLVGGKVVERG 562
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
361-580 |
2.80e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.09 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLI----PRFWDPVSGSVRMNGTELPQMASGE---VLSR-VAVVFQDSMll 432
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcgitKDNWHVTADRFRWNGIDLLKLSPRErrkIIGReIAMIFQEPS-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 rASIADNIRLGR------PGATDEQVQAAARQAQiHDRVMEL-----PQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDA 501
Cdd:COG4170 100 -SCLDPSAKIGDqlieaiPSWTFKGKWWQRFKWR-KKRAIELlhrvgIKDHKDIMNSYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 502 PILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH-Y-AA 576
Cdd:COG4170 178 RLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKSPHHpYtKA 257
|
....
gi 506241759 577 LWRS 580
Cdd:COG4170 258 LLRS 261
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
343-571 |
4.80e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 343 VCMEFEGVAfaygenlpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQM--ASGEVLS 420
Cdd:PRK15439 17 ISKQYSGVE---------VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 rVAVVFQDSMLL-RASIADNIRLGRPGATDEQVqaaarqaqihdRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAI 497
Cdd:PRK15439 88 -IYLVPQEPLLFpNLSVKENILFGLPKRQASMQ-----------KMKQLLAalGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 498 VQDAPILVLDEATAHADP-ENETAIQKALNALAKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAAD 571
Cdd:PRK15439 156 MRDSRILILDEPTASLTPaETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDD 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
347-558 |
4.94e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 347 FEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTE----LPQ----MASGEV 418
Cdd:COG0488 1 LENLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigyLPQepplDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 419 LSRVAVVFQDSMLLRASIADNIRlgrpgATDEQVQAAARQAQIHDRvMELPQGYD------TVLGSEG----------SD 482
Cdd:COG0488 79 LDTVLDGDAELRALEAELEELEA-----KLAEPDEDLERLAELQEE-FEALGGWEaearaeEILSGLGfpeedldrpvSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 483 LSGGEAQRVAIARAIVQDAPILVLDEATAHADPEnetAIQKALNALAKGRTTV-VIAH-R--LDTIVhaDQILVLVGGKV 558
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE---SIEWLEEFLKNYPGTVlVVSHdRyfLDRVA--TRILELDRGKL 227
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-317 |
6.89e-13 |
|
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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 69.49 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 24 IIGNVAIAALSSACEFV-PYLAIARVAQLSITEGVPPsdvLAMWVLVAVAGAAAGRMLFSMATGRC-HYADADFRVHVRT 101
Cdd:cd18778 1 LILTLLCALLSTLLGLVpPWLIRELVDLVTIGSKSLG---LLLGLALLLLGAYLLRALLNFLRIYLnHVAEQKVVADLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 102 VLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVVIGVA 181
Cdd:cd18778 78 DLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 182 WPFMMRdFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAcyvwtkrNGNAfSWVSALFSP 261
Cdd:cd18778 158 WLYSKK-VRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKA-------QLRA-MKLWAIFHP 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506241759 262 GAM--------LVVLLAATLAFvaNGVLPLERCVPFLVLGVGIPAGLVNLFRSIRMLQMSLQAA 317
Cdd:cd18778 229 LMEfltslgtvLVLGFGGRLVL--AGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGA 290
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
362-573 |
8.12e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.05 E-value: 8.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQD-----------SM 430
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDpstslnprqriSQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 431 LLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGydtvlgsegsdLSGGEAQRVAIARAIVQDAPILVLDEAT 510
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 511 AHADPENETAIQKALNAL--AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH 573
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASPLH 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
361-538 |
9.17e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.59 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAvvFQDSMLLRASIADNI 440
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 441 RLGRP--GATDEQVQAAARQAQIHDrVMELPQGYdtvlgsegsdLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENE 518
Cdd:PRK13539 95 EFWAAflGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|
gi 506241759 519 TAIQKALNALAKGRTTVVIA 538
Cdd:PRK13539 164 ALFAELIRAHLAQGGIVIAA 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
365-569 |
1.62e-12 |
|
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: 70.22 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 365 VDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVR-------MNGTELPQMASGEVLSRVAVVFQD-SMLLRASI 436
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQEyDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 ADN----IRLGRPgatDEQVQAAArqaqIHDRVMelpQGYD-----TVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLD 507
Cdd:TIGR03269 383 LDNlteaIGLELP---DELARMKA----VITLKM---VGFDeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 508 EATAHADPENETAIQKA-LNALAK-GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLA 569
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSiLKAREEmEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
350-562 |
1.71e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.57 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 350 VAFAYGENLPFVLQ---DVDVALEPGTVTALVGDSGSGKTTL-----ARLIPRfwdpvSGSVRMN-GTELPQMASGEVLS 420
Cdd:PRK13651 8 IVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFiehlnALLLPD-----TGTIEWIfKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 -----------------------RVAVVFQ--DSMLLRASIADNIRLG-RPGATDEQVQAAARQAQIhdRVMELPQGYdt 474
Cdd:PRK13651 83 vleklviqktrfkkikkikeirrRVGVVFQfaEYQLFEQTIEKDIIFGpVSMGVSKEEAKKRAAKYI--ELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 475 vLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIVH-ADQILV 552
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVLEwTKRTIF 237
|
250
....*....|
gi 506241759 553 LVGGKVVERG 562
Cdd:PRK13651 238 FKDGKIIKDG 247
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
361-562 |
1.81e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.93 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLAR-LIPRFWDP-------VSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLL 432
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 RASIADNI-RLGRPGATDEQVQAAARQAQIHDRVMELpQGYDTVLGSEGSDLSGGEAQRVAIARAIVQ---------DAP 502
Cdd:PRK13547 96 FAFSAREIvLLGRYPHARRAGALTHRDGEIAWQALAL-AGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 503 ILVLDEATAHADPENETAIQKALNALAK----GRTTVV----IAHRldtivHADQILVLVGGKVVERG 562
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVhdpnLAAR-----HADRIAMLADGAIVAHG 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
361-553 |
1.82e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 67.07 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVR-MNGTELPQMASGE--------------------VL 419
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvRHDGGWVDLAQASpreilalrrrtigyvsqflrVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 SRVA---VVFQDsmLLRASIADNIRLGRPGAtdeqvqaAARQAQIHDRVMELPQgydtvlgsegSDLSGGEAQRVAIARA 496
Cdd:COG4778 106 PRVSaldVVAEP--LLERGVDREEARARARE-------LLARLNLPERLWDLPP----------ATFSGGEQQRVNIARG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 497 IVQDAPILVLDEATAHADPEN-ETAIQKALNALAKGRTTVVIAHRLDTIVH-ADQILVL 553
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANrAVVVELIEEAKARGTAIIGIFHDEEVREAvADRVVDV 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
345-560 |
2.69e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVafayGENLPFV--LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVL-SR 421
Cdd:PRK11288 5 LSFDGI----GKTFPGVkaLDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALaAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 VAVVFQDSMLL-RASIADNIRLG----RPGATDEQVQAAARQAQIHDRVMEL-PqgyDTVLGSegsdLSGGEAQRVAIAR 495
Cdd:PRK11288 81 VAIIYQELHLVpEMTVAENLYLGqlphKGGIVNRRLLNYEAREQLEHLGVDIdP---DTPLKY----LSIGQRQMVEIAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 496 AIVQDAPILVLDEAT---AHADPENETAIQKALNalAKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVE 560
Cdd:PRK11288 154 ALARNARVIAFDEPTsslSAREIEQLFRVIRELR--AEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
345-567 |
2.70e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.59 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMAsgeVLSR-VA 423
Cdd:PRK11432 7 VVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQRdIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 424 VVFQDSMLL-RASIADNI-----RLGRPGAtdeqvqaaarqaQIHDRVMELPQGYDtVLGSEG---SDLSGGEAQRVAIA 494
Cdd:PRK11432 82 MVFQSYALFpHMSLGENVgyglkMLGVPKE------------ERKQRVKEALELVD-LAGFEDryvDQISGGQQQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 495 RAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAH-RLDTIVHADQILVLVGGKVVERGVHEEL 567
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
345-567 |
3.39e-12 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 66.24 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQmASGEVLSRVAV 424
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDSMLLRASIA-DNI----RL-GRPGA-----TDEQVqaaarqaqihdRVMELPQGYDTVLGSegsdLSGGEAQRVAI 493
Cdd:cd03265 78 VFQDLSVDDELTGwENLyihaRLyGVPGAerrerIDELL-----------DFVGLLEAADRLVKT----YSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 494 ARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEEL 567
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
343-593 |
4.87e-12 |
|
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: 68.68 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 343 VCMEFEGVAfaygenlpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRF--WDPVSGSVRMN-------------- 406
Cdd:TIGR03269 6 LTKKFDGKE---------VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 407 --GTELP----QMASGEV-------------LSRVAVVFQDSMLL--RASIADNI-----RLGRPG--ATDEQVQAAARQ 458
Cdd:TIGR03269 77 kvGEPCPvcggTLEPEEVdfwnlsdklrrriRKRIAIMLQRTFALygDDTVLDNVlealeEIGYEGkeAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 459 AQIHdRVMELPQgydtvlgsegsDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVV 536
Cdd:TIGR03269 157 QLSH-RITHIAR-----------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 537 IAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAAdghyaalwRSQQVDALEKALLVE 593
Cdd:TIGR03269 225 TSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVAV--------FMEGVSEVEKECEVE 274
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
362-557 |
5.90e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.42 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLI----PrfWDPVSGSVRMNGTELpqMASGEVLSR---VAVVFQDSMLLRA 434
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyP--HGTYEGEIIFEGEEL--QASNIRDTEragIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 435 -SIADNIRLG----RPGATDeqvqaaarQAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLD 507
Cdd:PRK13549 97 lSVLENIFLGneitPGGIMD--------YDAMYLRAQKLLAqlKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 508 EATAhADPENETAIqkALNAL----AKGRTTVVIAHRLDTIVH-ADQILVLVGGK 557
Cdd:PRK13549 169 EPTA-SLTESETAV--LLDIIrdlkAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
354-555 |
7.06e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.27 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 354 YGEN------LPfvlqdvdvALEPGTVTALVGDSGSGKTTLAR-----LIPRF--------WDPVSGSVRmnGTELPQ-- 412
Cdd:COG1245 83 YGENgfrlygLP--------VPKKGKVTGILGPNGIGKSTALKilsgeLKPNLgdydeepsWDEVLKRFR--GTELQDyf 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 413 --MASGEVlsRVAVVFQDSMLLRASIADNIR--LGRpgaTDEqvqaaarqaqiHDRVMELPQ--GYDTVLGSEGSDLSGG 486
Cdd:COG1245 153 kkLANGEI--KVAHKPQYVDLIPKVFKGTVRelLEK---VDE-----------RGKLDELAEklGLENILDRDISELSGG 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241759 487 EAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHR---LDTIvhADQILVLVG 555
Cdd:COG1245 217 ELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEeGKYVLVVEHDlaiLDYL--ADYVHILYG 287
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
354-555 |
7.75e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.85 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 354 YGENlPFVLQDVDVAlEPGTVTALVGDSGSGKTT----LA-RLIPRF--------WDPVSGSVRmnGTEL----PQMASG 416
Cdd:cd03236 10 YGPN-SFKLHRLPVP-REGQVLGLVGPNGIGKSTalkiLAgKLKPNLgkfddppdWDEILDEFR--GSELqnyfTKLLEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 417 EVlsRVAVVFQDSMLLRASIADNIR--LGRpgaTDEQVQAAARQaqihdRVMELpqgyDTVLGSEGSDLSGGEAQRVAIA 494
Cdd:cd03236 86 DV--KVIVKPQYVDLIPKAVKGKVGelLKK---KDERGKLDELV-----DQLEL----RHVLDRNIDQLSGGELQRVAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241759 495 RAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIVH-ADQILVLVG 555
Cdd:cd03236 152 AALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLAVLDYlSDYIHCLYG 214
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
365-580 |
8.59e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 66.75 E-value: 8.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 365 VDVALEPGTVTALVGDSGSGKTTLARLI----PRFWDPVSGSVRMNGTELPQMASGE----VLSRVAVVFQDSmllRASI 436
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRErrklVGHNVSMIFQEP---QSCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 ADNIRLGR------PGATDEQVQAAARQAQiHDRVMEL-----PQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILV 505
Cdd:PRK15093 103 DPSERVGRqlmqniPGWTYKGRWWQRFGWR-KRRAIELlhrvgIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 506 LDEATAHADPENETAIQKALNALAKGRTTVV--IAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH-YA-ALWRS 580
Cdd:PRK15093 182 ADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQwADKINVLYCGQTVETAPSKELVTTPHHpYTqALIRA 261
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
344-559 |
1.20e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 344 CMEFEGVAFAY--GENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEV--L 419
Cdd:PRK10535 4 LLELKDIRRSYpsGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 SR--VAVVFQDSMLL-RASIADNIRLGRPGATDEQVQAAARQAQIHDRVmelpqGYDTVLGSEGSDLSGGEAQRVAIARA 496
Cdd:PRK10535 84 RRehFGFIFQRYHLLsHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRL-----GLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 497 IVQDAPILVLDEATAHADP---ENETAIQKALNalAKGRTTVVIAHRLDTIVHADQILVLVGGKVV 559
Cdd:PRK10535 159 LMNGGQVILADEPTGALDShsgEEVMAILHQLR--DRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
349-573 |
1.22e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 349 GVAFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLA----RLIPRfwDPV---SGSVRMNGTELPQmASGEVL-- 419
Cdd:PRK15134 12 SVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlsilRLLPS--PPVvypSGDIRFHGESLLH-ASEQTLrg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 ---SRVAVVFQDSML-------LRASIADNIRLGRpGATDEQVQAaarqaqihdrvmELPQGYDTV--------LGSEGS 481
Cdd:PRK15134 89 vrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLHR-GMRREAARG------------EILNCLDRVgirqaakrLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 482 DLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDtIVH--ADQILVLVGGK 557
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLS-IVRklADRVAVMQNGR 234
|
250
....*....|....*.
gi 506241759 558 VVERGVHEELLAADGH 573
Cdd:PRK15134 235 CVEQNRAATLFSAPTH 250
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
361-542 |
1.25e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPR--FWDPVSGSVRMNGTELPQmasgevlsrvavvfqdsmllRASIAD 438
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGR--------------------EASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIrlGRPGATDEqvqaaarqaqihdrVMElpqgydtVLGSEG-----------SDLSGGEAQRVAIARAIVQDAPILVLD 507
Cdd:COG2401 105 AI--GRKGDFKD--------------AVE-------LLNAVGlsdavlwlrrfKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 506241759 508 EATAHADPENETAIQKALNALAK--GRTTVVIAHRLD 542
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARraGITLVVATHHYD 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
368-568 |
1.37e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 368 ALEPGTVTALVGDSGSGKTT-LARLIPRFwdPVSGSVRMNGTELPQMASGEvLSRVavvfqdsmllRASIADNIR----- 441
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTlLARMAGLL--PGSGSIQFAGQPLEAWSAAE-LARH----------RAYLSQQQTppfam 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 442 -------LGRPGATDEQVQAAARqaqihDRVMELPQGYDTvLGSEGSDLSGGEAQRVAIARAIVQDAP-------ILVLD 507
Cdd:PRK03695 85 pvfqyltLHQPDKTRTEAVASAL-----NEVAEALGLDDK-LGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506241759 508 EATAHADPENETAIQKALNALA-KGRTTVVIAHRLD-TIVHADQILVLVGGKVVERGVHEELL 568
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCqQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
372-555 |
1.73e-11 |
|
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: 64.74 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 372 GTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL---PQMASGEVLSRVavvfqDSMLlrASIADNIRLGRPGAT 448
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykPQYIKADYEGTV-----RDLL--SSITKDFYTHPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 449 DeqvqaaarqaqihdrVMElPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALN-- 526
Cdd:cd03237 98 E---------------IAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRrf 161
|
170 180 190
....*....|....*....|....*....|
gi 506241759 527 ALAKGRTTVVIAHRLDTIVH-ADQILVLVG 555
Cdd:cd03237 162 AENNEKTAFVVEHDIIMIDYlADRLIVFEG 191
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
371-565 |
1.85e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 371 PGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTEL----PQmASGEvlSRVAVVFQDSMLL-RASIADNIRLGRP 445
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngPK-SSQE--AGIGIIHQELNLIpQLTIAENIFLGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 446 -----GATDEQVQAAARqaqihDRVME---LPQGYDTVLGsegsDLSGGEAQRVAIARAIVQDAPILVLDEAT-AHADPE 516
Cdd:PRK10762 106 fvnrfGRIDWKKMYAEA-----DKLLArlnLRFSSDKLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506241759 517 NEtAIQKALNAL-AKGRTTVVIAHRLDTIVH-ADQILVLVGGK-VVERGVHE 565
Cdd:PRK10762 177 TE-SLFRVIRELkSQGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAEREVAD 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
362-562 |
2.32e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMA---SGEVlsRVAVVFQD-SMLLRASIA 437
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQL--GIGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 438 DNIRLGRPGATDEQVQAAARQAQIHDR--VMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADP 515
Cdd:PRK09700 99 ENLYIGRHLTKKVCGVNIIDWREMRVRaaMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506241759 516 ENETAIQKALNALAK-GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERG 562
Cdd:PRK09700 179 KEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
329-559 |
3.11e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 329 LAEPERPRPAAEGPVCMEFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGT 408
Cdd:COG3845 242 VLLRVEKAPAEPGEVVLEVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 409 ELPQMASGEVLSR-VAVV----FQDSMLLRASIADNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEG--- 480
Cdd:COG3845 321 DITGLSPRERRRLgVAYIpedrLGRGLVPDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDtpa 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 481 SDLSGGEAQRVAIARAIVQDAPILV-------LDEATAHadpenetAIQKALNALA-KGRTTVVIAHRLDTIV-HADQIL 551
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIaaqptrgLDVGAIE-------FIHQRLLELRdAGAAVLLISEDLDEILaLSDRIA 473
|
....*...
gi 506241759 552 VLVGGKVV 559
Cdd:COG3845 474 VMYEGRIV 481
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
361-569 |
3.21e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.73 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLAR-LIPRFwdpvsgsvrmngtelpQMASGEVLSR--VAVVFQDSMLLRASIA 437
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQF----------------EISEGRVWAErsIAYVPQQAWIMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 438 DNIRLGRPGATDEQVQAAARQAQIHDrVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPE- 516
Cdd:PTZ00243 739 GNILFFDEEDAARLADAVRVSQLEAD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHv 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 517 NETAIQKA-LNALAkGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLA 569
Cdd:PTZ00243 818 GERVVEECfLGALA-GKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
343-559 |
4.66e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 343 VCMEFEGVAfaygenlpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVL-SR 421
Cdd:PRK10982 4 ISKSFPGVK---------ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALeNG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 VAVVFQD-SMLLRASIADNIRLGR---PGATDEQVQAAARQAQIHDrvmELpqGYDTVLGSEGSDLSGGEAQRVAIARAI 497
Cdd:PRK10982 75 ISMVHQElNLVLQRSVMDNMWLGRyptKGMFVDQDKMYRDTKAIFD---EL--DIDIDPRAKVATLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506241759 498 VQDAPILVLDEATAHADPENETAIQKALNAL-AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVV 559
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLkERGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
360-567 |
4.96e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 64.86 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 360 FVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASgeVLSRVAVVFQDSMLL-RASIAD 438
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFpHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRLGrpgatdeQVQAAARQAQIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPE 516
Cdd:PRK11607 111 NIAFG-------LKQDKLPKAEIASRVNEMLGlvHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 517 NETAIQ-KALNALAK-GRTTVVIAH-RLDTIVHADQILVLVGGKVVERGVHEEL 567
Cdd:PRK11607 184 LRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-559 |
8.66e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.80 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRA---SIA 437
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMGTApsmTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 438 DNIRLG---------RPGATDEQVQAaarqaqIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDE 508
Cdd:COG1101 101 ENLALAyrrgkrrglRRGLTKKRREL------FRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 509 ATAHADPENETAIQKALNALAKGR--TTVVIAHRL-DTIVHADQILVLVGGKVV 559
Cdd:COG1101 175 HTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMeQALDYGNRLIMMHEGRII 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
361-562 |
1.16e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.39 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLI---PRFwDPVSGSVRMNGTELPQMASGE-VLSRVAVVFQDSMLLrasi 436
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPKY-EVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEI---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 adnirlgrPGATdeqvqaaarqaqihdrVMELPQGYDtvlgsEGsdLSGGEAQRVAIARAIVQDAPILVLDEATAHADPE 516
Cdd:cd03217 90 --------PGVK----------------NADFLRYVN-----EG--FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506241759 517 NETAIQKALNALA-KGRTTVVIAH--RLDTIVHADQILVLVGGKVVERG 562
Cdd:cd03217 139 ALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
361-553 |
1.42e-10 |
|
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: 60.97 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNI 440
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 441 RLGRPGATDEQVQAAARQAQIHDrVMELPQGYdtvlgsegsdLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETA 520
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGLNG-FEDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|...
gi 506241759 521 IQKALNALAKGRTTVVIAHRLDTIVHADQILVL 553
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
362-571 |
2.85e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVFQDSMLLRASIADNIR 441
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 442 LGRPGatdeqvqaaarqaqiHDRVMELPQGYDTVLGSEG--------------SDLSGGEAQRVAIARAIVQDAPILVLD 507
Cdd:PRK15056 103 MGRYG---------------HMGWLRRAKKRDRQIVTAAlarvdmvefrhrqiGELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 508 EATAHADPENETAIQKALNAL-AKGRTTVVIAHRLDTIVHADQILVLVGGKVVERGVHEELLAAD 571
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAE 232
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
362-562 |
4.05e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 59.26 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRfwdpVSGSVRMNGTElpqmasgEVLSRVAVVFQDSmlLRASIADNIr 441
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARLISFL-------PKFSRNKLIFIDQ--LQFLIDVGL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 442 lgrpgatdeqvqaaarqaqihdrvmelpqGYDTvLGSEGSDLSGGEAQRVAIARAIVQDAP--ILVLDEATAHADPENET 519
Cdd:cd03238 77 -----------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 506241759 520 AIQKALNAL-AKGRTTVVIAHRLDTIVHADQILVL------VGGKVVERG 562
Cdd:cd03238 127 QLLEVIKGLiDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
361-570 |
4.24e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.48 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTelpqMASgeVLSrVAVVFQDSMLLRasiaDNI 440
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSA--LLE-LGAGFHPELTGR----ENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 441 RLG------RPGATDEqvqaaarqaqIHDRVMELpqgydtvlgsegSDL-----------SGGEAQRVAIARAIVQDAPI 503
Cdd:COG1134 110 YLNgrllglSRKEIDE----------KFDEIVEF------------AELgdfidqpvktySSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 504 LVLDEATAHADPE-NETAIQKALNALAKGRTTVVIAHRLDTIV-HADQILVLVGGKVVERGVHEELLAA 570
Cdd:COG1134 168 LLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRrLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
99-320 |
4.99e-10 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. 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. 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: 349995 [Multi-domain] Cd Length: 289 Bit Score: 60.91 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 99 VRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVVI 178
Cdd:cd18551 71 LRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 179 GVAWPFMMRdFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELakacyvwtKRNGNAFSWVSAL 258
Cdd:cd18551 151 LIILPLGRR-IRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERL--------YRAGLKAAKIEAL 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 259 FSPGAMLVVLLA--ATLAF----VANGVLPLERCVPFLVLGVGIPAGLVNLFRSIRMLQMSLQAADHL 320
Cdd:cd18551 222 IGPLMGLAVQLAllVVLGVggarVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
374-558 |
5.30e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.72 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 374 VTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELpQMASGEVLSRVAVVFQDSMLLR-ASIADNIRL-----GRpgA 447
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHILFyaqlkGR--S 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 448 TDEQVqaaarqaqIHDRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNA 527
Cdd:TIGR01257 1035 WEEAQ--------LEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180 190
....*....|....*....|....*....|..
gi 506241759 528 LAKGRTTVVIAHRLDTI-VHADQILVLVGGKV 558
Cdd:TIGR01257 1107 YRSGRTIIMSTHHMDEAdLLGDRIAIISQGRL 1138
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
362-562 |
9.19e-10 |
|
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: 59.55 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLAR--LIPRFwdpvsgSVRMNGTELPQMASGEV-----LSRVAVVFQDSM---- 430
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPAL------ARRLHLKKEQPGNHDRIeglehIDKVIVIDQSPIgrtp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 431 ------------LLR-----------------------ASIADNIRLgrpgATDEQVQAAARQAQIHDRVMELPQ---GY 472
Cdd:cd03271 85 rsnpatytgvfdEIRelfcevckgkrynretlevrykgKSIADVLDM----TVEEALEFFENIPKIARKLQTLCDvglGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 473 DTvLGSEGSDLSGGEAQRVAIARAIVQDAP---ILVLDEATAHADPENetaIQKALNAL----AKGRTTVVIAHRLDTIV 545
Cdd:cd03271 161 IK-LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHD---VKKLLEVLqrlvDKGNTVVVIEHNLDVIK 236
|
250 260
....*....|....*....|...
gi 506241759 546 HADQILVL------VGGKVVERG 562
Cdd:cd03271 237 CADWIIDLgpeggdGGGQVVASG 259
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
341-551 |
1.53e-09 |
|
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: 60.72 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 341 GPVCMEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTelpqmasgevls 420
Cdd:TIGR03719 319 GDKVIEAENLTKAFGDKL--LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET------------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 rVAVVFQDSMllRASIADN-------------IRLGRpgatdeqvqaaarqaqihdrvMELP-QGYDTVLGSEGSD---- 482
Cdd:TIGR03719 385 -VKLAYVDQS--RDALDPNktvweeisggldiIKLGK---------------------REIPsRAYVGRFNFKGSDqqkk 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 483 ---LSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKgrTTVVIAH-R--LDTIvhADQIL 551
Cdd:TIGR03719 441 vgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdRwfLDRI--ATHIL 511
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
356-591 |
1.59e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.76 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 356 ENLPFVLQD-VDVALEPGTVTALVGDSGSGKTTLARLIPRFWD-P---VSGSVRMNGTELPQMASGE----VLSRVAVVF 426
Cdd:PRK11022 16 ESAPFRAVDrISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKErrnlVGAEVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 427 QDSML-------LRASIADNIRLGRPGATDEQvqaaarqaqiHDRVMEL--------PQGYDTVLGSEgsdLSGGEAQRV 491
Cdd:PRK11022 96 QDPMTslnpcytVGFQIMEAIKVHQGGNKKTR----------RQRAIDLlnqvgipdPASRLDVYPHQ---LSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 492 AIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTT--VVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELL 568
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIF 242
|
250 260
....*....|....*....|....*
gi 506241759 569 AADGH-YA-ALWRSQQVDALEKALL 591
Cdd:PRK11022 243 RAPRHpYTqALLRALPEFAQDKARL 267
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
364-576 |
1.78e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 364 DVDVALEPGTVTALVGDSGSGK--TTLARL--IPRFWDPVSGSVRMNGTELpqmASGEVLSR-VAVVFQDSmllRA---- 434
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKslTCAAALgiLPAGVRQTAGRVLLDGKPV---APCALRGRkIATIMQNP---RSafnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 435 --SIADNIR-----LGRPgATDEQVQAAARQAQIHDRvmelpqgyDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLD 507
Cdd:PRK10418 95 lhTMHTHARetclaLGKP-ADDATLTAALEAVGLENA--------ARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 508 EATAHADPENETAIQKALNALAKGRT--TVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGHYAA 576
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
476-567 |
1.99e-09 |
|
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: 60.80 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 476 LGSEGSDLSGGEAQRVAIARAIVQDA---PILVLDEATA--HADPenetaIQKALNAL----AKGRTTVVIAHRLDTIVH 546
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTglHFDD-----IKKLLEVLqrlvDKGNTVVVIEHNLDVIKT 897
|
90 100
....*....|....*....|....*..
gi 506241759 547 ADQILVL------VGGKVVERGVHEEL 567
Cdd:TIGR00630 898 ADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
362-508 |
2.01e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 57.88 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDP---VSGSVRMNGTELpqmASGEVLSR-VAVVFQDsMLLRA--S 435
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL---TALPAEQRrIGILFQD-DLLFPhlS 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 436 IADNIRLGRPGATDEQVQaaarqaqiHDRVME-LPQ-GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDE 508
Cdd:COG4136 93 VGENLAFALPPTIGRAQR--------RARVEQaLEEaGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
93-320 |
2.80e-09 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. 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: 350020 [Multi-domain] Cd Length: 289 Bit Score: 58.65 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 93 ADFRVHvrtvLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVA 172
Cdd:cd18576 69 ADLRKD----LYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 173 YFVVVIGVAwpfmmRDFG----PLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKacyVWTKRn 248
Cdd:cd18576 145 TVPVVVLVA-----VLFGrrirKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVK---LALKR- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 249 gnafSWVSALFSP-------GAMLVVL-LAATLafVANGVLPLERCVPFLVLG--VGIP-AGLVNLFRSirmLQMSLQAA 317
Cdd:cd18576 216 ----ARIRALFSSfiifllfGAIVAVLwYGGRL--VLAGELTAGDLVAFLLYTlfIAGSiGSLADLYGQ---LQKALGAS 286
|
...
gi 506241759 318 DHL 320
Cdd:cd18576 287 ERV 289
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
361-539 |
2.92e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.98 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMAS--GEVLSRVAvvFQDSMLLRASIAD 438
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDepHENILYLG--HLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NIRLGRP--GATDEQVQAAARQAQIHDRVmELPQGYdtvlgsegsdLSGGEAQRVAIARAIVQDAPILVLDEATAHADPE 516
Cdd:TIGR01189 93 NLHFWAAihGGAQRTIEDALAAVGLTGFE-DLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....
gi 506241759 517 NETAIQKALNA-LAKGRTTVVIAH 539
Cdd:TIGR01189 162 GVALLAGLLRAhLARGGIVLLTTH 185
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
362-562 |
4.54e-09 |
|
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: 57.27 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLA---------RlipRFWDPVSGSVR--MNGTELPQMASGEVLSRVAVVFQDSM 430
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqR---RYVESLSAYARqfLGQMDKPDVDSIEGLSPAIAIDQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 431 L--LRAS------IADNIRL--GRPGatdeqvqaaarqaqIHDRV---MELPQGYDTvLGSEGSDLSGGEAQRVAIARAI 497
Cdd:cd03270 88 SrnPRSTvgtvteIYDYLRLlfARVG--------------IRERLgflVDVGLGYLT-LSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506241759 498 VQ--DAPILVLDEATAHADPENETAIQKALNAL-AKGRTTVVIAHRLDTIVHADQILVL------VGGKVVERG 562
Cdd:cd03270 153 GSglTGVLYVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
362-573 |
5.17e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.10 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNG----------TELPQMASGEVL----SRVAVVFQ 427
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 428 DSML-------LRASIADNIRLGRPGATDEQVQAAARQAqihDRVmELPQGyDTVLGSEGSDLSGGEAQRVAIARAIVQD 500
Cdd:PRK10261 112 EPMTslnpvftVGEQIAESIRLHQGASREEAMVEAKRML---DQV-RIPEA-QTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 501 APILVLDEATAHADPENETAIQKALNALAKGRT--TVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLAADGH 573
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
361-562 |
6.68e-09 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 56.39 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMAsgevlsrVAVVFQDSMLLRasiaDNI 440
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG-------LGGGFNPELTGR----ENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 441 R-----LGRPGAtdeqvqaaARQAQIHDRVM--ELPQGYDTVLGSegsdLSGGEAQRVAIARAIVQDAPILVLDEATAHA 513
Cdd:cd03220 106 YlngrlLGLSRK--------EIDEKIDEIIEfsELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506241759 514 DPE-NETAIQKALNALAKGRTTVVIAHRLDTIV-HADQILVLVGGKVVERG 562
Cdd:cd03220 174 DAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
371-550 |
1.05e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.30 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 371 PGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVvfqdsmllrasiadnirlgrpgatde 450
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 451 qvqaaarqaqihdrvmelpqgydtvlGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKA------ 524
Cdd:smart00382 55 --------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrll 108
|
170 180
....*....|....*....|....*.
gi 506241759 525 LNALAKGRTTVVIAHRLDTIVHADQI 550
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALL 134
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
361-515 |
1.11e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.19 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTE----------------LPQMASgevlsrvav 424
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmhkrarlgigyLPQEAS--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 425 VFQDsmlLraSIADNIR-----LGRPGATdeqvqaaarqaqIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAI 497
Cdd:COG1137 89 IFRK---L--TVEDNILavlelRKLSKKE------------REERLEELLEefGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170
....*....|....*...
gi 506241759 498 VQDAPILVLDEATAHADP 515
Cdd:COG1137 152 ATNPKFILLDEPFAGVDP 169
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-544 |
1.13e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFwDPVSGSVRMNG-TELPQMASGE-------VLSRVAVVFQDSMLL 432
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrVEFFNQNIYErrvnlnrLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 RASIADNIRLG------RPGAT-DEQVQAAARQAQIHDRVmelpqgyDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILV 505
Cdd:PRK14258 101 PMSVYDNVAYGvkivgwRPKLEiDDIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 506241759 506 LDEATAHADPENETAIQKALNA--LAKGRTTVVIAHRLDTI 544
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQV 214
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
361-562 |
1.35e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 56.11 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLI---PRFwDPVSGSVRMNGTELPQMasgEVLSR----VAVVFQ------ 427
Cdd:TIGR01978 15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghPSY-EVTSGTILFKGQDLLEL---EPDERaragLFLAFQypeeip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 428 ---DSMLLRASIadNIRLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLGSEGsdLSGGEAQRVAIARAIVQDAPIL 504
Cdd:TIGR01978 91 gvsNLEFLRSAL--NARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEG--FSGGEKKRNEILQMALLEPKLA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 505 VLDEATAHADPENETAIQKALNALA-KGRTTVVIAH--RLDTIVHADQILVLVGGKVVERG 562
Cdd:TIGR01978 167 ILDEIDSGLDIDALKIVAEGINRLRePDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
342-562 |
1.38e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 342 PVCMEFEGVAF-----------AYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIP--RFWDPVSGSVRMNGT 408
Cdd:PLN03140 865 PLAMSFDDVNYfvdmpaemkeqGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGF 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 409 ELPQmasgEVLSRVA------------VVFQDSMLLRASiadnIRLGRPGATDEQVQAAarqaqihDRVMELPQG---YD 473
Cdd:PLN03140 945 PKKQ----ETFARISgyceqndihspqVTVRESLIYSAF----LRLPKEVSKEEKMMFV-------DEVMELVELdnlKD 1009
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 474 TVLGSEG-SDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKAL-NALAKGRTTVVIAHR--LDTIVHADQ 549
Cdd:PLN03140 1010 AIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQpsIDIFEAFDE 1089
|
250
....*....|....
gi 506241759 550 ILVLV-GGKVVERG 562
Cdd:PLN03140 1090 LLLMKrGGQVIYSG 1103
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
348-528 |
1.74e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 348 EGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNgtelPQMASGEVLSRVAVvfq 427
Cdd:PRK09544 8 ENVSVSFGQRR--VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----GKLRIGYVPQKLYL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 428 dSMLLRASIADNIRLgRPGATDEQ---VQAAARQAQIHDRVMElpqgydtvlgsegsDLSGGEAQRVAIARAIVQDAPIL 504
Cdd:PRK09544 79 -DTTLPLTVNRFLRL-RPGTKKEDilpALKRVQAGHLIDAPMQ--------------KLSGGETQRVLLARALLNRPQLL 142
|
170 180
....*....|....*....|....
gi 506241759 505 VLDEATAHADPENETAIQKALNAL 528
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQL 166
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
99-318 |
2.51e-08 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. 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. 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: 349996 [Multi-domain] Cd Length: 292 Bit Score: 55.89 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 99 VRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLvayFVVVI 178
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIA---LVVLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 179 GVAWPfmMRDFGPLNKRFN----EAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAcyvwtkrnGNAFSW 254
Cdd:cd18552 151 LAALP--IRRIGKRLRKISrrsqESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRL--------SMKIAR 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 255 VSALFSP------GAMLVVLLAATLAFVANGVLPLERCVPFLvlgvgipAGLVNLFRSIR-------MLQMSLQAAD 318
Cdd:cd18552 221 ARALSSPlmellgAIAIALVLWYGGYQVISGELTPGEFISFI-------TALLLLYQPIKrlsnvnaNLQRGLAAAE 290
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
361-557 |
2.72e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIP-RFW-DPVSGSVRMNGTELPQmasgEVLSRVAVVFQDSML-----LR 433
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPTK----QILKRTGFVTQDDILyphltVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 434 ASIADNIRLGRPGATDEQVQAAARQAQIHDrvMELPQGYDTVLG-SEGSDLSGGEAQRVAIARAIVQDAPILVLDEATAH 512
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISE--LGLTKCENTIIGnSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 506241759 513 ADPENETAIQKALNALA-KGRTTVVIAHRLDTIVHA--DQILVLVGGK 557
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
362-559 |
3.36e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.37 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRF-----WDpvsGSVRMNGTELPQMASGEVLSR-VAVVFQDSMLLRA- 434
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtWD---GEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 435 SIADNIRLGR----PGATDEQVQAAARQAQIHdRVMELPQGYDTvlgSEGSDLSGGEAQRVAIARAIVQDAPILVLDEAT 510
Cdd:TIGR02633 94 SVAENIFLGNeitlPGGRMAYNAMYLRAKNLL-RELQLDADNVT---RPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 511 AhADPENETAIqkALNAL----AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVV 559
Cdd:TIGR02633 170 S-SLTEKETEI--LLDIIrdlkAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
98-279 |
5.68e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU 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 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: 349986 [Multi-domain] Cd Length: 292 Bit Score: 54.74 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 98 HVRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVV 177
Cdd:cd18542 73 DLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 178 IGVAWpFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSR-------SRAGARYRAATEELAKacyVWtkrngn 250
Cdd:cd18542 153 ALFSY-VFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREdyeiekfDKENEEYRDLNIKLAK---LL------ 222
|
170 180 190
....*....|....*....|....*....|
gi 506241759 251 AFSW-VSALFSPGAMLVVLLAATLaFVANG 279
Cdd:cd18542 223 AKYWpLMDFLSGLQIVLVLWVGGY-LVING 251
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
348-568 |
6.34e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 348 EGVAFAYGENLPFvlQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSV--RMNG---TELPQMASGEV--LS 420
Cdd:PRK11701 10 RGLTKLYGPRKGC--RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyRMRDgqlRDLYALSEAERrrLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 421 RV--AVVFQ---DSMLLRASIADNI--RLGRPGAT------DEQVQAAARQAQIHDRVMELPQGYdtvlgsegsdlSGGE 487
Cdd:PRK11701 88 RTewGFVHQhprDGLRMQVSAGGNIgeRLMAVGARhygdirATAGDWLERVEIDAARIDDLPTTF-----------SGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 488 AQRVAIARAIVQdAPILVL-DEATAHADpeneTAIQKALNALAKGRTT------VVIAHRLDTI-VHADQILVLVGGKVV 559
Cdd:PRK11701 157 QQRLQIARNLVT-HPRLVFmDEPTGGLD----VSVQARLLDLLRGLVRelglavVIVTHDLAVArLLAHRLLVMKQGRVV 231
|
....*....
gi 506241759 560 ERGVHEELL 568
Cdd:PRK11701 232 ESGLTDQVL 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
348-569 |
6.51e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.74 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 348 EGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTT----LARLIPRfwD--------------PVSGSVRMNGTE 409
Cdd:PRK10895 7 KNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR--DagniiiddedisllPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 410 LPQMASgeVLSRVAVVfqDSMLLRASIADNIrlgrpgaTDEQVqaaarqaqiHDRVMELPQGYDT--VLGSEGSDLSGGE 487
Cdd:PRK10895 83 LPQEAS--IFRRLSVY--DNLMAVLQIRDDL-------SAEQR---------EDRANELMEEFHIehLRDSMGQSLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 488 AQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIA-HRL-DTIVHADQILVLVGGKVVERGVHE 565
Cdd:PRK10895 143 RRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPT 222
|
....
gi 506241759 566 ELLA 569
Cdd:PRK10895 223 EILQ 226
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
89-294 |
7.17e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 54.21 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 89 HYADADFRVHVRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFAL 168
Cdd:cd18561 61 HRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 169 LLVAyFVVVIGVAWPFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAcyvwTKRN 248
Cdd:cd18561 141 ILLV-FALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQA----TMKV 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 506241759 249 GNafswVSALFSPGAMLVVLLAATLA------FVANGVLPLERCVPFLVLGV 294
Cdd:cd18561 216 LA----VSLLSSGIMGLATALGTALAlgvgalRVLGGQLTLSSLLLILFLSR 263
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
364-567 |
7.91e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.35 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 364 DVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDP---VSGSVRMNGTE---LPQMASGEVLS-RVAVVFQDSMllrASI 436
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREilnLPEKELNKLRAeQISMIFQDPM---TSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 437 ADNIRLGrpgatdeqvqaaarqaqihDRVME---LPQGYDTVLGSEGS---------------------DLSGGEAQRVA 492
Cdd:PRK09473 111 NPYMRVG-------------------EQLMEvlmLHKGMSKAEAFEESvrmldavkmpearkrmkmyphEFSGGMRQRVM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 493 IARAIVQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHA---DQILVLVGGKVVERGVHEEL 567
Cdd:PRK09473 172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgicDKVLVMYAGRTMEYGNARDV 249
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
362-559 |
9.35e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 52.63 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDP--VSGSVRMNGTELP-----------QM--ASGEVLSRVAVVF 426
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDknfqrstgyveQQdvHSPNLTVREALRF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 427 qdSMLLRAsiadnirlgrpgatdeqvqaaarqaqihdrvmelpqgydtvlgsegsdLSGGEAQRVAIARAIVQDAPILVL 506
Cdd:cd03232 103 --SALLRG------------------------------------------------LSVEQRKRLTIGVELAAKPSILFL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 507 DEATAHADPENETAIQKALNALA-KGRTTVVIAHR--LDTIVHADQILVLV-GGKVV 559
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKLAdSGQAILCTIHQpsASIFEKFDRLLLLKrGGKTV 189
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
362-560 |
1.58e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIprfwdpvSGsVRMNGTelpqmASGEVLSRVAVV-FQDsmlLRAS----- 435
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVL-------SG-VYPHGS-----YEGEILFDGEVCrFKD---IRDSealgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 436 --------------IADNIRLGRPGAT------DEQvqaaarqaqiHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAI 493
Cdd:NF040905 81 viihqelalipylsIAENIFLGNERAKrgvidwNET----------NRRARELLAkvGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 494 ARAIVQDAPILVLDEATAHAdpeNETAIQKALNAL----AKGRTTVVIAHRLDTIVH-ADQILVLVGGKVVE 560
Cdd:NF040905 151 AKALSKDVKLLILDEPTAAL---NEEDSAALLDLLlelkAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
100-281 |
1.70e-07 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) 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: 349985 [Multi-domain] Cd Length: 293 Bit Score: 53.18 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 100 RTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVVIg 179
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 180 vawpFMMRDFGP-LNKRFN---EAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEElakacYVwtKRNgNAFSWV 255
Cdd:cd18541 155 ----LLVYRLGKkIHKRFRkvqEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEE-----YV--EKN-LRLARV 222
|
170 180
....*....|....*....|....*.
gi 506241759 256 SALFSPGAMLVVLLAATLAFVANGVL 281
Cdd:cd18541 223 DALFFPLIGLLIGLSFLIVLWYGGRL 248
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
482-555 |
4.09e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.65 E-value: 4.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 482 DLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVG 555
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFEG 147
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-266 |
6.03e-07 |
|
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: 51.36 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 24 IIGNVAIAALSSACEFV-PYLA---IARVAQLSITEGVPpsdVLAMWVLVAVAGAAAGRMLFSMATGR-CHYADADFRVH 98
Cdd:cd18563 1 LILGFLLMLLGTALGLVpPYLTkilIDDVLIQLGPGGNT---SLLLLLVLGLAGAYVLSALLGILRGRlLARLGERITAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 99 VRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALL-LVAYFVVV 177
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLvLIPVPLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 178 IGV--AWPFMMRDFGplnkRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKACYVWTKRNGNAFSWV 255
Cdd:cd18563 158 WGSyfFWKKIRRLFH----RQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLL 233
|
250
....*....|.
gi 506241759 256 SALFSPGAMLV 266
Cdd:cd18563 234 TFLTSLGTLIV 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
345-569 |
1.07e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.26 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 345 MEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLI---PRfwdPVSGSVRMNGTELPQMASGEVLSR 421
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdPR---ATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 422 -VAVVFQDSMLL-RASIADNIRLGRPGATDEQVQAAArqaqihDRVMEL-PQGYDTVLGSEGSdLSGGEAQRVAIARAIV 498
Cdd:PRK11614 81 aVAIVPEGRRVFsRMTVEENLAMGGFFAERDQFQERI------KWVYELfPRLHERRIQRAGT-MSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 499 QDAPILVLDEATAHADPeneTAIQKALNALAK----GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEELLA 569
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAP---IIIQQIFDTIEQlreqGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLA 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
365-567 |
1.16e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.37 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 365 VDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELpQMASGEVLSRVAVV--FQDSMLLRA-SIADNIR 441
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-EGLPGHQIARMGVVrtFQHVRLFREmTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 442 ---------------LGRPGATDEQVQAAARQAQIHDRVmelpqGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVL 506
Cdd:PRK11300 103 vaqhqqlktglfsglLKTPAFRRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506241759 507 DEATAHADPENETAIQKALNALAK--GRTTVVIAHRLDTIVH-ADQILVLVGGKVVERGVHEEL 567
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
98-289 |
1.50e-06 |
|
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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 50.26 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 98 HVRTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVV 177
Cdd:cd18565 88 DLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 178 IGVAWPFMMRdFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAcyvwtkrNGNAFSwVSA 257
Cdd:cd18565 168 IAGTYWFQRR-IEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDA-------NWRAIR-LRA 238
|
170 180 190
....*....|....*....|....*....|..
gi 506241759 258 LFSPGAMLVVLLAATLAFVANGVLPLERCVPF 289
Cdd:cd18565 239 AFFPVIRLVAGAGFVATFVVGGYWVLDGPPLF 270
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
361-538 |
2.50e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLARLIP----RFWDPVSGSVRMNGTELPQMA---SGEVL-SRVAVVFQDSMLL 432
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKkhyRGDVVyNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 433 RASIADNIRLGRPGATDEQVQAAARQAQIHDRVME---LPQGYDTVLGSE---GsdLSGGEAQRVAIARAIVQDAPILVL 506
Cdd:TIGR00956 156 GETLDFAARCKTPQNRPDGVSREEYAKHIADVYMAtygLSHTRNTKVGNDfvrG--VSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190
....*....|....*....|....*....|....*
gi 506241759 507 DEATAHADpeNETAIQ--KALNALAK-GRTTVVIA 538
Cdd:TIGR00956 234 DNATRGLD--SATALEfiRALKTSANiLDTTPLVA 266
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
374-551 |
3.18e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.37 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 374 VTALVGDSGSGKTTLARLIpRFwdPVSGSVRMN---GTELPQMA-SGEVLSRVAVVFQDS----MLLRASIAdnirlgrp 445
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAL-KY--ALTGELPPNskgGAHDPKLIrEGEVRAQVKLAFENAngkkYTITRSLA-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 446 gatdeqvqaaarqaqIHDRVMELPQG-YDTVLGSEGSDLSGGE------AQRVAIARAIVQDAPILVLDEATAHADPEN- 517
Cdd:cd03240 93 ---------------ILENVIFCHQGeSNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENi 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 506241759 518 ETAIQKALNALA--KGRTTVVIAHRLDTIVHADQIL 551
Cdd:cd03240 158 EESLAEIIEERKsqKNFQLIVITHDEELVDAADHIY 193
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
361-559 |
3.31e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 361 VLQDVDVALEPGTVTALVGDSGSGKTTLAR-LIPRFWDPV--SGSVRMNGTELP---QMASGEVLSrvavvfQDSML--- 431
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERVTTGVitGGDRLVNGRPLDssfQRSIGYVQQ------QDLHLpts 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 432 -LRASIADNIRLGRPGATDEQVQAAARQAQIhdRVMELPQGYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILV-LDEA 509
Cdd:TIGR00956 852 tVRESLRFSAYLRQPKSVSKSEKMEYVEEVI--KLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 506241759 510 TAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIVHA--DQILVLV-GGKVV 559
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAILFEefDRLLLLQkGGQTV 983
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
483-569 |
3.47e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.41 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 483 LSGGEAQRVAIARAIVQDAP---ILVLDEATA--H-ADpenetaIQK---ALNAL-AKGRTTVVIAHRLDTIVHADQILV 552
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTglHfHD------IRKlleVLHRLvDKGNTVVVIEHNLDVIKTADWIID 900
|
90 100
....*....|....*....|...
gi 506241759 553 L------VGGKVVERGVHEELLA 569
Cdd:COG0178 901 LgpeggdGGGEIVAEGTPEEVAK 923
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
136-281 |
3.52e-06 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. 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. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 48.98 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 136 QSVGHAPVDVTAALLSplipLVYLFTVDVRFALLLVAYFVVVIGVAWPFMmrdfGPLNKRFNEAMV---EVSSAAVEMVE 212
Cdd:cd18570 117 STTISLFLDLLMVIIS----GIILFFYNWKLFLITLLIIPLYILIILLFN----KPFKKKNREVMEsnaELNSYLIESLK 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 213 GIAVIKTFGSRSRAGARYRAATEELAKACYVwTKRNGNAFSWVSALFSPGAMLVVLLAATLaFVANGVL 281
Cdd:cd18570 189 GIETIKSLNAEEQFLKKIEKKFSKLLKKSFK-LGKLSNLQSSIKGLISLIGSLLILWIGSY-LVIKGQL 255
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
145-312 |
4.18e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 49.08 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 145 VTAALLSPLIpLVY---LFTVDVRFALLLVAYFVVVIGVAWpFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFG 221
Cdd:cd18779 120 LSALLDGTLV-LGYlalLFAQSPLLGLVVLGLAALQVALLL-ATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 222 SRSRAGARYraatEELAKACYVWTKRNGNAFSWVSALFSP---GAMLVVLLAATlAFVANGVLPLERCVPFLVLGVGIPA 298
Cdd:cd18779 198 AEDRALDRW----SNLFVDQLNASLRRGRLDALVDALLATlrlAAPLVLLWVGA-WQVLDGQLSLGTMLALNALAGAFLA 272
|
170
....*....|....
gi 506241759 299 GLVNLFRSIRMLQM 312
Cdd:cd18779 273 PLASLVGTAQQLQL 286
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
363-539 |
4.53e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 48.03 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 363 QDVDV-ALEPGTVTALVGDSGSGKTTLARLIP-RFWDPVSGSVRMNGTELpQMASGEVLSRVAVVFQdsmlLRASIADNI 440
Cdd:cd03279 18 QVIDFtGLDNNGLFLICGPTGAGKSTILDAITyALYGKTPRYGRQENLRS-VFAPGEDTAEVSFTFQ----LGGKKYRVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 441 RlgRPGATDEQVQaaarqaqihdRVMELPQG-YDTVLGSEGSDLSGGEAQRVAIARAI-----VQD---API--LVLDEA 509
Cdd:cd03279 93 R--SRGLDYDQFT----------RIVLLPQGeFDRFLARPVSTLSGGETFLASLSLALalsevLQNrggARLeaLFIDEG 160
|
170 180 190
....*....|....*....|....*....|.
gi 506241759 510 TAHADPENETAIQKALNALA-KGRTTVVIAH 539
Cdd:cd03279 161 FGTLDPEALEAVATALELIRtENRMVGVISH 191
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
483-569 |
6.07e-06 |
|
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: 49.63 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 483 LSGGEAQRVAIARAI------VqdapILVLDEATAHADP-ENETAIQKALNALAKGRTTVVIAHRLDTIVHADQILVL-- 553
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHQrDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIgp 564
|
90 100
....*....|....*....|
gi 506241759 554 ----VGGKVVERGVHEELLA 569
Cdd:TIGR00630 565 gageHGGEVVASGTPEEILA 584
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
364-558 |
6.39e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 364 DVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSRVAVVF----QDSML-LRASIAD 438
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLpedrQSSGLyLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 439 NI------RLG---RPGAtdeqvqaaarqaqiHDRVMElpqGYDTVLGSEGSD-------LSGGEAQRVAIARAIVQDAP 502
Cdd:PRK15439 361 NVcalthnRRGfwiKPAR--------------ENAVLE---RYRRALNIKFNHaeqaartLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 503 ILVLDEATAHADPENETAIQKALNALAKGRTTVV-IAHRLDTIVH-ADQILVLVGGKV 558
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
337-551 |
6.50e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 337 PAAE--GPVCMEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMngtelpqma 414
Cdd:PRK11819 315 PPGPrlGDKVIEAENLSKSFGDRL--LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 415 sGEVLsRVAVVFQDsmllRASIADN-------------IRLGRpgatdeqvqaaarqaqihdrvMELP-QGYDTVLGSEG 480
Cdd:PRK11819 384 -GETV-KLAYVDQS----RDALDPNktvweeisggldiIKVGN---------------------REIPsRAYVGRFNFKG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 481 SD-------LSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAkGrTTVVIAH-R--LDTIvhADQI 550
Cdd:PRK11819 437 GDqqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFP-G-CAVVISHdRwfLDRI--ATHI 512
|
.
gi 506241759 551 L 551
Cdd:PRK11819 513 L 513
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
335-540 |
1.00e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.59 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 335 PRPAAEGPVCMEFEGVAFaygENLPFV-------LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWdPVSGSVRMNG 407
Cdd:TIGR00954 437 NLVPGRGIVEYQDNGIKF---ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKP 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 408 TE-----LPQ---MASGEVlsRVAVVFQDSMLlrasiadniRLGRPGATDEQVQAAARQAQIHDrVMELPQGYDTVlgSE 479
Cdd:TIGR00954 513 AKgklfyVPQrpyMTLGTL--RDQIIYPDSSE---------DMKRRGLSDKDLEQILDNVQLTH-ILEREGGWSAV--QD 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 480 GSD-LSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKalNALAKGRTTVVIAHR 540
Cdd:TIGR00954 579 WMDvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYR--LCREFGITLFSVSHR 638
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
362-562 |
1.06e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEV--LSR-VAVVFQD---SMLLRAS 435
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqaLRRdIQFIFQDpyaSLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 436 IADNI----RLGRPGATDEqvqAAARQAQIHDRVMELPQGydtvLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATA 511
Cdd:PRK10261 420 VGDSImeplRVHGLLPGKA---AAARVAWLLERVGLLPEH----AWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 506241759 512 HADPENETAIQKALNALAK--GRTTVVIAHRL---DTIVHadQILVLVGGKVVERG 562
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRdfGIAYLFISHDMavvERISH--RVAVMYLGQIVEIG 546
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
104-296 |
1.11e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 47.50 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 104 IEHLGKIPLGWFND----------NSSAQVKQAATDDVlnlhqsvghapvdVTAALLSPLIP--LVYLFTVDVRFALLLV 171
Cdd:cd18555 82 FEHLLKLPYSFFENrssgdllfraNSNVYIRQILSNQV-------------ISLIIDLLLLViyLIYMLYYSPLLTLIVL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 172 AYFVVVIGVAwpFMMRdfgPLNKRFN----EAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAcyvwTKR 247
Cdd:cd18555 149 LLGLLIVLLL--LLTR---KKIKKLNqeeiVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKA----FKK 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 506241759 248 NGNAFSWVSAlfspgamlvvlLAATLAFVAngvlplercvPFLVLGVGI 296
Cdd:cd18555 220 KERLSNILNS-----------ISSSIQFIA----------PLLILWIGA 247
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
100-281 |
1.42e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis 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 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: 349987 [Multi-domain] Cd Length: 291 Bit Score: 47.09 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 100 RTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSpLIPLVYLFTVDVRFALLLVAYFVVVIG 179
Cdd:cd18543 75 RTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTL-VVGLVVMLVLSPPLALVALASLPPLVL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 180 VAWpFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKACYVWTKRNGNAFSWVSALf 259
Cdd:cd18543 154 VAR-RFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEAL- 231
|
170 180
....*....|....*....|..
gi 506241759 260 sPGAMLVVLLAATLAFVANGVL 281
Cdd:cd18543 232 -PELGLAAVLALGGWLVANGSL 252
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
362-514 |
1.53e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIprfwdpvSGSVRMNGTEL---------------PQMASGEVLSRVAV-V 425
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIiyeqdlivarlqqdpPRNVEGTVYDFVAEgI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSMLLRA--SIADNI----------RLGRPGATDEQVQAAARQAQIHDRVMELPQGYDTVLgsegSDLSGGEAQRVAI 493
Cdd:PRK11147 92 EEQAEYLKRyhDISHLVetdpseknlnELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAAL----SSLSGGWLRKAAL 167
|
170 180
....*....|....*....|.
gi 506241759 494 ARAIVQDAPILVLDEATAHAD 514
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLD 188
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
483-574 |
1.60e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 483 LSGGEAQRVAIARAIVQDA---PILVLDEATA--H-ADpenetaIQKALNAL----AKGRTTVVIAHRLDTIVHADQILV 552
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTglHfED------IRKLLEVLhrlvDKGNTVVVIEHNLDVIKTADWIID 904
|
90 100
....*....|....*....|....*...
gi 506241759 553 L------VGGKVVERGVHEELLAADGHY 574
Cdd:PRK00349 905 LgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
346-508 |
1.64e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.34 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFvlQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNgtelpqmasGEVLSRVAVV 425
Cdd:PRK13538 3 EARNLACERDERILF--SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ---------GEPIRRQRDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 426 FQDSML-----------------LRAsiadNIRLGRPgATDEQVQAAARQAQIHDRvMELPQGYdtvlgsegsdLSGGEA 488
Cdd:PRK13538 72 YHQDLLylghqpgikteltalenLRF----YQRLHGP-GDDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQ 135
|
170 180
....*....|....*....|
gi 506241759 489 QRVAIARAIVQDAPILVLDE 508
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDE 155
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
351-539 |
1.71e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 351 AFAYGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNG---TELPQMASGEVLSRVAVVFQ 427
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktaTRGDRSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 428 DSMLLRASIADNIRLGRpgatdeqvqaaarqaqihdRVMELPQGYDTVLGSEGSD------LSGGEAQRVAIARAIVQDA 501
Cdd:PRK13543 96 DLSTLENLHFLCGLHGR-------------------RAKQMPGSALAIVGLAGYEdtlvrqLSAGQKKRLALARLWLSPA 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 506241759 502 PILVLDEATAHADPENETAIQKALNA-LAKGRTTVVIAH 539
Cdd:PRK13543 157 PLWLLDEPYANLDLEGITLVNRMISAhLRGGGAALVTTH 195
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
354-551 |
2.14e-05 |
|
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: 45.04 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 354 YGENLPFVLQDVDVALEPGTVTALVGDSGSGKTTLARLIprfwdpvsgsvrmngtelpqmasgevlsrVAVVFQDSMLLR 433
Cdd:cd03227 3 VLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAI-----------------------------GLALGGAQSATR 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 434 ASIADNIRLGRPgatdeqvqaaarqAQIHDRVMELPQgydtvlgsegsdLSGGEAQRVAIARAI----VQDAPILVLDEA 509
Cdd:cd03227 54 RRSGVKAGCIVA-------------AVSAELIFTRLQ------------LSGGEKELSALALILalasLKPRPLYILDEI 108
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 506241759 510 TAHADPENETAIQKALNALAKGRTTV-VIAHRLDTIVHADQIL 551
Cdd:cd03227 109 DRGLDPRDGQALAEAILEHLVKGAQViVITHLPELAELADKLI 151
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
100-310 |
2.94e-05 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. 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. 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: 349993 [Multi-domain] Cd Length: 295 Bit Score: 46.29 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 100 RTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVVIG 179
Cdd:cd18549 78 RRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMII 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 180 VAWPF---MMRDFgplnKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKAcyvwtKRNGN----AF 252
Cdd:cd18549 158 FTIYFnkkMKKAF----RRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLES-----KKKAYkamaYF 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 506241759 253 SWVSALFSpGAMLVVLLAATLAFVANGVLPLERCVPFLVlgvgipagLVNLFRS-IRML 310
Cdd:cd18549 229 FSGMNFFT-NLLNLVVLVAGGYFIIKGEITLGDLVAFLL--------YVNVFIKpIRRL 278
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
307-539 |
4.47e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 307 IRMLQ-MSLQAADHLASVLNVAPLAEPERPRPaaegpvCMEFEGVAFAYGENLpfVLQDVDVALEPGTVTALVGDSGSGK 385
Cdd:PRK10636 280 IKMLErMELIAPAHVDNPFHFSFRAPESLPNP------LLKMEKVSAGYGDRI--ILDSIKLNLVPGSRIGLLGRNGAGK 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 386 TTLARLIPRFWDPVSGSVrmngtelpQMASGEVLSRVAvvfQDSM-LLRASIADNIRLGR--PGATDEQVQAAARQAQIH 462
Cdd:PRK10636 352 STLIKLLAGELAPVSGEI--------GLAKGIKLGYFA---QHQLeFLRADESPLQHLARlaPQELEQKLRDYLGGFGFQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 463 -DRVMELPQGYdtvlgsegsdlSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKAL----NALakgrttVVI 537
Cdd:PRK10636 421 gDKVTEETRRF-----------SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALidfeGAL------VVV 483
|
..
gi 506241759 538 AH 539
Cdd:PRK10636 484 SH 485
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
483-564 |
6.92e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.99 E-value: 6.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 483 LSGGEAQRVAIAR--AI--VQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQilvLVGGKV 558
Cdd:cd03278 114 LSGGEKALTALALlfAIfrVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADR---LYGVTM 190
|
....*.
gi 506241759 559 VERGVH 564
Cdd:cd03278 191 QESGVS 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
346-572 |
8.69e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 346 EFEGVAFAYGENLPFvlQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMngTE------LPQMASGEvl 419
Cdd:PRK15064 321 EVENLTKGFDNGPLF--KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW--SEnanigyYAQDHAYD-- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 420 srvavvFQDSMllraSIADNIRLGRPGATDEqvqaaarqaqihdrvmelpQGYDTVLGSE--GSD--------LSGGEAQ 489
Cdd:PRK15064 395 ------FENDL----TLFDWMSQWRQEGDDE-------------------QAVRGTLGRLlfSQDdikksvkvLSGGEKG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 490 RVAIARAIVQDAPILVLDEATAHADPEnetAIQkALN-ALAKGRTTVV-IAH-RLDTIVHADQILVLVGGKVVE-RGVHE 565
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDME---SIE-SLNmALEKYEGTLIfVSHdREFVSSLATRIIEITPDGVVDfSGTYE 521
|
....*..
gi 506241759 566 ELLAADG 572
Cdd:PRK15064 522 EYLRSQG 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
481-516 |
1.79e-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: 44.54 E-value: 1.79e-04
10 20 30
....*....|....*....|....*....|....*.
gi 506241759 481 SDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPE 516
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE 195
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
111-275 |
1.90e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 43.62 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 111 PLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVVIGVAWpFMMRDFG 190
Cdd:cd18577 94 DIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGG-IMGKLLS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 191 PLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEElakacyvwTKRNGNAFSWVSALFSPGAMLVVLLA 270
Cdd:cd18577 173 KYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEK--------ARKAGIKKGLVSGLGLGLLFFIIFAM 244
|
....*
gi 506241759 271 ATLAF 275
Cdd:cd18577 245 YALAF 249
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
483-574 |
1.92e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 483 LSGGEAQRVAIARAI------VqdapILVLDEATA--HA-DpenetaIQKALNALAK----GRTTVVIAHRLDTIVHADQ 549
Cdd:COG0178 486 LSGGEAQRIRLATQIgsglvgV----LYVLDEPSIglHQrD------NDRLIETLKRlrdlGNTVIVVEHDEDTIRAADY 555
|
90 100 110
....*....|....*....|....*....|....*.
gi 506241759 550 IL-------VLvGGKVVERGVHEELLAAD----GHY 574
Cdd:COG0178 556 IIdigpgagEH-GGEVVAQGTPEEILKNPdsltGQY 590
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
483-567 |
2.52e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.05 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 483 LSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALA-KGRTTVVIAHRLDTIVH-ADQILVLVGGKVVE 560
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKG 483
|
....*..
gi 506241759 561 RGVHEEL 567
Cdd:TIGR02633 484 DFVNHAL 490
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
366-586 |
3.64e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 366 DVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGS--------VRMNGTELPQMASGEvlsrvavvFQD--SMLLRAS 435
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDE--------WQRnnTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 436 IADNIRLGRPGATDEqvqaaarqaqIHD--RVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARAIVQDAPILVLDEATA 511
Cdd:PRK10938 95 EDDTGRTTAEIIQDE----------VKDpaRCEQLAQqfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 506241759 512 HADPENETAIQKALNALA-KGRTTVVIAHRLDTI-VHADQILVLVGGKVVERGVHEELLaADGHYAALWRSQQVDAL 586
Cdd:PRK10938 165 GLDVASRQQLAELLASLHqSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEIL-QQALVAQLAHSEQLEGV 240
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
156-282 |
5.23e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 42.55 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 156 LVYLFTVDVRFALLLVAYFVVVIGVAWpFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATE 235
Cdd:cd18557 128 LIILFILSWKLTLVLLLVIPLLLIASK-IYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALD 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 506241759 236 E---LAKACYVWtkrngNA-FSWVSALFSPGAMLVVL-LAATLafVANGVLP 282
Cdd:cd18557 207 RsyrLARKKALA-----NAlFQGITSLLIYLSLLLVLwYGGYL--VLSGQLT 251
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
28-240 |
6.72e-04 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 42.01 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 28 VAIAALSSACEFVPYLAIARVAQLSITEGVPPSDVLAMWVLVAVAGAAagRMLFSMATGR-CHYADADFRVHVRTVLIEH 106
Cdd:cd18584 2 VLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLL--RALLAWAQERlAARAAARVKAELRRRLLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 107 LGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFAL-LLVAY-----FVVVIGV 180
Cdd:cd18584 80 LLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALiLLVTApliplFMILIGK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 181 AwpfmMRDfgpLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKA 240
Cdd:cd18584 160 A----AQA---ASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRR 212
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
344-508 |
7.41e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 42.14 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 344 CMEFEGVAFAYGENLPfVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMasgEVLSR-V 422
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL---EPADRdI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 423 AVVFQDSMLL-RASIADNIRLG---RPGATDEqvqaaarqaqIHDRVMELPQ--GYDTVLGSEGSDLSGGEAQRVAIARA 496
Cdd:PRK11650 79 AMVFQNYALYpHMSVRENMAYGlkiRGMPKAE----------IEERVAEAARilELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170
....*....|..
gi 506241759 497 IVQDAPILVLDE 508
Cdd:PRK11650 149 IVREPAVFLFDE 160
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
483-558 |
1.01e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506241759 483 LSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNALAK-GRTTVVIAHRLDTIVH-ADQILVLVGGKV 558
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
100-240 |
1.03e-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: 41.62 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 100 RTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVVIG 179
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506241759 180 VAWpFMMRDFGPLNKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYRAATEELAKA 240
Cdd:cd18547 161 VTK-FIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKA 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
362-558 |
1.31e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 362 LQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNGTELPQMASGEVLSR-VAVVFQD-------SMLLR 433
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgFALVTEErrstgiyAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 434 A--SIADNIR--LGRPGATDEQVQAAARQAQIHDRVMELPqGYDTVLGSegsdLSGGEAQRVAIARAIVQDAPILVLDEA 509
Cdd:PRK10982 344 GfnSLISNIRnyKNKVGLLDNSRMKSDTQWVIDSMRVKTP-GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 506241759 510 TAHADPENETAIQKALNALA-KGRTTVVIAHRLDTIVH-ADQILVLVGGKV 558
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
360-407 |
1.62e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 1.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 506241759 360 FVLQDVDVALEPGTVTALVGDSGSGKTTLARLIPRFWDPVSGSVRMNG 407
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
331-570 |
1.69e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 331 EPERPRPA-AEGPVCMEFEGVAFAYGENLPFVLQDvdvalepGTVTALVGDSGSGKTTLARLI----PRfwdpVSGSVRM 405
Cdd:PRK10762 243 EDQYPRLDkAPGEVRLKVDNLSGPGVNDVSFTLRK-------GEILGVSGLMGAGRTELMKVLygalPR----TSGYVTL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 406 NGTEL----PQ--MASGevlsrvaVVF------QDSMLLRASIADNIRL----------GRPGATDEQVQAAARQAQ--I 461
Cdd:PRK10762 312 DGHEVvtrsPQdgLANG-------IVYisedrkRDGLVLGMSVKENMSLtalryfsragGSLKHADEQQAVSDFIRLfnI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 462 HDRVMELPQGydtvlgsegsDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPENETAIQKALNAL-AKGRTTVVIAHR 540
Cdd:PRK10762 385 KTPSMEQAIG----------LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkAEGLSIILVSSE 454
|
250 260 270
....*....|....*....|....*....|....*.
gi 506241759 541 LDTIV-HADQILVLVGGKV-----VERGVHEELLAA 570
Cdd:PRK10762 455 MPEVLgMSDRILVMHEGRIsgeftREQATQEKLMAA 490
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
481-516 |
1.92e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....*.
gi 506241759 481 SDLSGGEAQRVAIARAIVQDAPILVLDEATAHADPE 516
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
100-317 |
2.07e-03 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV 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 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: 349989 [Multi-domain] Cd Length: 293 Bit Score: 40.53 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 100 RTVLIEHLGKIPLGWFNDNSSAQVKQAATDDVLNLHQSVGHAPVDVTAALLSPLIPLVYLFTVDVRFALLLVAYFVVVIG 179
Cdd:cd18545 76 RQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 180 VAW---PFMMRDFgplnKRFNEAMVEVSSAAVEMVEGIAVIKTFGSRSRAGARYraatEELAKACYvwtkrngNAF---S 253
Cdd:cd18545 156 VVFllrRRARKAW----QRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIF----DELNRENR-------KANmraV 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 506241759 254 WVSALFSPGAMLVVLLAATLAFVANGvlplercvpFLVLGVGIPAGLV--------NLFRSIRMLQM---SLQAA 317
Cdd:cd18545 221 RLNALFWPLVELISALGTALVYWYGG---------KLVLGGAITVGVLvafigyvgRFWQPIRNLSNfynQLQSA 286
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
461-575 |
2.09e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 461 IHDRVMEL-PQGYDTV-LGSEGSDLSGGEAQRVAIARAIVQDAP---ILVLDEATAHADPENETAIQKALNALA-KGRTT 534
Cdd:PRK00635 786 IHEKIHALcSLGLDYLpLGRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTV 865
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 506241759 535 VVIAHRLDTIVHADQILVL------VGGKVVERGVHEELLAADGHYA 575
Cdd:PRK00635 866 VIIEHNMHVVKVADYVLELgpeggnLGGYLLASCSPEELIHLHTPTA 912
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
363-560 |
2.69e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.54 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 363 QDVDVALEPGTVTALVGDSGSGKTTLARLI----PRfwdpVSGSVRMNGTEL-PQMASGEVLSRVAVVFQD--------- 428
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLfgvdKR----AGGEIRLNGKDIsPRSPLDAVKKGMAYITESrrdngffpn 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 429 -SMLLRASIADNIRLGRPGAT-------DEQVQAAARQAQIHDRVMELPQGYdtvlgsegSDLSGGEAQRVAIARAIVQD 500
Cdd:PRK09700 356 fSIAQNMAISRSLKDGGYKGAmglfhevDEQRTAENQRELLALKCHSVNQNI--------TELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 506241759 501 APILVLDEATAHADPENETAIQKALNALA-KGRTTVVIAHRLDTIVHA-DQILVLVGGKVVE 560
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
374-539 |
5.63e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.45 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 374 VTALVGDSGSGKTTLARLIpRF--WDPVSGSVRMNGTelpQMASGEVLSRVAVVFQD--------------SMLLRAS-- 435
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAI-RYalYGKARSRSKLRSD---LINVGSEEASVELEFEHggkryrierrqgefAEFLEAKps 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 436 -----------------IADNIRLGRPGATDEQVQAAARQAQIHDRVMELpQGYDTVlgsegSDLSGGEAQRVAIARAIV 498
Cdd:COG0419 101 erkealkrllgleiyeeLKERLKELEEALESALEELAELQKLKQEILAQL-SGLDPI-----ETLSGGERLRLALADLLS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 506241759 499 qdapiLVLDeaTAHADPENETAIQKALNALAkgrttvVIAH 539
Cdd:COG0419 175 -----LILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
483-563 |
6.02e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506241759 483 LSGGEAQRVAIAR--AI--VQDAPILVLDEATAHADPENETAIQKALNALAKGRTTVVIAHRLDTIVHADQilvLVGGKV 558
Cdd:TIGR02168 1090 LSGGEKALTALALlfAIfkVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQ---LYGVTM 1166
|
....*
gi 506241759 559 VERGV 563
Cdd:TIGR02168 1167 QEKGV 1171
|
|
| TsaE |
pfam02367 |
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ... |
368-390 |
7.95e-03 |
|
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).
Pssm-ID: 460540 Cd Length: 127 Bit Score: 37.03 E-value: 7.95e-03
|
| |
