|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1-547 |
0e+00 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 1019.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 1 MELLLLVWRQYRWPFISVIALSLLSAALGIGLIAFINLRLMTVVDTSLAVLPEFLGLLLLLMVVTLGSQLALTTLGHHFV 80
Cdd:PRK10522 1 MELLRLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 81 FRLRGEFIKRILDTQIEKVEKIGSASLLAGLTSDIRNITIAFVRLPELVQGIILTFGSAAYLAWLSGKMMMVTALWMALT 160
Cdd:PRK10522 81 YRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITIAFVRLPELVQGIILTLGSAAYLAWLSPKMLLVTAIWMAVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 161 IWGGFVLVARVYRHMATLRETEDKLYHDYQTVLEGRKELTLNRERAEYVFNQLYLPDAREYRHHIIRADTFHLSAVNWSN 240
Cdd:PRK10522 161 IWGGFVLVARVYKHMATLRETEDKLYNDYQTVLEGRKELTLNRERAEYVFENEYEPDAQEYRHHIIRADTFHLSAVNWSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 241 IMMLGAIGLVFWMANSLGWANTAVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNTFSLAPYRADFPQPEPHPHW 320
Cdd:PRK10522 241 IMMLGAIGLVFYMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKLALAPYKAEFPRPQAFPDW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 321 QTLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFS 400
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFTDVWLFDRLLGPGGKAADSALVDQWMAYLKMTHKLQLDNGRIVDLKLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 481 DPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTELTGEERELATRDAVARTA 547
Cdd:PRK10522 481 DPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAVARTA 547
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-538 |
0e+00 |
|
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: 725.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 1 MELLLLVWRQYRWPFISVIALSLLSAALGIGLIAFINLRLMTVVDTSLAVLPEFLGLLLLLMVVTLGSQLALTTLGHHFV 80
Cdd:COG4615 1 MNLLRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 81 FRLRGEFIKRILDTQIEKVEKIGSASLLAGLTSDIRNITIAFVRLPELVQGIILTFGSAAYLAWLSGKMMMVTALWMALT 160
Cdd:COG4615 81 ARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 161 IWGGFVLVARVYRHMATLRETEDKLYHDYQTVLEGRKELTLNRERAEYVFNQLYLPDAREYRHHIIRADTFHLSAVNWSN 240
Cdd:COG4615 161 VAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAFFDEDLQPTAERYRDLRIRADTIFALANNWGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 241 IMMLGAIGLVFWMANSLGWANTAVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNTFSLAPYRA-----DFPQPE 315
Cdd:COG4615 241 LLFFALIGLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAepaaaDAAAPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 316 PHPHWQTLELRDVCFHYP----DNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADK 391
Cdd:COG4615 321 APADFQTLELRGVTYRYPgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 392 PEDYRKLFSAVFTDVWLFDRLLGPGGkAADSALVDQWMAYLKMTHKLQLDNGRIVDLKLSKGQKKRVALLLALAEERDII 471
Cdd:COG4615 401 REAYRQLFSAVFSDFHLFDRLLGLDG-EADPARARELLERLELDHKVSVEDGRFSTTDLSQGQRKRLALLVALLEDRPIL 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 472 LLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTELTGEERELA 538
Cdd:COG4615 480 VFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAA 546
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
2-527 |
7.64e-103 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 320.37 E-value: 7.64e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 2 ELLLLVWRQYRWPFISVIALSLLSAALGIGLIAFINLRLMTVVDTSLAVLPEFLGLLLLLMVVTLGSQLALTTLGHHFVF 81
Cdd:TIGR01194 7 EILALLRSPFPAITAFSIALGLAGGLAIIALLASINNAIHEENFLGQGSLFSFGGLCLLALLFRIGADIFPAYAGMHIIA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 82 RLRGEFIKRILDTQIEKVEKIGSASLLAGLTSDIRNITIAFVRLPELVQGIILTFGSAAYLAWLSGKMMMVTALWMALTI 161
Cdd:TIGR01194 87 NLRIALCEKILGAPIEEIDRRGAHNLIPLLTHDIDQINAFLFIFPPIAIALAIFFFCIAYLAYLSVPMFAITISAIIIGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 162 WGGFVLVARVYRHMATLRETEDKLYHDYQTVLEGRKELTLNR-ERAEYVFNQLYLPDAREYRHHIIRADTFHLsAVNWSN 240
Cdd:TIGR01194 167 AAQLLAFMGGFKFFHAARDEEDAFNEHTHAIAFGAKELKIHGiRRLSFAHGAIQESANNIADLHIIEILIFIA-AENFGQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 241 IMMLGAIGLVFWMANSLGWANTAVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNTFSLApyradFPQPEPHPH- 319
Cdd:TIGR01194 246 LLFFLLIGCALFAAAMFASIDAAAISAFVLALLYIKGPLEMLVSALPILAQAQIACQRLADFGER-----FNEPEPELEl 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 320 --------------WQTLELRDVCFHYPD----NSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQIL 381
Cdd:TIGR01194 321 sdadnvlllahdksVDSIELKDVHMNPKApegsEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 382 LDGQPLAADKPEDYRKLFSAVFTDVWLFDRLLGPG-GKAADSALVDQWMAYLKMTHKLQL-DNGRIVDLKLSKGQKKRVA 459
Cdd:TIGR01194 401 LDGAAVSADSRDDYRDLFSAIFADFHLFDDLIGPDeGEHASLDNAQQYLQRLEIADKVKIeDGGFSTTTALSTGQQKRLA 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491003152 460 LLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQL 527
Cdd:TIGR01194 481 LICAWLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDDQYFELADQIIKLAAGCI 548
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-529 |
2.72e-52 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 187.29 E-value: 2.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 4 LLLVWRQYRWPFISVIALSLLSAALGIGLIAFINL---RLMTVVDTS----LAVLpeFLGLLLLLMVVTLGSQLALTTLG 76
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRiidALLAGGDLSalllLLLL--LLGLALLRALLSYLQRYLLARLA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 77 HHFVFRLRGEFIKRILDTQIEKVEKIGSASLLAGLTSDIRNITIAFVR-LPELVQGIILTFGSAAYLAWLSGKMMMVTAL 155
Cdd:COG1132 90 QRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLFVIDWRLALIVLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 156 WMALTIWGGFVLVARVYRHMATLRETEDKLYHDYQTVLEGRKEL-TLNRERAEY-VFNQLylpdAREYRHHIIRAdtFHL 233
Cdd:COG1132 170 VLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVkAFGREERELeRFREA----NEELRRANLRA--ARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 234 SAVNWSNIMMLGAIGLVF------WMANSlGWANTAVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNTF-SLAP 306
Cdd:COG1132 244 SALFFPLMELLGNLGLALvllvggLLVLS-GSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELlDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 307 YRADFPQPEPHPHWQ-TLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQ 385
Cdd:COG1132 323 EIPDPPGAVPLPPVRgEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 386 PLAADKPEDYRKLFSAVFTDVWLFDR------LLGPGG-------KAADSALVDQWMAylkmthklQLDNG---RIVD-- 447
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGtireniRYGRPDatdeeveEAAKAAQAHEFIE--------ALPDGydtVVGErg 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 448 LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPhfRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQL 527
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDT--ETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
..
gi 491003152 528 TE 529
Cdd:COG1132 553 VE 554
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
323-526 |
4.52e-45 |
|
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: 156.39 E-value: 4.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS-FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFDRLLgpggkaadsalvdqwmaylkmthklqLDNgrIvdlkLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:cd03228 81 VPQDPFLFSGTI--------------------------REN--I----LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491003152 482 PHFRREFYqqLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQ 526
Cdd:cd03228 129 PETEALIL--EALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
323-527 |
1.26e-38 |
|
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: 141.32 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRK----- 397
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 -------LFSA-VFTDVwlfdrLLGP-----GGKAADsALVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLAL 464
Cdd:COG1122 81 fqnpddqLFAPtVEEDV-----AFGPenlglPREEIR-ERVEEALELVGLEHLAD----RPPH-ELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 465 AEERDIILLDEWAADQDPHFRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDlDLVAELADRVIVLDDGRI 212
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-542 |
1.67e-38 |
|
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: 148.76 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 4 LLLVWRQYRWPFISVIALSLLSAALGIGLIA----FInlrlmtvvdTSLAVLPEFlglllllmvvtlgsqLALTT----- 74
Cdd:COG4987 6 LLRLLRPHRGRLLLGVLLGLLTLLAGIGLLAlsgwLI---------AAAALAPPI---------------LNLFVpivgv 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 75 ----------------LGHHFVFR----LRGEFIKRILDTQIEKVEKIGSASLLAGLTSDIRNITIAFVRL--PELVqGI 132
Cdd:COG4987 62 rafaigrtvfrylerlVSHDATLRlladLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVllPLLV-AL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 133 ILTFGSAAYLAWLSGKMMMVTALWMALTIWGGFVLVARVYRHM-ATLRETEDKLYHDYQTVLEGRKELTLN------RER 205
Cdd:COG4987 141 LVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAgRRLAAARAALRARLTDLLQGAAELAAYgaldraLAR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 206 AEYVFNQLylpDAREYRHHIIRADTfhlSAVNWsnIMMLGAIGLVFWMAnSLGWANTAVAATYSLTLLFLRTPLLSAVGA 285
Cdd:COG4987 221 LDAAEARL---AAAQRRLARLSALA---QALLQ--LAAGLAVVAVLWLA-APLVAAGALSGPLLALLVLAALALFEALAP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 286 LPT----LLSAQVAFNKLNTFSLAPYRADFP-QPEPHPHWQTLELRDVCFHYPDNSFAV-GPINLTLQRGELVFLIGGNG 359
Cdd:COG4987 292 LPAaaqhLGRVRAAARRLNELLDAPPAVTEPaEPAPAPGGPSLELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGPSG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 360 SGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVFTDVWLFD-------RLLGPGgkAADSALV------- 425
Cdd:COG4987 372 SGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDttlrenlRLARPD--ATDEELWaalervg 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 426 -DQWMAYLKmtHKLQL---DNGRivdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQqmGK 501
Cdd:COG4987 450 lGDWLAALP--DGLDTwlgEGGR----RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GR 521
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 491003152 502 TVFAISHDDHYFQHADRLLEMRSGQLTElTGEERELATRDA 542
Cdd:COG4987 522 TVLLITHRLAGLERMDRILVLEDGRIVE-QGTHEELLAQNG 561
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-529 |
1.88e-38 |
|
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: 149.98 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 9 RQYRWPFISVIALSLLSAALGIGLIAFInlrlMTVVDTslaVLP----EFLGLLLLLMVVTLGSQLALTTLGHHFV---- 80
Cdd:COG2274 152 RRYRRLLLQVLLASLLINLLALATPLFT----QVVIDR---VLPnqdlSTLWVLAIGLLLALLFEGLLRLLRSYLLlrlg 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 81 ----FRLRGEFIKRILDTQIEKVEKIGSASLLAGLtSDIRNITIAFV-RLPELVQGIILTFGSAAYLAWLSGKMMMVTAL 155
Cdd:COG2274 225 qridLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgSLLTALLDLLFVLIFLIVLFFYSPPLALVVLL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 156 WMALTIWGGFVLVARVYRHMATLRETEDKLYHDYQTVLEGRKEL-TLNRE-RAEYVFNQLYlpdaREYRHHIIRADTFHL 233
Cdd:COG2274 304 LIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIkALGAEsRFRRRWENLL----AKYLNARFKLRRLSN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 234 SAVNWSN-IMMLGAIGLVFWMAN-------SLGwantAVAATYSLTLLFLrTPLLSAVGALPTLLSAQVAFNKLNT-FSL 304
Cdd:COG2274 380 LLSTLSGlLQQLATVALLWLGAYlvidgqlTLG----QLIAFNILSGRFL-APVAQLIGLLQRFQDAKIALERLDDiLDL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 305 APYRADFPQPEPHPHWQ-TLELRDVCFHYPDNSFAV-GPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILL 382
Cdd:COG2274 455 PPEREEGRSKLSLPRLKgDIELENVSFRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 383 DGQPLAADKPEDYRKLFSAVFTDVWLF-----------------DRLLgpggKAADSALVDQWMAYLKMTHKLQL-DNGR 444
Cdd:COG2274 535 DGIDLRQIDPASLRRQIGVVLQDVFLFsgtirenitlgdpdatdEEII----EAARLAGLHDFIEALPMGYDTVVgEGGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 445 ivdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQqmGKTVFAISHDDHYFQHADRLLEMRS 524
Cdd:COG2274 611 ----NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDK 684
|
....*
gi 491003152 525 GQLTE 529
Cdd:COG2274 685 GRIVE 689
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
324-526 |
9.20e-36 |
|
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: 132.59 E-value: 9.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYPD-NSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAV 402
Cdd:cd03225 1 ELKNLSFSYPDgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 F--TDVWLF------DRLLGPG----GKAADSALVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLALAEERDI 470
Cdd:cd03225 81 FqnPDDQFFgptveeEVAFGLEnlglPEEEIEERVEEALELVGLEGLRD----RSPF-TLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 471 ILLDEWAADQDPHFRREFyQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQ 526
Cdd:cd03225 156 LLLDEPTAGLDPAGRREL-LELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
341-478 |
1.22e-33 |
|
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: 125.07 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 341 PINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVFTDVWLFDRL-----LGP 415
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenLRL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491003152 416 GG------KAADSALVDQWMAYLKMTHKlqldNGRIVDLK---LSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:pfam00005 83 GLllkglsKREKDARAEEALEKLGLGDL----ADRPVGERpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
323-527 |
1.45e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 126.85 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFaVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAV 402
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTD-VWL-------FDRLLGPGGKAADSALVDQWMAYLKMTHKLqLDngRIVDlKLSKGQKKRVALLLALAEERDIILLD 474
Cdd:COG4619 80 PQEpALWggtvrdnLPFPFQLRERKFDRERALELLERLGLPPDI-LD--KPVE-RLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491003152 475 EWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLEMRSGQL 527
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
324-528 |
1.89e-32 |
|
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: 122.54 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYPDNsFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFsavf 403
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 404 tdvwlfdrllgpggkaadsALVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:cd03214 76 -------------------AYVPQALELLGLAHLAD----RPFN-ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491003152 484 FRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLT 528
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDlNLAARYADRVILLKDGRIV 177
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
324-526 |
1.12e-31 |
|
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: 119.66 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYPDNsFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVF 403
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 404 tdvwlfdrllgpggkaadsalvdQwmaylkmthklqldngrivdlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:cd00267 80 -----------------------Q----------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491003152 484 FRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGQ 526
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDpELAELAADRVIVLKDGK 157
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
322-541 |
2.99e-31 |
|
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: 127.57 E-value: 2.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 322 TLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFD-------RLLGPGG------KAADSALVDQWMAYLKmtHKLQ---LDNGRivdlKLSKGQKKRVALLLALA 465
Cdd:COG4988 416 VPQNPYLFAgtirenlRLGRPDAsdeeleAALEAAGLDEFVAALP--DGLDtplGEGGR----GLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 466 EERDIILLDEWAADQDPHfrREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEERELATRD 541
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAE--TEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVE-QGTHEELLAKN 562
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
323-527 |
4.44e-31 |
|
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: 118.65 E-value: 4.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNsFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLaADKPEDYRKLFSAV 402
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRLLGpggkaadsalvdqwmaylkmthklqLDNgrivdLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:cd03230 79 PEEPSLYENLTV-------------------------REN-----LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491003152 483 HFRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:cd03230 129 ESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
323-546 |
3.06e-30 |
|
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: 118.61 E-value: 3.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNsFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAV 402
Cdd:COG1120 2 LEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 ---------FT--DVWLFDRL--LGPGGK--AADSALVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLALAEE 467
Cdd:COG1120 81 pqeppapfgLTvrELVALGRYphLGLFGRpsAEDREAVEEALERTGLEHLAD----RPVD-ELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 468 RDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTElTGEERELATRDAVART 546
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDlNLAARYADRLVLLKDGRIVA-QGPPEEVLTPELLEEV 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
323-527 |
6.69e-28 |
|
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: 111.04 E-value: 6.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS---FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED----Y 395
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 396 RKLFSAVFTDVWLFDRL-----------LGPGGKAADSALVDQWMAYLKMTHKLqldnGRIVDlKLSKGQKKRVALLLAL 464
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLtalenvelpllLAGVPKKERRERAEELLERVGLGDRL----NHYPS-ELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 465 AEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQL 527
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
323-527 |
7.68e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 111.69 E-value: 7.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNsFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADkPEDYRKLFSAV 402
Cdd:COG1131 1 IEVRGLTKRYGDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD-PAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRL-----------LGPGGKAADSALVDQWMAYLKMTHKLqldnGRIVDlKLSKGQKKRVALLLALAEERDII 471
Cdd:COG1131 79 PQEPALYPDLtvrenlrffarLYGLPRKEARERIDELLELFGLTDAA----DRKVG-TLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 472 LLDEWAADQDPHFRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYlEEAERLCDRVAIIDKGRI 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
323-527 |
8.32e-28 |
|
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: 111.14 E-value: 8.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:cd03245 3 IEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLF-----------------DRLLgpggKAADSALVDQWMAYLKMTHKLQL-DNGRivdlKLSKGQKKRVALLLA 463
Cdd:cd03245 83 VPQDVTLFygtlrdnitlgapladdERIL----RAAELAGVTDFVNKHPNGLDLQIgERGR----GLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 464 LAEERDIILLDEWAADQDphFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQL 527
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD--MNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
323-526 |
9.19e-28 |
|
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: 109.58 E-value: 9.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNsFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAA--DKPEDYRKLFS 400
Cdd:cd03229 1 LELKNVSKRYGQK-TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFTDVWLFdrllgpggkaadsalvdqwmaylkmTHKLQLDNgriVDLKLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:cd03229 80 MVFQDFALF-------------------------PHLTVLEN---IALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491003152 481 DPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLEMRSGQ 526
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
323-527 |
4.23e-27 |
|
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: 108.76 E-value: 4.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNsFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEdyRKLFSAV 402
Cdd:cd03259 1 LELKGLSKTYGSV-RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRL---------LGPGGKAADsALVDQWMAYLKMTHkLQLDNGRIVDlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:cd03259 78 FQDYALFPHLtvaeniafgLKLRGVPKA-EIRARVRELLELVG-LEGLLNRYPH-ELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 474 DEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDqEEALALADRIAVMNEGRI 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
323-529 |
9.97e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 109.72 E-value: 9.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS-FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:PRK13635 6 IRVEHISFRYPDAAtYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDvwlfdrllgP-----GGKAADS---ALVDQWMAYLKMTHKLQ--LDNGRIVDL------KLSKGQKKRVALLLALA 465
Cdd:PRK13635 86 VFQN---------PdnqfvGATVQDDvafGLENIGVPREEMVERVDqaLRQVGMEDFlnrephRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 466 EERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTE 529
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
324-528 |
1.16e-26 |
|
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: 107.34 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADK--------PED- 394
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErrksigyvMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 395 YRKLFSA-VFTDVWLFDRLLGPGGKAADSALVDQWMAYLKMTHKLQLdngrivdlklSKGQKKRVALLLALAEERDIILL 473
Cdd:cd03226 81 DYQLFTDsVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSL----------SGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 474 DEWAADQDPHFRREFyQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLT 528
Cdd:cd03226 151 DEPTSGLDYKNMERV-GELIRELAAQGKAVIVITHDyEFLAKVCDRVLLLANGAIV 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
323-546 |
3.84e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.10 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYpDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKP--------ED 394
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrigyvpqrAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 395 YRKLFSA-VFtDV----WLFDRLLGPGGKAADSALVDQWMAYLKMTHKLqldnGRIVDlKLSKGQKKRVALLLALAEERD 469
Cdd:COG1121 86 VDWDFPItVR-DVvlmgRYGRRGLFRRPSRADREAVDEALERVGLEDLA----DRPIG-ELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491003152 470 IILLDEWAADQDPHFRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGQLTEltGEERELATRDAVART 546
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDlGAVREYFDRVLLLNRGLVAH--GPPEEVLTPENLSRA 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
323-542 |
7.07e-26 |
|
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: 106.23 E-value: 7.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAV 402
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFdrllgPGGKAADS-ALVDQWMAYLKMTHKLQLDNG-RIVDL-----------KLSKGQKKRVALLLALAEERD 469
Cdd:cd03295 81 IQQIGLF-----PHMTVEENiALVPKLLKWPKEKIRERADELlALVGLdpaefadryphELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 470 IILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTELtGEERELATRDA 542
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEIVQV-GTPDEILRSPA 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
324-537 |
8.56e-26 |
|
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: 105.39 E-value: 8.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVF 403
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 404 TDVWLFDR------LLGpggkaADSALVDQWMAYLKMTHKLQ----LDNGRIVDLK-----LSKGQKKRVALLLALAEER 468
Cdd:cd03254 84 QDTFLFSGtimeniRLG-----RPNATDEEVIEAAKEAGAHDfimkLPNGYDTVLGenggnLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 469 DIILLDEWAADQDPHfrREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEEREL 537
Cdd:cd03254 159 KILILDEATSNIDTE--TEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIE-EGTHDEL 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
323-547 |
1.43e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.47 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPL--AADKPEDYRKLFS 400
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFT--DVWLFdrllgpggkaadSALVDQWMAYLKMTHKLQLDNGR-----------IVDLK------LSKGQKKRVALL 461
Cdd:PRK13636 86 MVFQdpDNQLF------------SASVYQDVSFGAVNLKLPEDEVRkrvdnalkrtgIEHLKdkpthcLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 462 LALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTeLTGEERELATR 540
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAE 232
|
....*..
gi 491003152 541 DAVARTA 547
Cdd:PRK13636 233 KEMLRKV 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
323-529 |
1.83e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 104.36 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS---FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL- 398
Cdd:COG1136 5 LELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 -----FsaVFTDVWLFDRL-----------LGPGGKAADSALVDQWMAYLKMTHKLqldngrivDLK---LSKGQKKRVA 459
Cdd:COG1136 85 rrhigF--VFQFFNLLPELtalenvalpllLAGVSRKERRERARELLERVGLGDRL--------DHRpsqLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 460 LLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTE 529
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
75-509 |
2.46e-25 |
|
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: 109.76 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 75 LGHHFVFR----LRGEFIKRILDTQIEKVEKIGSASLLAGLTSDIRNITIAFVR--LPELVqGIILTFGSAAYLAWLSGK 148
Cdd:TIGR02868 76 VGHDAALRslgaLRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRviVPAGV-ALVVGAAAVAAIAVLSVP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 149 MMMVTALWMALTIWGGFVLVARVYR-HMATLRETEDKLYHDYQTVLEGRKELTLNRERAEYVfnqlylPDAREYRHHIIR 227
Cdd:TIGR02868 155 AALILAAGLLLAGFVAPLVSLRAARaAEQALARLRGELAAQLTDALDGAAELVASGALPAAL------AQVEEADRELTR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 228 ADTFHLSAVNWSNIMMLGAIGLVFWMANSLG---WANTAVAATYSLTLLFLRTPLLSAVGALP----TLLSAQVAFNKLN 300
Cdd:TIGR02868 229 AERRAAAATALGAALTLLAAGLAVLGALWAGgpaVADGRLAPVTLAVLVLLPLAAFEAFAALPaaaqQLTRVRAAAERIV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 301 TFSLAPYR---ADFPQPEPHPHWQ-TLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPA 376
Cdd:TIGR02868 309 EVLDAAGPvaeGSAPAAGAVGLGKpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 377 SGQILLDGQPLAADKPEDYRKLFSAVFTDVWLFD-------RLLGPGG------KAADSALVDQWMAYLK--MTHKLQLD 441
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDttvrenlRLARPDAtdeelwAALERVGLADWLRALPdgLDTVLGEG 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491003152 442 NGRivdlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQqmGKTVFAISHD 509
Cdd:TIGR02868 469 GAR-----LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
263-537 |
4.00e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.84 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 263 AVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNTFSLAPYRADFPQPEPHPhwqTLELRDVCFHYPDNSF----A 338
Cdd:COG1123 204 GVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEP---LLEVRNLSKRYPVRGKggvrA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 339 VGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL-----------FSA------ 401
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELrrrvqmvfqdpYSSlnprmt 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFDRLLGPGGKAADSALVDQWMaylkmthklqldngRIVDLK----------LSKGQKKRVALLLALAEERDII 471
Cdd:COG1123 361 VGDIIAEPLRLHGLLSRAERRERVAELL--------------ERVGLPpdladrypheLSGGQRQRVAIARALALEPKLL 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 472 LLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD----DHYfqhADRLLEMRSGQLTElTGEEREL 537
Cdd:COG1123 427 ILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlavvRYI---ADRVAVMYDGRIVE-DGPTEEV 492
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
323-527 |
6.36e-25 |
|
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: 101.52 E-value: 6.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAV-GPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:cd03246 1 LEVENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFDrllgpggkaadsalvdqwmaylkmthklqldnGRIVDLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:cd03246 81 LPQDDELFS--------------------------------GSIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491003152 482 PHfRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQL 527
Cdd:cd03246 129 VE-GERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
323-541 |
1.67e-24 |
|
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: 102.19 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDY---RKLF 399
Cdd:cd03261 1 IELRGLTKSFGGRTVLKG-VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 400 SAVFTDVWLFdrllgpggkaaDSALVDQWMAY-LKMTHKLQLDN-GRIVDLKL----------------SKGQKKRVALL 461
Cdd:cd03261 80 GMLFQSGALF-----------DSLTVFENVAFpLREHTRLSEEEiREIVLEKLeavglrgaedlypaelSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 462 LALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDH-YFQHADRLLEMRSGQLtELTGEERELATR 540
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDtAFAIADRIAVLYDGKI-VAEGTPEELRAS 227
|
.
gi 491003152 541 D 541
Cdd:cd03261 228 D 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
323-537 |
2.71e-24 |
|
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: 102.51 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS-FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDG-QPLAADKPEDYRKLFS 400
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFT-------------DVwLFdrllGPGGKAADSA----LVDQWMAYLKMTHklQLDNGrivDLKLSKGQKKRVALLLA 463
Cdd:TIGR04520 81 MVFQnpdnqfvgatvedDV-AF----GLENLGVPREemrkRVDEALKLVGMED--FRDRE---PHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 464 LAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLtELTGEEREL 537
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKI-VAEGTPREI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-529 |
2.71e-24 |
|
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: 106.14 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS-FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPA---SGQILLDGQPLAADKPEDYRKL 398
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 FSAVFTD-------VWLFD------RLLGPGGKAADsALVDQWMAYLKMTHKLQLDNGRivdlkLSKGQKKRVALLLALA 465
Cdd:COG1123 85 IGMVFQDpmtqlnpVTVGDqiaealENLGLSRAEAR-ARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 466 EERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTE 529
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIVE 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
324-522 |
4.60e-24 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 100.30 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYpDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPlaadkPEDYRKLFSAV- 402
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-----LEKERKRIGYVp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 ---------------------FTDVWLFDRLlgpggKAADSALVDQWMAYLKMTHKL--QLDNgrivdlkLSKGQKKRVA 459
Cdd:cd03235 75 qrrsidrdfpisvrdvvlmglYGHKGLFRRL-----SKADKAKVDEALERVGLSELAdrQIGE-------LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 460 LLLALAEERDIILLDEWAADQDPHFRREFYqQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEM 522
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIY-ELLRELRREGMTILVVTHDlGLVLEYFDRVLLL 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
324-527 |
5.17e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 101.61 E-value: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYPDNS-FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAV 402
Cdd:PRK13632 9 KVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FT-------------DV--WLFDRLLGPG---GKAADSALVDQWMAYLKMThklqldngrivDLKLSKGQKKRVALLLAL 464
Cdd:PRK13632 89 FQnpdnqfigatvedDIafGLENKKVPPKkmkDIIDDLAKKVGMEDYLDKE-----------PQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 465 AEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQL 527
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
323-543 |
5.32e-24 |
|
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: 100.77 E-value: 5.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYP-DNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFDrllgpgGKAADS-------ALVDQWMAYLKMTHKLQ----LDNG---RIVD--LKLSKGQKKRVALLLALA 465
Cdd:cd03251 81 VSQDVFLFN------DTVAENiaygrpgATREEVEEAARAANAHEfimeLPEGydtVIGErgVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491003152 466 EERDIILLDEWAADQDPhfRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEERELATRDAV 543
Cdd:cd03251 155 KDPPILILDEATSALDT--ESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE-RGTHEELLAQGGV 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
323-488 |
6.40e-24 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 100.70 E-value: 6.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYpDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSaV 402
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRL-----------LGPGGKAADSALVDQWMAYLKMTHKLqldNGRIvdLKLSKGQKKRVALLLALAEERDII 471
Cdd:COG4555 80 PDERGLYDRLtvreniryfaeLYGLFDEELKKRIEELIELLGLEEFL---DRRV--GELSTGMKKKVALARALVHDPKVL 154
|
170
....*....|....*..
gi 491003152 472 LLDEWAADQDPHFRREF 488
Cdd:COG4555 155 LLDEPTNGLDVMARRLL 171
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
323-540 |
1.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.58 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS--FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFS 400
Cdd:PRK13650 5 IEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFTDvwlfdrllgP-----GGKAADS---ALVDQWMAYLKMTHKLQ--LDNGRIVDLK------LSKGQKKRVALLLAL 464
Cdd:PRK13650 85 MVFQN---------PdnqfvGATVEDDvafGLENKGIPHEEMKERVNeaLELVGMQDFKereparLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 465 AEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLtELTGEERELATR 540
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV-ESTSTPRELFSR 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
323-509 |
1.70e-23 |
|
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: 98.70 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSF---AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEdyrklF 399
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 400 SAVFTDVWLFDRL-------LGPGGK-AADSALVDQWMAYLKMthklqldngriVDLK---------LSKGQKKRVALLL 462
Cdd:cd03293 76 GYVFQQDALLPWLtvldnvaLGLELQgVPKAEARERAEELLEL-----------VGLSgfenayphqLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491003152 463 ALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD 509
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-546 |
5.15e-23 |
|
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: 97.95 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYP---DNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLF 399
Cdd:COG1124 2 LEVRNLSVSYGqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 400 SAVFTD-------VWLFDRLLG-PG---GKAADSALVDQWMAYLKMTHKLqLDngRIVDlKLSKGQKKRVALLLALAEER 468
Cdd:COG1124 82 QMVFQDpyaslhpRHTVDRILAePLrihGLPDREERIAELLEQVGLPPSF-LD--RYPH-QLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 469 DIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLEMRSGQLTELTGEERELA-TRDAVART 546
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAgPKHPYTRE 237
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
323-529 |
6.95e-23 |
|
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: 95.84 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKpEDYRKLFSA 401
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFDRLLgpggkaadsalvdqwmaylkmthklqLDNgriVDLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:cd03247 80 LNQRPYLFDTTL--------------------------RNN---LGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491003152 482 PHFRREFYQQLLPLLQqmGKTVFAISHDDHYFQHADRLLEMRSGQLTE 529
Cdd:cd03247 131 PITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-482 |
1.51e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.46 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPE--DYRKLFS 400
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFTDVwlFDRLLGPggkaadsaLVDQWMAYLKMTHKLQLDN--GRIVD-LK--------------LSKGQKKRVALLLA 463
Cdd:PRK13639 82 IVFQNP--DDQLFAP--------TVEEDVAFGPLNLGLSKEEveKRVKEaLKavgmegfenkpphhLSGGQKKRVAIAGI 151
|
170
....*....|....*....
gi 491003152 464 LAEERDIILLDEWAADQDP 482
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDP 170
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
323-475 |
4.66e-22 |
|
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: 94.08 E-value: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYpDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADkPEDYRKLFSAV 402
Cdd:COG4133 3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-REDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRL---------LGPGGKAADSALVDQWMAYLKMTHKLQLDNGrivdlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:COG4133 81 GHADGLKPELtvrenlrfwAALYGLRADREAIDEALEAVGLAGLADLPVR-----QLSAGQKRRVALARLLLSPAPLWLL 155
|
..
gi 491003152 474 DE 475
Cdd:COG4133 156 DE 157
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
78-540 |
6.06e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.80 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 78 HFVFRLRGEFIKRILDTQIEKVEKIGSASLLAGLTSDIRNI--TIAFvRLPELVQGIILTFGSAAYLAWLSGKMMMVTAL 155
Cdd:TIGR00958 231 RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsrSLSL-NVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 156 WMALTIwggfvLVARVY--RHMATLRETEDKLYHDYQTVLEG-------------RKELTLNRERAEYVFnQLYLPDARE 220
Cdd:TIGR00958 310 NLPLVF-----LAEKVFgkRYQLLSEELQEAVAKANQVAEEAlsgmrtvrsfaaeEGEASRFKEALEETL-QLNKRKALA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 221 YRHHIiradtfhlsavnWSN-IMMLGAIGLVFW------MANSLGWANTAVAATYSL-------TLLFLRTPLLSAVGAl 286
Cdd:TIGR00958 384 YAGYL------------WTTsVLGMLIQVLVLYyggqlvLTGKVSSGNLVSFLLYQEqlgeavrVLSYVYSGMMQAVGA- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 287 ptllSAQVafnklntFSLAPYRADFPQPEPH-PHWQT--LELRDVCFHYP---DNSFAVGpINLTLQRGELVFLIGGNGS 360
Cdd:TIGR00958 451 ----SEKV-------FEYLDRKPNIPLTGTLaPLNLEglIEFQDVSFSYPnrpDVPVLKG-LTFTLHPGEVVALVGPSGS 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 361 GKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVFTDVWLFDRLLGPG-GKAADSALVDQWMAYLKMTHK-- 437
Cdd:TIGR00958 519 GKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENiAYGLTDTPDEEIMAAAKAANAhd 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 438 --LQLDNGRIVDL-----KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLlqqmGKTVFAISHDD 510
Cdd:TIGR00958 599 fiMEFPNGYDTEVgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA----SRTVLLIAHRL 674
|
490 500 510
....*....|....*....|....*....|
gi 491003152 511 HYFQHADRLLEMRSGQLTELtGEERELATR 540
Cdd:TIGR00958 675 STVERADQILVLKKGSVVEM-GTHKQLMED 703
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-528 |
7.09e-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: 92.49 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDyrklfsav 402
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 ftdvwlfdrllgpgGKAADSALVDQwmaylkmthklqldngrivdlkLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:cd03216 72 --------------ARRAGIAMVYQ----------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491003152 483 HFRREFYqQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLT 528
Cdd:cd03216 116 AEVERLF-KVIRRLRAQGVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
323-509 |
1.29e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 93.67 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAvgpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPedYRKLFSAV 402
Cdd:COG3840 2 LRLDDLTYRYGDFPLR---FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRL---------LGPGGK--AADSALVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLALAEERDII 471
Cdd:COG3840 77 FQENNLFPHLtvaqniglgLRPGLKltAEQRAQVEQALERVGLAGLLD----RLPG-QLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 491003152 472 LLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD 509
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
332-509 |
1.61e-21 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 92.10 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 332 YPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADK----------------PEDy 395
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkgllerrqrvglvfqdPDD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 396 rKLFSA-VFTDVWLFDRLLGpGGKAADSALVDQWMAYLKMTHKLQldngRIVDLkLSKGQKKRVALLLALAEERDIILLD 474
Cdd:TIGR01166 80 -QLFAAdVDQDVAFGPLNLG-LSEAEVERRVREALTAVGASGLRE----RPTHC-LSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 491003152 475 EWAADQDPHFRREFyQQLLPLLQQMGKTVFAISHD 509
Cdd:TIGR01166 153 EPTAGLDPAGREQM-LAILRRLRAEGMTVVISTHD 186
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
323-540 |
2.11e-21 |
|
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: 93.32 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHY-PDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFDRLLgpggkAADSALVDQWM--------AYLKMTH----KLQLDNGRIVDLK---LSKGQKKRVALLLALAE 466
Cdd:cd03252 81 VLQENVLFNRSI-----RDNIALADPGMsmervieaAKLAGAHdfisELPEGYDTIVGEQgagLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 467 ERDIILLDEWAADQDphFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEERELATR 540
Cdd:cd03252 156 NPRILIFDEATSALD--YESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVE-QGSHDELLAE 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
338-534 |
2.47e-21 |
|
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: 93.86 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL----FSAVFTDVWLFdrll 413
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALL---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 414 gPGGKAADSAL-------VDQWMAYLKMTHKLQLdngriVDLK---------LSKGQKKRVALLLALAEERDIILLDEWA 477
Cdd:cd03294 115 -PHRTVLENVAfglevqgVPRAEREERAAEALEL-----VGLEgwehkypdeLSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 478 ADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTEL-TGEE 534
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDlDEALRLGDRIAIMKDGRLVQVgTPEE 247
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
292-522 |
2.98e-21 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 96.97 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 292 AQVAFNKLNTFSLAPYRADFPQ-PEPHPHWQTLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLT 370
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRPLAGKaPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 371 GLYQPASGQILLDGQPLAADKPEDYRKLFSAVFTDVWLFD-------RLLGPGGKAADS------ALVDQWMAYLKMTHK 437
Cdd:TIGR02857 370 GFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAgtiaeniRLARPDASDAEIrealerAGLDEFVAALPQGLD 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 438 LQL-DNGRivdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQqmGKTVFAISHDDHYFQHA 516
Cdd:TIGR02857 450 TPIgEGGA----GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA 523
|
....*.
gi 491003152 517 DRLLEM 522
Cdd:TIGR02857 524 DRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
323-537 |
7.38e-21 |
|
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: 91.52 E-value: 7.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAV 402
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRLLGPGGKAADSALVDQWM---AYLKMTHK--LQLDNG--RIV---DLKLSKGQKKRVALLLALAEERDIIL 472
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVieaAKAAQIHDkiMRFPDGydTIVgerGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 473 LDEWAADQDPHFRREFYQQLLPLLQqmGKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEEREL 537
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVE-RGTHEEL 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
323-529 |
7.93e-21 |
|
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: 91.41 E-value: 7.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSF---AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPE---DYR 396
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 397 KLFSAVFTD----------VW--LFDRLLGPGGKAADSALVDQWMAYLKmthKLQLDNgRIVDLK---LSKGQKKRVALL 461
Cdd:cd03257 82 KEIQMVFQDpmsslnprmtIGeqIAEPLRIHGKLSKKEARKEAVLLLLV---GVGLPE-EVLNRYpheLSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 462 LALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLEMRSGQLTE 529
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
323-527 |
8.92e-21 |
|
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: 90.99 E-value: 8.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPD--NSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFS 400
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFTDVWLFDRLL------GPGGK-------AADSALVDQWMAylKMTHKLQLDNGRIVDLkLSKGQKKRVALLLALAEE 467
Cdd:cd03248 92 LVGQEPVLFARSLqdniayGLQSCsfecvkeAAQKAHAHSFIS--ELASGYDTEVGEKGSQ-LSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 468 RDIILLDEWAADQDPHFRREFYQQLLPLLQQmgKTVFAISHDDHYFQHADRLLEMRSGQL 527
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
323-527 |
3.66e-20 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 89.10 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL--- 398
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 --FSAVFTD------VWLFDRLLGPGGKAADsALVDQWMAYLKMTHKLqldNGRIVDlkLSKGQKKRVALLLALAEERDI 470
Cdd:cd03263 81 pqFDALFDEltvrehLRFYARLKGLPKSEIK-EEVELLLRVLGLTDKA---NKRART--LSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491003152 471 ILLDEWAADQDPHFRREFYQQLLPLLQqmGKTVFAISHDDHYFQH-ADRLLEMRSGQL 527
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
323-475 |
7.05e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 91.31 E-value: 7.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNsFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDyRKlFSAV 402
Cdd:COG3842 6 LELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-RN-VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFD------------RLLGPGGKAADsALVDQWMAYLKMTHKLqldnGRIVDlKLSKGQKKRVALLLALAEERDI 470
Cdd:COG3842 83 FQDYALFPhltvaenvafglRMRGVPKAEIR-ARVAELLELVGLEGLA----DRYPH-QLSGGQQQRVALARALAPEPRV 156
|
....*
gi 491003152 471 ILLDE 475
Cdd:COG3842 157 LLLDE 161
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
323-509 |
1.66e-19 |
|
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: 87.73 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYpdNSFAV--GpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL-- 398
Cdd:COG1127 6 IEVRNLTKSF--GDRVVldG-VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 -------FSAVFTD--VW------LFDRLLGPGGKAADSALVdqwmaylkmthKLQLdngriVDLK---------LSKGQ 454
Cdd:COG1127 83 rigmlfqGGALFDSltVFenvafpLREHTDLSEAEIRELVLE-----------KLEL-----VGLPgaadkmpseLSGGM 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 455 KKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD 509
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHD 201
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
323-525 |
1.74e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.27 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHY-PDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTD--------VWLFDRLLGpggkaadsaLVDQWMAYLKMTHKLQ--------LDNGRIVDLKLSKGQKKRVALLLALA 465
Cdd:PRK13648 88 VFQNpdnqfvgsIVKYDVAFG---------LENHAVPYDEMHRRVSealkqvdmLERADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 466 EERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSG 525
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-529 |
1.75e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.42 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED---YRKLF 399
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 400 SAVFTDVWLFD------------RLLGPGGKAADSAlVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLALAEE 467
Cdd:COG2884 82 GVVFQDFRLLPdrtvyenvalplRVTGKSRKEIRRR-VREVLDLVGLSDKAK----ALPH-ELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491003152 468 RDIILLDEWAADQDP--------HFRRefyqqllplLQQMGKTVFAISHDDHYFQHAD-RLLEMRSGQLTE 529
Cdd:COG2884 156 PELLLADEPTGNLDPetsweimeLLEE---------INRRGTTVLIATHDLELVDRMPkRVLELEDGRLVR 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
267-537 |
3.51e-19 |
|
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: 91.34 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 267 TYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNTFSLAPyrADFPQPEPHPHWQTL----ELRDVCFHYPDNSFAVGPI 342
Cdd:TIGR01193 416 TFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVD--SEFINKKKRTELNNLngdiVINDVSYSYGYGSNILSDI 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 343 NLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVFTDVWLFD------RLLG-- 414
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSgsilenLLLGak 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 415 PGG------KAADSALVDQWMAYLKMTHKLQL--DNGRIvdlklSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRR 486
Cdd:TIGR01193 574 ENVsqdeiwAACEIAEIKDDIENMPLGYQTELseEGSSI-----SGGQKQRIALARALLTDSKVLILDESTSNLDTITEK 648
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 491003152 487 EFYQQLLPLLQqmgKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEEREL 537
Cdd:TIGR01193 649 KIVNNLLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKIIE-QGSHDEL 695
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
323-527 |
3.56e-19 |
|
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: 86.52 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYpDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPedYRKLFSAV 402
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRL-------LGPGGKAADSALVDQWMA-YLKMTHKLQLDNGRIVdlKLSKGQKKRVALLLALAEERDIILLD 474
Cdd:cd03300 78 FQNYALFPHLtvfeniaFGLRLKKLPKAEIKERVAeALDLVQLEGYANRKPS--QLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491003152 475 EWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGKI 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
312-537 |
3.61e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.51 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 312 PQPEPHPHWQT---LELRDVCFHYpDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLA 388
Cdd:PRK11607 6 PRPQAKTRKALtplLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 389 ADKPedYRKLFSAVFTDVWLF---------------DRLlgpgGKAADSALVDQwmaYLKMTHKLQLDNGRivDLKLSKG 453
Cdd:PRK11607 85 HVPP--YQRPINMMFQSYALFphmtveqniafglkqDKL----PKAEIASRVNE---MLGLVHMQEFAKRK--PHQLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 454 QKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTELtG 532
Cdd:PRK11607 154 QRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGKFVQI-G 232
|
....*
gi 491003152 533 EEREL 537
Cdd:PRK11607 233 EPEEI 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
323-475 |
4.49e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.07 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS---FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEdyrklF 399
Cdd:COG1116 8 LELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 400 SAVFTDvwlfDRL-----------LGPGGKAADSALVDQW-MAYLKMthklqldngriVDLK---------LSKGQKKRV 458
Cdd:COG1116 83 GVVFQE----PALlpwltvldnvaLGLELRGVPKAERRERaRELLEL-----------VGLAgfedayphqLSGGMRQRV 147
|
170
....*....|....*..
gi 491003152 459 ALLLALAEERDIILLDE 475
Cdd:COG1116 148 AIARALANDPEVLLMDE 164
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-547 |
1.19e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.01 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAV 402
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 F--TDVWLF------DRLLGPGGKAADSALVDQWMAylKMTHKLQLDNGRI-VDLKLSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK13652 84 FqnPDDQIFsptveqDIAFGPINLGLDEETVAHRVS--SALHMLGLEELRDrVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 474 DEWAADQDPHFRREFYQQLLPLLQQMGKTV-FAISHDDHYFQHADRLLEMRSGQLTElTGEERELATRDAVARTA 547
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTViFSTHQLDLVPEMADYIYVMDKGRIVA-YGTVEEIFLQPDLLARV 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
323-526 |
1.52e-18 |
|
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: 84.93 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFS-- 400
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 -AVFTDVWLFDRL------LgpGGKAADSALvdqWMAYLKMTHKLQ-------LDNGRIVDL------KLSKGQKKRVAL 460
Cdd:cd03256 81 gMIFQQFNLIERLsvlenvL--SGRLGRRST---WRSLFGLFPKEEkqralaaLERVGLLDKayqradQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 461 LLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYF-QHADRLLEMRSGQ 526
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGR 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
323-533 |
1.56e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPlAAD--KPEDYRKLFS 400
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDfsKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFTD--------VWLFDRLLGPGG---------KAADSALVDqwmaylkmthkLQLDNGRIVDLK-LSKGQKKRVALLL 462
Cdd:PRK13644 81 IVFQNpetqfvgrTVEEDLAFGPENlclppieirKRVDRALAE-----------IGLEKYRHRSPKtLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491003152 463 ALAEERDIILLDEWAADQDPHfRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTeLTGE 533
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPD-SGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV-LEGE 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
323-527 |
1.90e-18 |
|
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: 84.00 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKP---------- 392
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipylrrki 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 393 ----EDYRKLFS-AVFTDVWLFDRLLGPGGKAAD---SALVDQwmayLKMTHKlqldnGRIVDLKLSKGQKKRVALLLAL 464
Cdd:cd03292 81 gvvfQDFRLLPDrNVYENVAFALEVTGVPPREIRkrvPAALEL----VGLSHK-----HRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 465 AEERDIILLDEWAADQDPHFRREFyQQLLPLLQQMGKTVFAISHDDHYFQ-HADRLLEMRSGQL 527
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEI-MNLLKKINKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
323-527 |
2.15e-18 |
|
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: 84.41 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCfhypdNSF----AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL 398
Cdd:cd03219 1 LEVRGLT-----KRFgglvALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 -FSAVFTDVWLFDRL---------------------LGPGGKAADSALVDQWMAYLKMTHKLqldnGRIVDLkLSKGQKK 456
Cdd:cd03219 76 gIGRTFQIPRLFPELtvlenvmvaaqartgsglllaRARREEREARERAEELLERVGLADLA----DRPAGE-LSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491003152 457 RVALLLALAEERDIILLDEWAADQDPHFRREFyQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEEL-AELIRELRERGITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
324-527 |
3.09e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 84.36 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYpDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDY-RKL---- 398
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELaKRLailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 ----FSAVFT--DVWLFDRLLGPGGK--AADSALVDQWMAYLKMTHkLQldnGRIVDlKLSKGQKKRVALLLALAEERDI 470
Cdd:COG4604 82 qenhINSRLTvrELVAFGRFPYSKGRltAEDREIIDEAIAYLDLED-LA---DRYLD-ELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491003152 471 ILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD----DHYfqhADRLLEMRSGQL 527
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDinfaSCY---ADHIVAMKDGRV 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
323-527 |
3.72e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.85 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQP---ASGQILLDGQPLAADKPEDYRKL 398
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 FSAVFTDvwlfdrllgPGGKAAdSALVDQWMAY------------LKMTHKLQLDNGRIVDLK-----LSKGQKKRVALL 461
Cdd:PRK13640 86 VGIVFQN---------PDNQFV-GATVGDDVAFglenravprpemIKIVRDVLADVGMLDYIDsepanLSGGQKQRVAIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 462 LALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQL 527
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
323-527 |
3.83e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 84.32 E-value: 3.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHypdnsF----AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL 398
Cdd:COG0411 5 LEVRGLTKR-----FgglvAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 -----F--SAVFTD----------------VWLFDRLLGPGGKAAD----SALVDQWMAYLKMTHKLqldnGRIVDLkLS 451
Cdd:COG0411 80 giartFqnPRLFPEltvlenvlvaaharlgRGLLAALLRLPRARREereaRERAEELLERVGLADRA----DEPAGN-LS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 452 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIVVLDFGRV 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
323-533 |
4.22e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 4.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFaVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFS-- 400
Cdd:PRK10247 8 LQLQNVGYLAGDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSyc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 ----AVFTDVwLFDRLLGP---GGKAAD-SALVDQWMAYLKMTHKLQldnGRIVDlkLSKGQKKRVALLLALAEERDIIL 472
Cdd:PRK10247 87 aqtpTLFGDT-VYDNLIFPwqiRNQQPDpAIFLDDLERFALPDTILT---KNIAE--LSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 473 LDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRL--LEMRSGQLTELTGE 533
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVitLQPHAGEMQEARYE 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
323-519 |
5.25e-18 |
|
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: 82.93 E-value: 5.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAvgpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDyrKLFSAV 402
Cdd:cd03298 1 VRLDKIRFSYGEQPMH---FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRL---------LGPGGK--AADSALVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLALAEERDII 471
Cdd:cd03298 76 FQENNLFAHLtveqnvglgLSPGLKltAEDRQAIEVALARVGLAGLEK----RLPG-ELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491003152 472 LLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAIShddHYFQHADRL 519
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVT---HQPEDAKRL 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
323-544 |
5.28e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.40 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRK----- 397
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 -------LFSA-VFTDVWLFDRLLGPGGKAADS------ALVDQWMAYLKMTHklqldngrivdlKLSKGQKKRVALLLA 463
Cdd:PRK13647 85 fqdpddqVFSStVWDDVAFGPVNMGLDKDEVERrveealKAVRMWDFRDKPPY------------HLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 464 LAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGQlTELTGEERELATRDA 542
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDvDLAAEWADQVIVLKEGR-VLAEGDKSLLTDEDI 230
|
..
gi 491003152 543 VA 544
Cdd:PRK13647 231 VE 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
321-541 |
8.44e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.60 E-value: 8.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 321 QTLELRDVCFHYPDNSFA--VGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL 398
Cdd:PRK13642 3 KILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 FSAVFTDVwlfDRLLGPGGKAADSA--LVDQWMAYLKMTHKLQ--LDNGRIVDLK------LSKGQKKRVALLLALAEER 468
Cdd:PRK13642 83 IGMVFQNP---DNQFVGATVEDDVAfgMENQGIPREEMIKRVDeaLLAVNMLDFKtreparLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 469 DIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTELTGEERELATRD 541
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
322-527 |
1.15e-17 |
|
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: 82.39 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 322 TLELRDVCFHYPDnsF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFs 400
Cdd:cd03296 2 SIEVRNVSKRFGD--FvALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 aVFTDVWLFDRL-----------LGPGGKAADSALVDQ-WMAYLKMthkLQLDN-GRIVDLKLSKGQKKRVALLLALAEE 467
Cdd:cd03296 79 -VFQHYALFRHMtvfdnvafglrVKPRSERPPEAEIRAkVHELLKL---VQLDWlADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491003152 468 RDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDqEEALEVADRVVVMNKGRI 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-541 |
1.16e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAV-GPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLF-----DRLLGPGGKAADSALV------------------DQWMAylkmthklqlDNGRivdlKLSKGQKKRV 458
Cdd:PRK11160 419 VSQRVHLFsatlrDNLLLAAPNASDEALIevlqqvgleklleddkglNAWLG----------EGGR----QLSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 459 ALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQqmGKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEERELA 538
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIE-QGTHQELL 561
|
...
gi 491003152 539 TRD 541
Cdd:PRK11160 562 AQQ 564
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
323-529 |
1.29e-17 |
|
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: 81.77 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS-FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:cd03244 3 IEFKNVSLRYRPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFD---RL-LGPGGKAADSALvdqWMAyLKMTH-------KLQLDNGRIVD--LKLSKGQKKRVALLLALAEER 468
Cdd:cd03244 83 IPQDPVLFSgtiRSnLDPFGEYSDEEL---WQA-LERVGlkefvesLPGGLDTVVEEggENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 469 DIILLDEWAADQDPH--------FRREFyqqllpllqqMGKTVFAISHDDHYFQHADRLLEMRSGQLTE 529
Cdd:cd03244 159 KILVLDEATASVDPEtdaliqktIREAF----------KDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
338-526 |
2.46e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 80.79 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADK-------PED---YRKLfsAVFTDVW 407
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEErglYPKM--KVIDQLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 408 LFDRLLGPGGKAAdSALVDQWMAYLKMTHKLqldNGRIVdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDP----H 483
Cdd:cd03269 93 YLAQLKGLKKEEA-RRRIDEWLERLELSEYA---NKRVE--ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPvnveL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491003152 484 FRREFyqqllPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQ 526
Cdd:cd03269 167 LKDVI-----RELARAGKTVILSTHQmELVEELCDRVLLLNKGR 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
323-529 |
3.30e-17 |
|
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: 81.78 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSF--------AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED 394
Cdd:TIGR02769 3 LEVRDVTHTYRTGGLfgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 395 ---YRKLFSAVFTDvwlfdrllGPGGKAADSALvdQWMAYLKMTHKLQLDNG----------RIVDL----------KLS 451
Cdd:TIGR02769 83 rraFRRDVQLVFQD--------SPSAVNPRMTV--RQIIGEPLRHLTSLDESeqkariaellDMVGLrsedadklprQLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 452 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLEMRSGQLTE 529
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
323-536 |
3.51e-17 |
|
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: 80.84 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDnsFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEdyRKLFSAV 402
Cdd:cd03299 1 LKVENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRL-----------LGPGGKAADSALVDQWMAYLKMTHKLQLDNGRivdlkLSKGQKKRVALLLALAEERDII 471
Cdd:cd03299 77 PQNYALFPHMtvykniayglkKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-----LSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 472 LLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTELtGEERE 536
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQV-GKPEE 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
333-536 |
3.97e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.02 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 333 PDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAAD--KPEDYRKLFSAVFT--DVWL 408
Cdd:PRK13637 17 PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvKLSDIRKKVGLVFQypEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 409 F------DRLLGPGGKA-ADSALVDQWMAYLKMthkLQLDNGRIVD---LKLSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:PRK13637 97 FeetiekDIAFGPINLGlSEEEIENRVKRAMNI---VGLDYEDYKDkspFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 479 DQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLtELTGEERE 536
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKC-ELQGTPRE 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
342-525 |
5.96e-17 |
|
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: 80.20 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPE------DYRKL-FSAVFTDVWL-FDRLL 413
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvvfqNYSLLpWLTVRENIALaVDRVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 414 GPGGKAADSALVDQWMAYLKMTHKLQLDNGrivdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLL 493
Cdd:TIGR01184 84 PDLSKSERRAIVEEHIALVGLTEAADKRPG-----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190
....*....|....*....|....*....|...
gi 491003152 494 PLLQQMGKTVFAISHD-DHYFQHADRLLEMRSG 525
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
323-537 |
1.21e-16 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 79.16 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSF---AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRK-- 397
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 -----------LFSA--VFTDVWLFDRLLGPGGKAADSAlVDQWMAYLKMTHKlqldnGRIVDLKLSKGQKKRVALLLAL 464
Cdd:cd03258 82 rrigmifqhfnLLSSrtVFENVALPLEIAGVPKAEIEER-VLELLELVGLEDK-----ADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 465 AEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLEMRSGQLTElTGEEREL 537
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVE-EGTVEEV 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
342-528 |
2.96e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.52 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSavftdvWLFDRLLGPGG---- 417
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA------LLPQHHLTPEGitvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 418 -----------------KAADSALVDQWMAylkMTHKLQLDNGRIVDlkLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:PRK11231 95 elvaygrspwlslwgrlSAEDNARVNQAME---QTRINHLADRRLTD--LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491003152 481 DPHFRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGQLT 528
Cdd:PRK11231 170 DINHQVELMRLMRELNTQ-GKTVVTVLHDlNQASRYCDHLVVLANGHVM 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
342-529 |
3.47e-16 |
|
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: 77.57 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPlaadkpedyrklfsavftdVWLFD----------- 410
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-------------------SSLLGlgggfnpeltg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 411 --------RLLGpggkaADSALVDQWMAYLKMTHKLqldnGRIVDLKL---SKGQKKRVALLLALAEERDIILLDEWAAD 479
Cdd:cd03220 102 reniylngRLLG-----LSRKEIDEKIDEIIEFSEL----GDFIDLPVktySSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491003152 480 QDPHFR-------REFyqqllpllQQMGKTVFAISHDDHYF-QHADRLLEMRSGQLTE 529
Cdd:cd03220 173 GDAAFQekcqrrlREL--------LKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRF 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
342-527 |
3.60e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.10 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKP----EDYRKLFSAVF--TDVWLF------ 409
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFqfPEAQLFentvlk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 410 DRLLGPGG------KAADSALvdQWMAYLKMTHKLQLDNgrivDLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:PRK13641 106 DVEFGPKNfgfsedEAKEKAL--KWLKKVGLSEDLISKS----PFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491003152 484 FRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:PRK13641 180 GRKEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
323-487 |
5.07e-16 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 77.18 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPE--DYRKLFS 400
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKG-IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFTDVWLFDRL-------LGP---GGKAADSAlVDQWMAYLKmthKLQLDNgRIVDL--KLSKGQKKRVALLLALAEER 468
Cdd:cd03262 80 MVFQQFNLFPHLtvlenitLAPikvKGMSKAEA-EERALELLE---KVGLAD-KADAYpaQLSGGQQQRVAIARALAMNP 154
|
170
....*....|....*....
gi 491003152 469 DIILLDEWAADQDPHFRRE 487
Cdd:cd03262 155 KVMLFDEPTSALDPELVGE 173
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
322-537 |
6.37e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.28 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 322 TLELRDVCFHY----PDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDY-- 395
Cdd:PRK13646 2 TIRFDNVSYTYqkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 396 --RKLFSAVFT--DVWLFDR------LLGPGGKAADsalVDQWMAYlkmTHKLQLDNGRIVDL------KLSKGQKKRVA 459
Cdd:PRK13646 82 pvRKRIGMVFQfpESQLFEDtvereiIFGPKNFKMN---LDEVKNY---AHRLLMDLGFSRDVmsqspfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 460 LLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTElTGEEREL 537
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVS-QTSPKEL 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
339-527 |
7.99e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 7.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 339 VGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYqPASGQILLDGQPLAADKPED---YRKLFS-----AVFTDVWLFD 410
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElarHRAYLSqqqspPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 411 RLLGPGGkaADSALVDQWMAYLkmTHKLQLDN--GRIVDlKLSKGQKKRV---ALLL----ALAEERDIILLDEWAADQD 481
Cdd:COG4138 91 ALHQPAG--ASSEAVEQLLAQL--AEALGLEDklSRPLT-QLSGGEWQRVrlaAVLLqvwpTINPEGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491003152 482 PH-------FRREFyqqllpllQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:COG4138 166 VAqqaaldrLLREL--------CQQGITVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-537 |
8.33e-16 |
|
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: 76.81 E-value: 8.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYPD--NSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:cd03249 2 EFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFDR------LLGpggkaADSALVDQWMAYLKMT--HKLqldngrIVDL-------------KLSKGQKKRVAL 460
Cdd:cd03249 82 VSQEPVLFDGtiaeniRYG-----KPDATDEEVEEAAKKAniHDF------IMSLpdgydtlvgergsQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 461 LLALAEERDIILLDEWAADQDPHfrREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEEREL 537
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAE--SEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE-QGTHDEL 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
342-475 |
1.40e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.73 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLfSAV----------FT--DVWLF 409
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAVlpqhsslsfpFTveEVVAM 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491003152 410 DRLLGPGGKAADSALVDQWMAYLKMTHKLQLDNgrivdLKLSKGQKKRVALLLALA------EERDIILLDE 475
Cdd:PRK13548 100 GRAPHGLSRAEDDALVAAALAQVDLAHLAGRDY-----PQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDE 166
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
323-537 |
1.52e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.37 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS-F---AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADK-PEDYRK 397
Cdd:PRK13634 3 ITFQKVEHRYQYKTpFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 LFSAV-----FTDVWLF------DRLLGP---GGKAADS-ALVDQWMAYLKMTHKLqLDNGrivDLKLSKGQKKRVALLL 462
Cdd:PRK13634 83 LRKKVgivfqFPEHQLFeetvekDICFGPmnfGVSEEDAkQKAREMIELVGLPEEL-LARS---PFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 463 ALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTeLTGEEREL 537
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKGTVF-LQGTPREI 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
336-530 |
1.98e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.15 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 336 SFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLA----ADKPEDYRKLFSAVFTDVWLFdr 411
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRRKKIAMVFQSFALM-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 412 llgPGGKAADSALVDQWMAYLKMTHKLQ--LDNGRIVDL---------KLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:PRK10070 119 ---PHMTVLDNTAFGMELAGINAEERREkaLDALRQVGLenyahsypdELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491003152 481 DPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTEL 530
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQV 246
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
278-528 |
2.00e-15 |
|
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: 79.02 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 278 PLLSAVGALPTLLSAQVAFNKLNT-FSLAPYRADF-PQPEPHPHwqtLELRDVCFHYP-DNSFAVGPINLTLQRGELVFL 354
Cdd:COG4618 287 PIEQAIGGWKQFVSARQAYRRLNElLAAVPAEPERmPLPRPKGR---LSVENLTVVPPgSKRPILRGVSFSLEPGEVLGV 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 355 IGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVFTDVWLFD--------RLLGPGG----KAADS 422
Cdd:COG4618 364 IGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDgtiaeniaRFGDADPekvvAAAKL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 423 ALVDQWMaylkmthkLQLDNG---RIVD--LKLSKGQKKRVALLLALAEERDIILLDEWAADQDP-----------HFRR 486
Cdd:COG4618 444 AGVHEMI--------LRLPDGydtRIGEggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDegeaalaaairALKA 515
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 491003152 487 EfyqqllpllqqmGKTVFAISHDDHYFQHADRLLEMRSGQLT 528
Cdd:COG4618 516 R------------GATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
323-527 |
2.87e-15 |
|
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: 74.98 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYpDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDyRKLfSAV 402
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDI-AMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRL-----------LGPGGKAADSALVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLALAEERDII 471
Cdd:cd03301 78 FQNYALYPHMtvydniafglkLRKVPKDEIDERVREVAELLQIEHLLD----RKPK-QLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 472 LLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqVEAMTMADRIAVMNDGQI 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
322-475 |
3.23e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.11 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 322 TLELRDVCFHYPDnsF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL-F 399
Cdd:COG1118 2 SIEVRNISKRFGS--FtLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVgF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 400 saVFTDVWLFDRL-----------LGPGGKAADSALVDQWmayLKMthkLQLDngrivDLK------LSKGQKKRVALLL 462
Cdd:COG1118 80 --VFQHYALFPHMtvaeniafglrVRPPSKAEIRARVEEL---LEL---VQLE-----GLAdrypsqLSGGQRQRVALAR 146
|
170
....*....|...
gi 491003152 463 ALAEERDIILLDE 475
Cdd:COG1118 147 ALAVEPEVLLLDE 159
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
342-529 |
5.76e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.11 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED---YRKLFSAVFTDvwlfdrllGPGgk 418
Cdd:PRK10419 31 VSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQD--------SIS-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 419 AADSALVDQWMAYLKMTHKLQLDNG----------RIVDL----------KLSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:PRK10419 101 AVNPRKTVREIIREPLRHLLSLDKAerlarasemlRAVDLddsvldkrppQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491003152 479 DQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLEMRSGQLTE 529
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
323-543 |
7.62e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.37 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPD-NSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:PRK11176 342 IEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLF-DRLLGPGGKAADsalvDQW----------MAYL-----KMTHKLQL---DNGrivdLKLSKGQKKRVALLL 462
Cdd:PRK11176 422 VSQNVHLFnDTIANNIAYART----EQYsreqieeaarMAYAmdfinKMDNGLDTvigENG----VLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 463 ALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQqmGKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEERELATRDA 542
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVE-RGTHAELLAQNG 570
|
.
gi 491003152 543 V 543
Cdd:PRK11176 571 V 571
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
323-537 |
1.83e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.97 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS-----FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGqpLAADKPE---D 394
Cdd:PRK13633 5 IKCKNVSYKYESNEestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEEnlwD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 395 YRKLFSAVFT--DVWLF------DRLLGPGG---------KAADSAL--VDQWmAYLKMTHKLqldngrivdlkLSKGQK 455
Cdd:PRK13633 83 IRNKAGMVFQnpDNQIVativeeDVAFGPENlgippeeirERVDESLkkVGMY-EYRRHAPHL-----------LSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 456 KRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTeLTGEER 535
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV-MEGTPK 229
|
..
gi 491003152 536 EL 537
Cdd:PRK13633 230 EI 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-475 |
1.96e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYP-----DNsfavgpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRK 397
Cdd:COG3845 6 LELRGITKRFGgvvanDD------VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 L--------FSavftdvwLFDRL-------LG----PGGKAADSALVDQWMAYLKmTHKLQLDNGRIVDlKLSKGQKKRV 458
Cdd:COG3845 80 LgigmvhqhFM-------LVPNLtvaenivLGleptKGGRLDRKAARARIRELSE-RYGLDVDPDAKVE-DLSVGEQQRV 150
|
170
....*....|....*..
gi 491003152 459 ALLLALAEERDIILLDE 475
Cdd:COG3845 151 EILKALYRGARILILDE 167
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
323-483 |
2.63e-14 |
|
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: 72.21 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLY-----QPASGQILLDGQPLAADK--PEDY 395
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDvdVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 396 RK----------LFSA-VFTDVWLFDRLLGPGGKAADSALVDQW--MAYLKMTHKLQLDNgrivdLKLSKGQKKRVALLL 462
Cdd:cd03260 80 RRrvgmvfqkpnPFPGsIYDNVAYGLRLHGIKLKEELDERVEEAlrKAALWDEVKDRLHA-----LGLSGGQQQRLCLAR 154
|
170 180
....*....|....*....|.
gi 491003152 463 ALAEERDIILLDEWAADQDPH 483
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPI 175
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
349-527 |
2.76e-14 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 71.94 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 349 GELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPL-----AADKPEDYRKLfSAVFTDVWLFDRL---------LG 414
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkKINLPPQQRKI-GLVFQQYALFPHLnvrenlafgLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 415 PGGKAADSALVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLP 494
Cdd:cd03297 102 RKRNREDRISVDELLDLLGLDHLLN----RYPA-QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....
gi 491003152 495 LLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:cd03297 177 IKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGRL 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
313-527 |
3.47e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 313 QPEPHPHWQTLELRDVCFHYPDNSFaVGPINLTLQRGELVFLIGGNGSGKSTLAMLLtGLYQPAS-GQILLDGQPLAADK 391
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSeGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 392 PEDY--------RKLFSA--------VFTDVWLFDRLLGPGGkAADSALVDQWMAYLKMTHKLQldngRIVDlKLSKGQK 455
Cdd:PRK10575 80 SKAFarkvaylpQQLPAAegmtvrelVAIGRYPWHGALGRFG-AADREKVEEAISLVGLKPLAH----RLVD-SLSGGER 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 456 KRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDiNMAARYCDYLVALRGGEM 226
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
342-522 |
3.67e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.11 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDG--------QPLAADK--PEDYRKLfsaVFTDVWLFDR 411
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpQRSEVPDslPLTVRDL---VAMGRWARRG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 412 LLGPGGkAADSALVDQWMAYLKMT--HKLQLDngrivdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFY 489
Cdd:NF040873 88 LWRRLT-RDDRAAVDDALERVGLAdlAGRQLG-------ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|...
gi 491003152 490 QQLLPLLQQmGKTVFAISHDDHYFQHADRLLEM 522
Cdd:NF040873 160 ALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
323-536 |
3.86e-14 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 72.08 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVG---PINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAA-DkpEDYRKL 398
Cdd:COG4181 9 IELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAlD--EDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 FSA-----VFTDVWLFDRL-----------LGPGGKAADSALvdQWMAYLKMTHKL-----QldngrivdlkLSKGQKKR 457
Cdd:COG4181 87 LRArhvgfVFQSFQLLPTLtalenvmlpleLAGRRDARARAR--ALLERVGLGHRLdhypaQ----------LSGGEQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 458 VALLLALAEERDIILLDEWAADQDPH---------F--RREfyqqllpllqqMGKTVFAISHDDHYFQHADRLLEMRSGQ 526
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAAtgeqiidllFelNRE-----------RGTTLVLVTHDPALAARCDRVLRLRAGR 223
|
250
....*....|
gi 491003152 527 LTELTGEERE 536
Cdd:COG4181 224 LVEDTAATAA 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
342-540 |
3.94e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 73.96 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFS----AVFTDVWLFD------R 411
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVfqhyALFRHMTVFDniafglT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 412 LLgPGGKAADSALVDQ-WMAYLKMthkLQLdnGRIVD---LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE 487
Cdd:PRK10851 101 VL-PRRERPNAAAIKAkVTQLLEM---VQL--AHLADrypAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 488 FYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTEL-TGEE--RELATR 540
Cdd:PRK10851 175 LRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQGNIEQAgTPDQvwREPATR 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
323-488 |
4.64e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 71.07 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPdNSFAVGPINLTLQRGELVfLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL---- 398
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIgylp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 ----FSAVFTdVWLFDRLLGPGGKAADS---ALVDQwmaYLKMTHKLQLDNGRIVdlKLSKGQKKRVALLLALAEERDII 471
Cdd:cd03264 79 qefgVYPNFT-VREFLDYIAWLKGIPSKevkARVDE---VLELVNLGDRAKKKIG--SLSGGMRRRVGIAQALVGDPSIL 152
|
170
....*....|....*..
gi 491003152 472 LLDEWAADQDPHFRREF 488
Cdd:cd03264 153 IVDEPTAGLDPEERIRF 169
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
323-526 |
6.54e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 70.58 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGP----INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQ-PLAADKPEdyrk 397
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiAYVSQEPW---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 LFSAVFTDVWLFdrllgpgGKAADSalvdQWmaYLKMTHKLQLDNgrivDLK----------------LSKGQKKRVALL 461
Cdd:cd03250 77 IQNGTIRENILF-------GKPFDE----ER--YEKVIKACALEP----DLEilpdgdlteigekginLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 462 LALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQ 526
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
322-488 |
7.61e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.59 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 322 TLELRDVCFHYPDNSFaVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQP---ASGQILLDGQPLAADKPEDyRKL 398
Cdd:COG4136 1 MLSLENLTITLGGRPL-LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ-RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 fSAVFTDVWLFDRL---------LGPG-GKAADSALVDQWMAYLKMTHKLQLDNGrivdlKLSKGQKKRVALLLALAEER 468
Cdd:COG4136 79 -GILFQDDLLFPHLsvgenlafaLPPTiGRAQRRARVEQALEEAGLAGFADRDPA-----TLSGGQRARVALLRALLAEP 152
|
170 180
....*....|....*....|
gi 491003152 469 DIILLDEWAADQDPHFRREF 488
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQF 172
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-475 |
7.74e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 7.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYP-----DNsfavgpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRK 397
Cdd:COG1129 5 LEMRGISKSFGgvkalDG------VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 L-FSAVFTDVWLFD-----------RLLGPGGKAADSALVDQWMAYLKMTHkLQLDNGRIVDlKLSKGQKKRVALLLALA 465
Cdd:COG1129 79 AgIAIIHQELNLVPnlsvaeniflgREPRRGGLIDWRAMRRRARELLARLG-LDIDPDTPVG-DLSVAQQQLVEIARALS 156
|
170
....*....|
gi 491003152 466 EERDIILLDE 475
Cdd:COG1129 157 RDARVLILDE 166
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
321-531 |
9.22e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 321 QTLELRDVCFhypdnsfavgpinlTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPL----AADKPE-DY 395
Cdd:PRK11629 21 QTDVLHNVSF--------------SIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAElRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 396 RKL-----FSAVFTDVWLFDRLLGP---GGKAADSAlvdQWMAyLKMTHKLQLDN-GRIVDLKLSKGQKKRVALLLALAE 466
Cdd:PRK11629 87 QKLgfiyqFHHLLPDFTALENVAMPlliGKKKPAEI---NSRA-LEMLAAVGLEHrANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 467 ERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLT-ELT 531
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTaELS 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
323-487 |
1.40e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.31 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHY----PDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAAD-KPEDYRK 397
Cdd:PRK13649 3 INLQNVSYTYqagtPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 L---------F--SAVFTDVWLFDRLLGPG----GKAADSALVDQWMAYLKMTHKLQLDNgrivDLKLSKGQKKRVALLL 462
Cdd:PRK13649 83 IrkkvglvfqFpeSQLFEETVLKDVAFGPQnfgvSQEEAEALAREKLALVGISESLFEKN----PFELSGGQMRRVAIAG 158
|
170 180
....*....|....*....|....*
gi 491003152 463 ALAEERDIILLDEWAADQDPHFRRE 487
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKE 183
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-475 |
1.47e-13 |
|
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: 71.62 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNS---FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQP---ASGQILLDGQPLAADKPEDYR 396
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 397 KL----FSAVF-----------------TDVWlfdRLLGPGGKAADSALVDQWMAYLKMThklqlDNGRIVDL---KLSK 452
Cdd:COG0444 82 KIrgreIQMIFqdpmtslnpvmtvgdqiAEPL---RIHGGLSKAEARERAIELLERVGLP-----DPERRLDRyphELSG 153
|
170 180
....*....|....*....|...
gi 491003152 453 GQKKRVALLLALAEERDIILLDE 475
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADE 176
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
323-529 |
1.70e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.12 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED--YRKLFS 400
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHN-IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFTDVWLFDRL-------LGP----GGKAADSAlvDQWMAYL-------KMTHklqldngriVDLKLSKGQKKRVALLL 462
Cdd:PRK09493 81 MVFQQFYLFPHLtalenvmFGPlrvrGASKEEAE--KQARELLakvglaeRAHH---------YPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491003152 463 ALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQmGKTVFAISHDDHYFQH-ADRLLEMRSGQLTE 529
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKvASRLIFIDKGRIAE 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
323-527 |
1.72e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.81 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADK----------- 391
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKG-LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgllalrqqva 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 392 ----PEDYRKLFSAVFTDVWLFDRLLGPgGKAADSALVDQWMAYLKMTH----KLQLdngrivdlkLSKGQKKRVALLLA 463
Cdd:PRK13638 81 tvfqDPEQQIFYTDIDSDIAFSLRNLGV-PEAEITRRVDEALTLVDAQHfrhqPIQC---------LSHGQKKRVAIAGA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 464 LAEERDIILLDEWAADQDPHFRREFyQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQM-IAIIRRIVAQGNHVIISSHDiDLIYEISDAVYVLRQGQI 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
338-528 |
2.39e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 69.67 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEdYRKLFSAVF---TDVWlFDRllg 414
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK-FLRRIGVVFgqkTQLW-WDL--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 415 pggKAADSALVDQWM------AYLKMTHKLQ--LDNGRIVDL---KLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:cd03267 111 ---PVIDSFYLLAAIydlppaRFKKRLDELSelLDLEELLDTpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491003152 484 FRREFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLEMRSGQLT 528
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
342-475 |
3.05e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.71 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGL--YQPASGQILLDGQPLAADKPEDYRK--LFSAvFTD------VWLFD- 410
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARagIFLA-FQYpveipgVSVSNf 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491003152 411 -------RLLGPGGKAADSALVDQWMAYLKMTHKLqLDngRIVDLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:COG0396 98 lrtalnaRRGEELSAREFLKLLKEKMKELGLDEDF-LD--RYVNEGFSGGEKKRNEILQMLLLEPKLAILDE 166
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
338-527 |
3.24e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.65 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQI----LLDGQPLAADKPEDY------------RKLFSA 401
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNpyskkiknfkelRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFT--DVWLF------DRLLGP---GGKAADSALVDQWmaYLKmthKLQLDNGRI--VDLKLSKGQKKRVALLLALAEER 468
Cdd:PRK13631 121 VFQfpEYQLFkdtiekDIMFGPvalGVKKSEAKKLAKF--YLN---KMGLDDSYLerSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 469 DIILLDEWAADQDPHFRREFyQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEM-MQLILDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-475 |
4.75e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.75 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADK-------PED---YRKLfsAVFTDVW 407
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEErglYPKM--KVGEQLV 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491003152 408 LFDRLLGPGGKAADSALvDQWMAYLKMTH----KLQldngrivdlKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:COG4152 94 YLARLKGLSKAEAKRRA-DEWLERLGLGDrankKVE---------ELSKGNQQKVQLIAALLHDPELLILDE 155
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
342-475 |
5.35e-13 |
|
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: 67.94 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGL--YQPASGQILLDGQPLAADKPEDYRKLfsAVFtdvwlfdrlLG----- 414
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARL--GIF---------LAfqypp 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 415 --PGGKAADsalvdqwmaYLkmthklqldngRIVDLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03217 88 eiPGVKNAD---------FL-----------RYVNEGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
323-529 |
6.71e-13 |
|
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: 67.82 E-value: 6.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHY-PDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFD---RL-LGPGGKAADsalvDQWMAYLKMThklqlDNGrivdLKLSKGQKKRVALLLALAEERDIILLDEWA 477
Cdd:cd03369 87 IPQDPTLFSgtiRSnLDPFDEYSD----EEIYGALRVS-----EGG----LNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 478 ADQDPH--------FRREFyqqllpllqqMGKTVFAISHDDHYFQHADRLLEMRSGQLTE 529
Cdd:cd03369 154 ASIDYAtdaliqktIREEF----------TNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
338-509 |
7.77e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.48 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAAdKP--EDYRKLFSAVFTDVWLF------ 409
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG-LPghQIARMGVVRTFQHVRLFremtvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 410 DRLL-----------------GPGGKAADSALVDQWMAYLKMTHKLQLDN---GrivdlKLSKGQKKRVALLLALAEERD 469
Cdd:PRK11300 99 ENLLvaqhqqlktglfsgllkTPAFRRAESEALDRAATWLERVGLLEHANrqaG-----NLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491003152 470 IILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD 509
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
343-487 |
1.18e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.68 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 343 NLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEdyRKLFSAVFTDVWLFDRL---------L 413
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHLtvaqniglgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 414 GPGgkaadsalvdqwmayLKMTHKLQLDNGRIVDL------------KLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:PRK10771 97 NPG---------------LKLNAAQREKLHAIARQmgiedllarlpgQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
....*.
gi 491003152 482 PHFRRE 487
Cdd:PRK10771 162 PALRQE 167
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
323-488 |
1.66e-12 |
|
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: 67.42 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNsFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQ-ILLDGQPLAADKPEDYRK---L 398
Cdd:COG1119 4 LELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKrigL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 FSAVFTD-------VW------LFDRL-LGPGGKAADSALVDQWMAYLKMTHKLQLDNGRivdlkLSKGQKKRVALLLAL 464
Cdd:COG1119 83 VSPALQLrfprdetVLdvvlsgFFDSIgLYREPTDEQRERARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARAL 157
|
170 180
....*....|....*....|....
gi 491003152 465 AEERDIILLDEWAADQDPHFRREF 488
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELL 181
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-482 |
1.79e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.80 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAAdKPEDYR-KLFSAVFTDVWL------------ 408
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-LPEYKRaKYIGRVFQDPMMgtapsmtieenl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 409 -------FDRLLGPGGKAADSalvDQWMAYLKmthklQLDNG---RI---VDLkLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:COG1101 104 alayrrgKRRGLRRGLTKKRR---ELFRELLA-----TLGLGlenRLdtkVGL-LSGGQRQALSLLMATLTKPKLLLLDE 174
|
....*..
gi 491003152 476 WAADQDP 482
Cdd:COG1101 175 HTAALDP 181
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
338-519 |
2.19e-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: 66.62 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADkPEDYRKLFSAVFTD------------ 405
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE-PREVRRRIGIVFQDlsvddeltgwen 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 406 VWLFDRLLGPGGKAADSAlVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 485
Cdd:cd03265 94 LYIHARLYGVPGAERRER-IDELLDFVGLLEAAD----RLVK-TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190
....*....|....*....|....*....|....
gi 491003152 486 REFYQQLLPLLQQMGKTVFAIShddHYFQHADRL 519
Cdd:cd03265 168 AHVWEYIEKLKEEFGMTILLTT---HYMEEAEQL 198
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
342-475 |
4.37e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFsavftdvWlfdrlLG--PGGKA 419
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLL-------Y-----LGhqPGIKT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 420 ADSALVDqwmayLKMTHKLQ--LDNGRIVD------LK---------LSKGQKKRVALL-LALAeERDIILLDE 475
Cdd:PRK13538 88 ELTALEN-----LRFYQRLHgpGDDEALWEalaqvgLAgfedvpvrqLSAGQQRRVALArLWLT-RAPLWILDE 155
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
255-481 |
4.82e-12 |
|
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: 69.20 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 255 NSLGWANTAVAATYSLTLLFLRTPLLSAVGALPTLLsaqVAFNKLNTFSL----APYRADFPQP-EPHPHWQTLELRDVC 329
Cdd:TIGR00957 1215 HSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNI---VAVERLKEYSEtekeAPWQIQETAPpSGWPPRGRVEFRNYC 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 330 FHY-PDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVFTDVWL 408
Cdd:TIGR00957 1292 LRYrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVL 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 409 FD---RL-LGPGGKAADSalvDQWMAyLKMTHKLQLDNGRIVDL---------KLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:TIGR00957 1372 FSgslRMnLDPFSQYSDE---EVWWA-LELAHLKTFVSALPDKLdhecaeggeNLSVGQRQLVCLARALLRKTKILVLDE 1447
|
....*.
gi 491003152 476 WAADQD 481
Cdd:TIGR00957 1448 ATAAVD 1453
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
322-509 |
5.42e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.56 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 322 TLELRDVCFHYPDNSFAVGpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDG-VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWL---FD--------------RLLGPGgkAADSALVDQWMAylkmthklQLDNGRIVD---LKLSKGQKKRVALL 461
Cdd:PRK09536 82 VPQDTSLsfeFDvrqvvemgrtphrsRFDTWT--ETDRAAVERAME--------RTGVAQFADrpvTSLSGGERQRVLLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491003152 462 LALAEERDIILLDEWAADQDPHfRREFYQQLLPLLQQMGKTVFAISHD 509
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDIN-HQVRTLELVRRLVDDGKTAVAAIHD 198
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
324-540 |
8.79e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.68 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVF 403
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 404 TDVWLFDRLLGPG---GK----------AADSALVDQWMayLKMTHKLQL---DNGRivdlKLSKGQKKRVALLLALAEE 467
Cdd:PRK13657 416 QDAGLFNRSIEDNirvGRpdatdeemraAAERAQAHDFI--ERKPDGYDTvvgERGR----QLSGGERQRLAIARALLKD 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 468 RDIILLDEWAADQDPhfRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEERELATR 540
Cdd:PRK13657 490 PPILILDEATSALDV--ETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE-SGSFDELVAR 559
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
323-545 |
8.92e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.89 E-value: 8.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYpDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED-------- 394
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENrhvntvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 395 -YrKLFS--AVFTDVWLFDRLlgpgGKAADSALVDQWMAYLKMTHKLQLDNGRIvdLKLSKGQKKRVALLLALAEERDII 471
Cdd:PRK09452 94 sY-ALFPhmTVFENVAFGLRM----QKTPAAEITPRVMEALRMVQLEEFAQRKP--HQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491003152 472 LLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLtELTGEERELATRDA---VAR 545
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGRI-EQDGTPREIYEEPKnlfVAR 243
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
323-527 |
9.06e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYP--DNSFAV-GPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL- 398
Cdd:PRK10535 5 LELKDIRRSYPsgEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 ---FSAVFTDVWLFDRLlgpggKAADSALVDQWMAYLKMTHKLQLDNGRIVDL-----------KLSKGQKKRVALLLAL 464
Cdd:PRK10535 85 rehFGFIFQRYHLLSHL-----TAAQNVEVPAVYAGLERKQRLLRAQELLQRLgledrveyqpsQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 465 AEERDIILLDEWAADQDPHFRREFyQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQL 527
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEV-MAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
282-529 |
9.69e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.56 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 282 AVGA---LPTLLSAQVAfnklntfslAPYRADFPQPEPHPhwQTLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGN 358
Cdd:PRK11174 317 AVGAaesLVTFLETPLA---------HPQQGEKELASNDP--VTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 359 GSGKSTLAMLLTGlYQPASGQILLDGQPLAADKPEDYRKLFSAVFTDVWLF-----DRLLgPGGKAADSALVDQWMAYLK 433
Cdd:PRK11174 386 GAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPhgtlrDNVL-LGNPDASDEQLQQALENAW 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 434 MTHKL-QLDNG---RIVD--LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHfrREFYQQLLPLLQQMGKTVFAIS 507
Cdd:PRK11174 464 VSEFLpLLPQGldtPIGDqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH--SEQLVMQALNAASRRQTTLMVT 541
|
250 260
....*....|....*....|..
gi 491003152 508 HDDHYFQHADRLLEMRSGQLTE 529
Cdd:PRK11174 542 HQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-527 |
9.88e-12 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 63.61 E-value: 9.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYpdnsfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAV 402
Cdd:cd03215 5 LEVRGLSVKG-----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDvwlfDRLlgpggkaaDSALVDQWMAYlkmthklqlDNGRIVDLkLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:cd03215 80 VPE----DRK--------REGLVLDLSVA---------ENIALSSL-LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491003152 483 HFRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:cd03215 138 GAKAEIYRLIRELADA-GKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
338-475 |
1.19e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 63.92 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLfsavftdVWLFDRllgPGG 417
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENI-------LYLGHL---PGL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 418 KAADSALVD-QWMAYLKMTHKLQLDNG-RIVDLK---------LSKGQKKRVALLLALAEERDIILLDE 475
Cdd:TIGR01189 85 KPELSALENlHFWAAIHGGAQRTIEDAlAAVGLTgfedlpaaqLSAGQQRRLALARLWLSRRPLWILDE 153
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
342-529 |
1.36e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.72 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQ---PLAadkpedyrklFSAVFTD-------VWLFDR 411
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsaLLE----------LGAGFHPeltgrenIYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 412 LLGPGGKAADsALVDQ--WMAYLkmthklqldnGRIVDLKL---SKGQKKRVALLLALAEERDIILLDEWAADQDPHFR- 485
Cdd:COG1134 115 LLGLSRKEID-EKFDEivEFAEL----------GDFIDQPVktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQk 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491003152 486 ------REFYQQllpllqqmGKTVFAISHDDHYF-QHADRLLEMRSGQLTE 529
Cdd:COG1134 184 kclariRELRES--------GRTVIFVSHSMGAVrRLCDRAIWLEKGRLVM 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
323-527 |
1.44e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLA--ADKPEDYRKLFS 400
Cdd:PRK11432 7 VVLKNITKRFGSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 --AVFTDVWLFD------RLLGPgGKAADSALVDQWMAYLkmthKLQLDNGRIVDlKLSKGQKKRVALLLALAEERDIIL 472
Cdd:PRK11432 86 syALFPHMSLGEnvgyglKMLGV-PKEERKQRVKEALELV----DLAGFEDRYVD-QISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 473 LDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDD-HYFQHADRLLEMRSGQL 527
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQsEAFAVSDTVIVMNKGKI 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
338-527 |
1.80e-11 |
|
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: 63.78 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQplAADKPEDYRKLFSAVFTDVWLFDRLLG--- 414
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALIEAPGFYPNLTAren 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 415 -------PGGKAADsalVDQWMAYLKMTHklqlDNGRIVDlKLSKGQKKRVALLLALAEERDIILLDEWAADQDP---HF 484
Cdd:cd03268 93 lrllarlLGIRKKR---IDEVLDVVGLKD----SAKKKVK-GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPdgiKE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491003152 485 RREFYQQLLPLlqqmGKTVFAISHDDHYFQH-ADRLLEMRSGQL 527
Cdd:cd03268 165 LRELILSLRDQ----GITVLISSHLLSEIQKvADRIGIINKGKL 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
323-394 |
1.88e-11 |
|
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: 63.99 E-value: 1.88e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491003152 323 LELRDVCFHYpDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED 394
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE 71
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
323-509 |
2.42e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.95 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDyrklfSAV 402
Cdd:PRK11248 2 LQISHLYADYGGKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWL-----------FDRLLGPGGKAADSALVDQWMAYLKMThklQLDNGRIvdLKLSKGQKKRVALLLALAEERDII 471
Cdd:PRK11248 76 FQNEGLlpwrnvqdnvaFGLQLAGVEKMQRLEIAHQMLKKVGLE---GAEKRYI--WQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 491003152 472 LLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD 509
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
342-482 |
3.18e-11 |
|
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: 63.33 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLaADKPEDYRKLF--------SAVFTDVWLFDRLL 413
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMHKRARLgigylpqeASIFRKLTVEENIL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 414 G-----PGGKAADSALVDQWMAYLKMTHkLQLDNGrivdLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:cd03218 98 AvleirGLSKKEREEKLEELLEEFHITH-LRKSKA----SSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
321-475 |
3.64e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 321 QTLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQP--------LAADKP 392
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPtrqalqknLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 393 --EDYRKLFSAVFTDVWLFDRLLGPG----GKAADSALVDQWMAYLKMthkLQLDNGRIVDlkLSKGQKKRVALLLALAE 466
Cdd:PRK15056 85 qsEEVDWSFPVLVEDVVMMGRYGHMGwlrrAKKRDRQIVTAALARVDM---VEFRHRQIGE--LSGGQKKRVFLARAIAQ 159
|
....*....
gi 491003152 467 ERDIILLDE 475
Cdd:PRK15056 160 QGQVILLDE 168
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
338-475 |
3.70e-11 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 62.77 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL--FSA---------VFTDV 406
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLgfVSDstglydrltARENL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 407 WLFDRLLGPGGKAADSAlVDQWMAYLKMTHKLQLDNGrivdlKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03266 100 EYFAGLYGLKGDELTAR-LEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDE 162
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
338-529 |
6.69e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLA----ADKPEDYRKLFSAVFTDV------- 406
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRIRMIFQDPSTSLnprqris 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 407 WLFDRLLGPGGKAADSALVDQWMAYLKMThKLQLDNGRIVDLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRR 486
Cdd:PRK15112 108 QILDFPLRLNTDLEPEQREKQIIETLRQV-GLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491003152 487 EFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLEMRSGQLTE 529
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVE 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
342-475 |
7.27e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.74 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLfsavftdVWLFDRllgPGGKAAD 421
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL-------LYLGHA---PGIKTTL 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 422 SALVD-QWMAYLKMTHKL-----QLDNGRIVDL---KLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03231 89 SVLENlRFWHADHSDEQVeealaRVGLNGFEDRpvaQLSAGQQRRVALARLLLSGRPLWILDE 151
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
323-526 |
8.92e-11 |
|
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: 60.15 E-value: 8.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFaVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLdgqplaadkpedyrklfsav 402
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 ftdvwlfdrllgpgGKAADSALVDQwmaylkmthklqldngrivdlkLSKGQKKRVALLLALAEERDIILLDE------- 475
Cdd:cd03221 60 --------------GSTVKIGYFEQ----------------------LSGGEKMRLALAKLLLENPNLLLLDEptnhldl 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 476 ----WAADqdphFRREFYqqllpllqqmgKTVFAISHdDHYF--QHADRLLEMRSGQ 526
Cdd:cd03221 104 esieALEE----ALKEYP-----------GTVILVSH-DRYFldQVATKIIELEDGK 144
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-520 |
9.30e-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: 62.43 E-value: 9.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 345 TLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDG-------QPLAADKPEDYRKLFSavftdvwlfdrllgpgG 417
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsykpQYIKADYEGTVRDLLS----------------S 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 418 KAADSALVDQWMAylKMTHKLQLDngRIVD---LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLP 494
Cdd:cd03237 85 ITKDFYTHPYFKT--EIAKPLQIE--QILDrevPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180
....*....|....*....|....*...
gi 491003152 495 LLQQMGKTVFAISHdDHYFQH--ADRLL 520
Cdd:cd03237 161 FAENNEKTAFVVEH-DIIMIDylADRLI 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
340-528 |
1.01e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 340 GPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYqPASGQILLDGQPLA---ADKPEDYRKLFS----AVFT-DVWLFDR 411
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEawsAAELARHRAYLSqqqtPPFAmPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 412 LLGPGG--KAADSALVDQWMAYLKMTHKLqldnGRIVDlKLSKGQKKRV---ALLL----ALAEERDIILLDEWAADQDP 482
Cdd:PRK03695 92 LHQPDKtrTEAVASALNEVAEALGLDDKL----GRSVN-QLSGGEWQRVrlaAVVLqvwpDINPAGQLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491003152 483 HFRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGQLT 528
Cdd:PRK03695 167 AQQAALDRLLSELCQQ-GIAVVMSSHDlNHTLRHADRVWLLKQGKLL 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
323-509 |
1.28e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.09 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFaVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQ---PLAADKPEDYRKLF 399
Cdd:PRK11831 8 VDMRGVSFTRGNRCI-FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 400 S------AVFTDVWLFDRLLGPggKAADSALVDqwmAYLKMTHKLQLD------NGRIVDLKLSKGQKKRVALLLALAEE 467
Cdd:PRK11831 87 SmlfqsgALFTDMNVFDNVAYP--LREHTQLPA---PLLHSTVMMKLEavglrgAAKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491003152 468 RDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD 509
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
338-527 |
1.56e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 62.33 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAAD-----KPEDYRKLFSAVFT--DVWLF- 409
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikEVKRLRKEIGLVFQfpEYQLFq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 410 -----DRLLGPGGKAADSALVDQWMAYLKMTHKLQLDNGRIVDLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF 484
Cdd:PRK13645 106 etiekDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491003152 485 RREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
312-475 |
1.86e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.16 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 312 PQPEPHPHWQT----LELRDVCFHYP---------DNSF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLyQPAS 377
Cdd:COG4172 261 PRGDPRPVPPDapplLEARDLKVWFPikrglfrrtVGHVkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 378 GQILLDGQPLAADKPEDYRKLFSA---VFTDVW----------------LfdRLLGPGGKAAD-SALVDQWMAYlkmthk 437
Cdd:COG4172 340 GEIRFDGQDLDGLSRRALRPLRRRmqvVFQDPFgslsprmtvgqiiaegL--RVHGPGLSAAErRARVAEALEE------ 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491003152 438 lqldngriVDLK----------LSKGQKKRVALLLALAEERDIILLDE 475
Cdd:COG4172 412 --------VGLDpaarhrypheFSGGQRQRIAIARALILEPKLLVLDE 451
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
322-388 |
2.56e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.81 E-value: 2.56e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 322 TLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLA 388
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS 406
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-519 |
3.04e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL---- 398
Cdd:PRK13537 8 IDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 --------FSaVFTDVWLFDRLLGPGGKAAdSALVDQWMAYLKMTHKLQLDNGrivdlKLSKGQKKRVALLLALAEERDI 470
Cdd:PRK13537 87 qfdnldpdFT-VRENLLVFGRYFGLSAAAA-RALVPPLLEFAKLENKADAKVG-----ELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491003152 471 ILLDEWAADQDPHFRREFYQQLLPLLQQmGKTVFAIShddHYFQHADRL 519
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTT---HFMEEAERL 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
342-527 |
3.54e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.85 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKpEDYRKLFSAVFTDVW--LFDRL-LGPGGK 418
Cdd:PRK11247 31 LDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-EDTRLMFQDARLLPWkkVIDNVgLGLKGQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 419 AADSAL-----------VDQWMAylkmthklqldngrivdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE 487
Cdd:PRK11247 110 WRDAALqalaavgladrANEWPA------------------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491003152 488 FYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:PRK11247 172 MQDLIESLWQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
342-527 |
4.26e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQI---LLDGQPLAADKP---------------------EDYRK 397
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkekvleklviqktrfkkikkiKEIRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 LFSAVF--TDVWLF------DRLLGPggkaaDSALVDQWMAYlkmthKLQLDNGRIVDL----------KLSKGQKKRVA 459
Cdd:PRK13651 106 RVGVVFqfAEYQLFeqtiekDIIFGP-----VSMGVSKEEAK-----KRAAKYIELVGLdesylqrspfELSGGQKRRVA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 460 LLLALAEERDIILLDEWAADQDPHFRREFyQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEI-LEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFKDGKI 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
342-538 |
4.97e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDG----------QPLAADKPedyrkLFSAV---FTDVW- 407
Cdd:COG0488 17 VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqePPLDDDLT-----VLDTVldgDAELRa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 408 LFDRLLGPGGKAADSAlvDQWMAYLKMTHKLQLDNG-----RI-----------VDL-----KLSKGQKKRVALLLALAE 466
Cdd:COG0488 92 LEAELEELEAKLAEPD--EDLERLAELQEEFEALGGweaeaRAeeilsglgfpeEDLdrpvsELSGGWRRRVALARALLS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 467 ERDIILLDE-----------WAADqdphFRREFyqqllpllqqmGKTVFAISHdDHYF--QHADRLLEMRSGQLTELTG- 532
Cdd:COG0488 170 EPDLLLLDEptnhldlesieWLEE----FLKNY-----------PGTVLVVSH-DRYFldRVATRILELDRGKLTLYPGn 233
|
250
....*....|.
gi 491003152 533 -----EERELA 538
Cdd:COG0488 234 ysaylEQRAER 244
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
325-509 |
7.66e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.81 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 325 LRDVCFHYPDNSFAvGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQpLAADKPEDYRKLfSAVFT 404
Cdd:PRK11000 6 LRNVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-RMNDVPPAERGV-GMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 405 DVWLFDRL-----------LGPGGKAADSALVDQWMAYLKMTHKLqldngrivDLK---LSKGQKKRVALLLALAEERDI 470
Cdd:PRK11000 83 SYALYPHLsvaenmsfglkLAGAKKEEINQRVNQVAEVLQLAHLL--------DRKpkaLSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 491003152 471 ILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD 509
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
257-529 |
7.93e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 257 LGWANTAVAATYSLTLL-FLRTPLlsavGALPTLLS----AQVAFNKLNTFSLAPYRADFPQPEPHPHWQTLELRDVCFH 331
Cdd:PLN03232 548 LGGDLTPARAFTSLSLFaVLRSPL----NMLPNLLSqvvnANVSLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFS 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 332 YPDNSF--AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPA-SGQILLDGQplAADKPEdYRKLFSAVFTDVWL 408
Cdd:PLN03232 624 WDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGS--VAYVPQ-VSWIFNATVRENIL 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 409 FDRLLGPG--GKAADSAlvdqwmaylKMTHKLQLDNGRIVD------LKLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:PLN03232 701 FGSDFESEryWRAIDVT---------ALQHDLDLLPGRDLTeigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 491003152 481 DPHFRREFYQQLLPLLQQmGKTVFAISHDDHYFQHADRLLEMRSGQLTE 529
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
342-475 |
8.58e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKP---------EDYRKLFSAVFTDVWLFDRL 412
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeachylghRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 413 LGPGGKAADSALVDqwmaylkmthkLQLdnGRIVDLK---LSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK13539 101 LGGEELDIAAALEA-----------VGL--APLAHLPfgyLSAGQKRRVALARLLVSNRPIWILDE 153
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
342-546 |
8.86e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 59.38 E-value: 8.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKP--------EDYRKLFSAVFTDVWLF---- 409
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQLRQHVGFVFQNFNLFphrt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 410 ---DRLLGP-----GGKAADSALVDQWMAYLKMTHKLQLDNGRivdlkLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:PRK11264 102 vleNIIEGPvivkgEPKEEATARARELLAKVGLAGKETSYPRR-----LSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 482 PHFRREFYQQLLPLLQQMgKTVFAISHDDHYFQH-ADRLLEMRSGQLTElTGEERELATRDAVART 546
Cdd:PRK11264 177 PELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDvADRAIFMDQGRIVE-QGPAKALFADPQQPRT 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
333-527 |
1.18e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.36 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 333 PDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILL-DGQPLAADKPEDYRKLF-----------S 400
Cdd:PRK13643 16 PFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVRkkvgvvfqfpeS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFTDVWLFDRLLGPGGKAADSALVDQWMAYLKMTHKLQLDNGRIVDLKLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:PRK13643 96 QLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491003152 481 DPHFRREFyQQLLPLLQQMGKTVFAISH-DDHYFQHADRLLEMRSGQL 527
Cdd:PRK13643 176 DPKARIEM-MQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHI 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
342-545 |
1.73e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.84 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLA-----------------ADKPED--YRKLFS-A 401
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaskevarrigllaqnATTPGDitVQELVArG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFDRLlgpggKAADSALVDQWMAYLKMTHKLqldnGRIVDlKLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:PRK10253 106 RYPHQPLFTRW-----RKEDEEAVTKAMQATGITHLA----DQSVD-TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 482 PHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTElTGEERELATRDAVAR 545
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKIVA-QGAPKEIVTAELIER 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
310-532 |
1.87e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.08 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 310 DFPQPEPHPHwQTLELRDVCFHYPDNsfavgPI----NLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILL--- 382
Cdd:COG0488 304 RFPPPERLGK-KVLELEGLSKSYGDK-----TLlddlSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLget 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 383 --------DGQPLAADKpedyrklfsavftDVWLFDRLLGPGGKAADSalvdqwMAYLK-------MTHKLqldngriVD 447
Cdd:COG0488 378 vkigyfdqHQEELDPDK-------------TVLDELRDGAPGGTEQEV------RGYLGrflfsgdDAFKP-------VG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 448 lKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRR-------EFyqqllpllqqmGKTVFAISHdDHYF--QHADR 518
Cdd:COG0488 432 -VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEaleealdDF-----------PGTVLLVSH-DRYFldRVATR 498
|
250
....*....|....
gi 491003152 519 LLEMRSGQLTELTG 532
Cdd:COG0488 499 ILEFEDGGVREYPG 512
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
338-475 |
1.89e-09 |
|
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: 60.22 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPAS--GQILLDGQPLAADKPEDY-RKLFS------------AV 402
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAGIViihqeltlvpelSV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 403 FTDVWLFDRLLGPGGKAADSALVDQWMAYLKmthKLQLD---NGRIVdLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:TIGR02633 96 AENIFLGNEITLPGGRMAYNAMYLRAKNLLR---ELQLDadnVTRPV-GDYGGGQQQLVEIAKALNKQARLLILDE 167
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
323-398 |
2.05e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 59.32 E-value: 2.05e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 323 LELRDVC--FHYPDNSF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL 398
Cdd:COG1135 2 IELENLSktFPTKGGPVtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
323-544 |
2.35e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCfhypdNSFAVGP----INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL 398
Cdd:PRK15439 12 LCARSIS-----KQYSGVEvlkgIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 -FSAVFTDVWLF-------DRLLGPGGKAADSAlvdqwmaylKMTHKLQLDNGRIvDLKLSKG-----QKKRVALLLALA 465
Cdd:PRK15439 87 gIYLVPQEPLLFpnlsvkeNILFGLPKRQASMQ---------KMKQLLAALGCQL-DLDSSAGslevaDRQIVEILRGLM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 466 EERDIILLDEWAADQDPHFRREFYQQLLPLLQQmGKTVFAISHDDH-YFQHADRLLEMRSGQLTeLTGEERELATRDAVA 544
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPeIRQLADRISVMRDGTIA-LSGKTADLSTDDIIQ 234
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-519 |
2.60e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.07 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAAdKPEDYRKLFSAV 402
Cdd:PRK13536 42 IDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 ---------FT---DVWLFDRLLGPGGKAADsALVDQWMAYLKMTHKLqldNGRIVDLklSKGQKKRVALLLALAEERDI 470
Cdd:PRK13536 120 pqfdnldleFTvreNLLVFGRYFGMSTREIE-AVIPSLLEFARLESKA---DARVSDL--SGGMKRRLTLARALINDPQL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491003152 471 ILLDEWAADQDPHFRREFYQQLLPLLQQmGKTVFAIShddHYFQHADRL 519
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTT---HFMEEAERL 238
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
338-527 |
2.64e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.10 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTL----AMLLTGLYQPASGQILLDGQPLAADK-PEDYRKLFS---AVFTDVWLF 409
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITGDKSAGSHIELLGRTVQREGRlARDIRKSRAntgYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 410 DRL-------LGPGGKAADSALVDQWMAYLKMTHKLQ---------LDNGRIVdlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK09984 99 NRLsvlenvlIGALGSTPFWRTCFSWFTREQKQRALQaltrvgmvhFAHQRVS--TLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 474 DEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHV 231
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
330-539 |
3.06e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.34 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 330 FHYPDNSF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVFTDVWL 408
Cdd:PRK10789 321 FTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 409 F-DRLLGP---GGKAADSALVDQwMAYLKMTHK--LQLDNGRIVD-----LKLSKGQKKRVALLLALAEERDIILLDEWA 477
Cdd:PRK10789 401 FsDTVANNialGRPDATQQEIEH-VARLASVHDdiLRLPQGYDTEvgergVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491003152 478 ADQDPhfRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTElTGEERELAT 539
Cdd:PRK10789 480 SAVDG--RTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQ-RGNHDQLAQ 538
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
324-475 |
3.16e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 58.66 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 324 ELRDVCFHYPDNSF---AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRK--- 397
Cdd:PRK11153 3 ELKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 ----------LFSA--VFTDVWLFDRLLGpggkaADSALVDQWMAYLkmthkLQLdngriVDL---------KLSKGQKK 456
Cdd:PRK11153 83 qigmifqhfnLLSSrtVFDNVALPLELAG-----TPKAEIKARVTEL-----LEL-----VGLsdkadrypaQLSGGQKQ 147
|
170
....*....|....*....
gi 491003152 457 RVALLLALAEERDIILLDE 475
Cdd:PRK11153 148 RVAIARALASNPKVLLCDE 166
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
338-537 |
5.14e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.66 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQI-------LLDGQPLAADKPEDYRKLFSAVFTDVWLFD 410
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 411 R--LLGPGGKAADSALVDQwMAYLKMTHKLQ---LDNGRIVDL------KLSKGQKKRVALLLALAEERDIILLDEWAAD 479
Cdd:TIGR03269 379 HrtVLDNLTEAIGLELPDE-LARMKAVITLKmvgFDEEKAEEIldkypdELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 480 QDPHFRREFYQQLLPLLQQMGKTVFAISHD-DHYFQHADRLLEMRSGQLTElTGEEREL 537
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKIVK-IGDPEEI 515
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
342-529 |
5.65e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.71 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA----VFTDVWLFDRL----- 412
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhvgfVFQSFMLIPTLnalen 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 413 -----LGPGGKAADSAlvDQWMAYLKmthklQLDNGRIVD---LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF 484
Cdd:PRK10584 109 velpaLLRGESSRQSR--NGAKALLE-----QLGLGKRLDhlpAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491003152 485 RREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTE 529
Cdd:PRK10584 182 GDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
322-475 |
5.66e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 58.68 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 322 TLELRDVCFHY-PDN------SFAVGPinltlqrGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED 394
Cdd:COG5265 357 EVRFENVSFGYdPERpilkgvSFEVPA-------GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 395 YRKLFSAVFTDVWLFDRLLG-------PGG------KAADSALVDQWMAylkmthklQLDNG-------RivDLKLSKGQ 454
Cdd:COG5265 430 LRAAIGIVPQDTVLFNDTIAyniaygrPDAseeeveAAARAAQIHDFIE--------SLPDGydtrvgeR--GLKLSGGE 499
|
170 180
....*....|....*....|.
gi 491003152 455 KKRVALLLALAEERDIILLDE 475
Cdd:COG5265 500 KQRVAIARTLLKNPPILIFDE 520
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
323-475 |
6.43e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFaVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLF--- 399
Cdd:PRK13540 2 LDVIELDFDYHDQPL-LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCfvg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491003152 400 --SAVFTDVWLFDRLLGPGGKAADSALVDQWMAYLKMTHKLQLDNGRivdlkLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK13540 81 hrSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
338-389 |
1.15e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 1.15e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYqPA---SGQILLDGQPLAA 389
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQA 73
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-398 |
1.18e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.34 E-value: 1.18e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL 398
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
338-475 |
1.63e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL-FSAVFTDVWLFDRL---- 412
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELtvle 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 413 ---LG--PGGKAADSALVDqWMAYLKMTHKLQLDNGRIVDL-----KLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK09700 100 nlyIGrhLTKKVCGVNIID-WREMRVRAAMMLLRVGLKVDLdekvaNLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
323-510 |
1.78e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSfavgpiNLTLQRGELVFLIGGNGSGKSTLAMLLTGLY--QPASGQI------------LLDGQPLA 388
Cdd:COG2401 36 VELRVVERYVLRDL------NLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVdvpdnqfgreasLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 389 ADKPEDYRKLFSAVFTDVWLFDRllgpggkaadsalvdqwmaylKMTHklqldngrivdlkLSKGQKKRVALLLALAEER 468
Cdd:COG2401 110 GDFKDAVELLNAVGLSDAVLWLR---------------------RFKE-------------LSTGQKFRFRLALLLAERP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491003152 469 DIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDD 510
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
342-527 |
2.39e-08 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 54.09 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGL--YQPASGQILLDGQPLaadKPEDYRKLFSAVFTDVWLFDRLlgpggka 419
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTL------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 420 adsaLVDQwmaYLKMTHKLQldngrivdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPhFRREFYQQLLPLLQQM 499
Cdd:cd03213 98 ----TVRE---TLMFAAKLR---------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS-SSALQVMSLLRRLADT 160
|
170 180 190
....*....|....*....|....*....|
gi 491003152 500 GKTVFAISHDDHY--FQHADRLLEMRSGQL 527
Cdd:cd03213 161 GRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
342-388 |
3.46e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 3.46e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLA 388
Cdd:PRK11288 23 ISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR 69
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
15-173 |
5.24e-08 |
|
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: 54.36 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 15 FISVIALSLLSAALGIgliaFINLRLMTVVDTSLAVLPEFLGLLL------LLMVVTLGSQLALTTLGHHFVFRLRGEFI 88
Cdd:cd18551 1 LILALLLSLLGTAASL----AQPLLVKNLIDALSAGGSSGGLLALlvalflLQAVLSALSSYLLGRTGERVVLDLRRRLW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 89 KRILDTQIEKVEKIGSASLLAGLTSD---IRN-ITIAfvrLPELVQGIILTFGSAAYLAWLSGKMMMVTALWMALTIWGG 164
Cdd:cd18551 77 RRLLRLPVSFFDRRRSGDLVSRVTNDttlLRElITSG---LPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLII 153
|
....*....
gi 491003152 165 FVLVARVYR 173
Cdd:cd18551 154 LPLGRRIRK 162
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
339-482 |
5.77e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.74 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 339 VGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLA-------ADKPEDYRKLFSAVFTDVWLFDR 411
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplharARRGIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 412 LLG--------PGGKAADSAlvDQWMAYLKMTHkLQLDNGRivdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:PRK10895 99 LMAvlqirddlSAEQREDRA--NELMEEFHIEH-LRDSMGQ----SLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
341-543 |
6.36e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 341 PINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADK------------PEDY------------- 395
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSprdairagimlcPEDRkaegiipvhsvad 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 396 ------RKLFSAVFtdvWLFDRllgpgGKAADSAlvDQWMAYLkmthKLQLDNGRIVDLKLSKGQKKRVALLLALAEERD 469
Cdd:PRK11288 351 ninisaRRHHLRAG---CLINN-----RWEAENA--DRFIRSL----NIKTPSREQLIMNLSGGNQQKAILGRWLSEDMK 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 470 IILLDEWAADQDPHFRREFYQQLLPLLQQmGKTVFAISHD-DHYFQHADRLLEMRSGqltELTGE-ERELATRDAV 543
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDlPEVLGVADRIVVMREG---RIAGElAREQATERQA 488
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
338-394 |
7.09e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.02 E-value: 7.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED 394
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD 323
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
342-511 |
7.22e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRkLFSAVFTDVWLFDRlLGPGGKAAD 421
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY-LDTTLPLTVNRFLR-LRPGTKKED 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 422 --SALVDQWMAYLkMTHKLQldngrivdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQM 499
Cdd:PRK09544 101 ilPALKRVQAGHL-IDAPMQ---------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRREL 170
|
170
....*....|..
gi 491003152 500 GKTVFAISHDDH 511
Cdd:PRK09544 171 DCAVLMVSHDLH 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
322-482 |
8.05e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.48 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 322 TLELRDVCFHYPDNSfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPL---AADKPEDYRKL 398
Cdd:PRK11124 2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 ---FSAVFT--DVW--------LFD---RLLGPGGKAAdsalVDQWMAYLKmthKLQLDNgrIVD---LKLSKGQKKRVA 459
Cdd:PRK11124 81 rrnVGMVFQqyNLWphltvqqnLIEapcRVLGLSKDQA----LARAEKLLE---RLRLKP--YADrfpLHLSGGQQQRVA 151
|
170 180
....*....|....*....|...
gi 491003152 460 LLLALAEERDIILLDEWAADQDP 482
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDP 174
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-475 |
8.83e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.94 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEdYRKLFSAVF---TDVWlFD---- 410
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKE-FARRIGVVFgqrSQLW-WDlpai 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 411 ---RLLgpggKA---ADSALVDQWMAYLkmTHKLQLDngrivDL------KLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:COG4586 115 dsfRLL----KAiyrIPDAEYKKRLDEL--VELLDLG-----ELldtpvrQLSLGQRMRCELAAALLHRPKILFLDE 180
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
338-528 |
1.09e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.57 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED---YRKLFSAVFTD-VWLFDR-- 411
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhHLLMDRtv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 412 -------LLGPGGKAAD-----SALVDQWMAylkmthklqLDNGRIVDLKLSKGQKKRVALLLALAEERDIILLDEWAAD 479
Cdd:PRK10908 97 ydnvaipLIIAGASGDDirrrvSAALDKVGL---------LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491003152 480 QDPHFrREFYQQLLPLLQQMGKTVFAISHDDHYFQHAD-RLLEMRSGQLT 528
Cdd:PRK10908 168 LDDAL-SEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
345-475 |
1.19e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 345 TLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLD------GQPLAADKPEDYRKLFSAV---FTDVWLFDRLLGP 415
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPDYDGTVEDLLRSItddLGSSYYKSEIIKP 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 416 ggkaadsalvdqwmaylkmthkLQLDngRIVDLK---LSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK13409 441 ----------------------LQLE--RLLDKNvkdLSGGELQRVAIAACLSRDADLYLLDE 479
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
226-544 |
1.34e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 226 IRADTFHLSAVNWSNIMMLGAIGLVFWMANS---LGWANTAVAATYSLTLLFLrtplLSAVGALPTLLS-----AQVAFN 297
Cdd:PLN03232 1123 IRFTLANTSSNRWLTIRLETLGGVMIWLTATfavLRNGNAENQAGFASTMGLL----LSYTLNITTLLSgvlrqASKAEN 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 298 KLNTFSLAPYRADFPQPEPH-----------PHWQTLELRDVCFHYPDN--------SFAVGPinltlqrGELVFLIGGN 358
Cdd:PLN03232 1199 SLNSVERVGNYIDLPSEATAiiennrpvsgwPSRGSIKFEDVHLRYRPGlppvlhglSFFVSP-------SEKVGVVGRT 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 359 GSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAVFTDVWLFDRL----LGPGGKAADSALvdqWMAYLKM 434
Cdd:PLN03232 1272 GAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTvrfnIDPFSEHNDADL---WEALERA 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 435 THKLQLDNGRI-VDLKLSK-------GQKKRVALLLALAEERDIILLDEWAADQDphFRREFYQQLLPLLQQMGKTVFAI 506
Cdd:PLN03232 1349 HIKDVIDRNPFgLDAEVSEggenfsvGQRQLLSLARALLRRSKILVLDEATASVD--VRTDSLIQRTIREEFKSCTMLVI 1426
|
330 340 350
....*....|....*....|....*....|....*...
gi 491003152 507 SHDDHYFQHADRLLEMRSGQLTELTGEErELATRDAVA 544
Cdd:PLN03232 1427 AHRLNTIIDCDKILVLSSGQVLEYDSPQ-ELLSRDTSA 1463
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
342-515 |
2.29e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 52.28 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILL-----------DGQPLAADKPE--DYRKLFSAVFT--DV 406
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdkDGQLKVADKNQlrLLRTRLTMVFQhfNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 407 WLFD-----------RLLGPGGKAADSALVdQWMAYLKMTHKLQLDngriVDLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK10619 104 WSHMtvlenvmeapiQVLGLSKQEARERAV-KYLAKVGIDERAQGK----YPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491003152 476 WAADQDPHFRREFYQQLLPLLQQmGKTVFAISHDDHYFQH 515
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARH 217
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
321-389 |
2.84e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 2.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 321 QTLELRDVCFhYPDNSFaVGPINLTLQRGELVFLIGGNGSGKS-----TLAMLLTGLYQPAsGQILLDGQPLAA 389
Cdd:PRK10418 3 QQIELRNIAL-QAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQTA-GRVLLDGKPVAP 73
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
233-529 |
3.07e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 233 LSAVNwsnIMMLGAIGLV-----FWMANSLGWANTAVAATYSLTLL-FLRTPLLsavgALPTLLS----AQVAFNKLNTF 302
Cdd:PLN03130 522 LSAFN---SFILNSIPVLvtvvsFGVFTLLGGDLTPARAFTSLSLFaVLRFPLF----MLPNLITqavnANVSLKRLEEL 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 303 SLAPYRADFPQPEPHPHWQTLELRDVCFHYpdNSFAVGP----INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPAS- 377
Cdd:PLN03130 595 LLAEERVLLPNPPLEPGLPAISIKNGYFSW--DSKAERPtlsnINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSd 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 378 GQILLDGQplAADKPEdYRKLFSAVFTDVWLFdrllgpgGKAADSALVDQWMAYLKMTHKLQLDNGRivDL--------K 449
Cdd:PLN03130 673 ASVVIRGT--VAYVPQ-VSWIFNATVRDNILF-------GSPFDPERYERAIDVTALQHDLDLLPGG--DLteigergvN 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 450 LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQmGKTVFAISHDDHYFQHADRLLEMRSGQLTE 529
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELR-GKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
345-520 |
4.01e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 345 TLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLD------GQPLAADKP---EDY-RKLFSAVFTDVWLFDRLLG 414
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQYISPDYDgtvEEFlRSANTDDFGSSYYKTEIIK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 415 PggkaadsalvdqwmaylkmthkLQLDngRIVDLK---LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQ 491
Cdd:COG1245 442 P----------------------LGLE--KLLDKNvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
|
170 180 190
....*....|....*....|....*....|.
gi 491003152 492 LLPLLQQMGKTVFAISHdDHYFQH--ADRLL 520
Cdd:COG1245 498 IRRFAENRGKTAMVVDH-DIYLIDyiSDRLM 527
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
322-385 |
4.74e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 4.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 322 TLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQ 385
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR 66
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
342-475 |
5.90e-07 |
|
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: 50.73 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPA---SGQILLDGQPLaadKPEDYRKLFSAVFTDvwlfDRLLgPGGK 418
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPR---KPDQFQKCVAYVRQD----DILL-PGLT 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 419 AADSALvdqWMAYLKMTHK---------------LQLDNGRIVDLK---LSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03234 98 VRETLT---YTAILRLPRKssdairkkrvedvllRDLALTRIGGNLvkgISGGERRRVSIAVQLLWDPKVLILDE 169
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
340-482 |
6.43e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 340 GPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKpedyRKLFSAVFTDVwlfdrllgPGGKA 419
Cdd:PRK13543 28 GPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRFMAYLGHL--------PGLKA 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 420 ADSALVD-QWMAYLKMTHKLQLDNG--RIVDL---------KLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:PRK13543 96 DLSTLENlHFLCGLHGRRAKQMPGSalAIVGLagyedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
333-527 |
7.17e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.32 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 333 PDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL-----FSAVFTDVW 407
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLgmcpqHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 408 LFDRLLGPG---GKAADSALVDQwMAYLKMTHKLQLDNGRIVDlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF 484
Cdd:TIGR01257 1020 VAEHILFYAqlkGRSWEEAQLEM-EAMLEDTGLHHKRNEEAQD--LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491003152 485 RREFYQQLLPLLQqmGKTVFAISHD-DHYFQHADRLLEMRSGQL 527
Cdd:TIGR01257 1097 RRSIWDLLLKYRS--GRTIIMSTHHmDEADLLGDRIAIISQGRL 1138
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
338-402 |
7.38e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 7.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAV 402
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKI 94
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
342-475 |
7.63e-07 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 51.25 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVF-------------LIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPL---AAD---KPEdyRKLFSAV 402
Cdd:COG4148 5 VDFRLRRGGFTLdvdftlpgrgvtaLFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsARGiflPPH--RRRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 403 FTDVWLFDRL---------LGPGGKAADSALVDQWMAYLKMTHKLQldngRIVDlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:COG4148 83 FQEARLFPHLsvrgnllygRKRAPRAERRISFDEVVELLGIGHLLD----RRPA-TLSGGERQRVAIGRALLSSPRLLLM 157
|
..
gi 491003152 474 DE 475
Cdd:COG4148 158 DE 159
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
342-525 |
7.67e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.02 E-value: 7.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQIL----LDGQPLAADKPEDYRKLFSAVFTDVWLFDRLL---- 413
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLNATVeeni 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 414 ---GPGGKAADSALVDQWMAYLKMTHKLQLDNGRIVD--LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREF 488
Cdd:cd03290 100 tfgSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGErgINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 491003152 489 YQQLLPLLQQMGK-TVFAISHDDHYFQHADRLLEMRSG 525
Cdd:cd03290 180 MQEGILKFLQDDKrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
323-543 |
8.64e-07 |
|
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: 50.68 E-value: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAV-GPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:cd03288 20 IKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VFTDVWLFD---RL-LGPGGKAADSALvdqW----MAYLK-MTHKLQLDNGRIVD---LKLSKGQKKRVALLLALAEERD 469
Cdd:cd03288 100 ILQDPILFSgsiRFnLDPECKCTDDRL---WealeIAQLKnMVKSLPGGLDAVVTeggENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 470 IILLDEWAADQDphFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLTELTGEERELATRDAV 543
Cdd:cd03288 177 ILIMDEATASID--MATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGV 248
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-547 |
1.07e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADK------------PEDYRKlfSAVFTDV--- 406
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrlarglvylPEDRQS--SGLYLDApla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 407 W-----LFDRL---LGPggkAADSALVDQWMAYL--KMTHKLQLDNGrivdlkLSKGQKKRVALLLALAEERDIILLDEW 476
Cdd:PRK15439 360 WnvcalTHNRRgfwIKP---ARENAVLERYRRALniKFNHAEQAART------LSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 477 AADQDPHFRREFYQQLLPLLQQmGKTVFAISHDDHYFQH-ADRLLEMRSGQLT-ELTGEERELatrDAVARTA 547
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQmADRVLVMHQGEISgALTGAAINV---DTIMRLA 499
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
323-398 |
2.38e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 50.07 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRD--VCFHYPDNSF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQP----ASGQILLDGQPLAADKPEDY 395
Cdd:COG4172 7 LSVEDlsVAFGQGGGTVeAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSEREL 86
|
...
gi 491003152 396 RKL 398
Cdd:COG4172 87 RRI 89
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-530 |
2.45e-06 |
|
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: 47.37 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 348 RGELVFLIGGNGSGKSTLAMLLTGLYQPASGQ-ILLDGQPLAADKPEdyrklfsavftdvwlfdrllgpggkaadsalvd 426
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLD--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 427 qwmaylkmthklQLDNGRIVDLKLSKGQKKRVALLLALAEER--DIILLDEWAADQDPHFRRE-----FYQQLLPLLQQM 499
Cdd:smart00382 48 ------------QLLLIIVGGKKASGSGELRLRLALALARKLkpDVLILDEITSLLDAEQEALlllleELRLLLLLKSEK 115
|
170 180 190
....*....|....*....|....*....|.
gi 491003152 500 GKTVFAISHDDHYFQhaDRLLEMRSGQLTEL 530
Cdd:smart00382 116 NLTVILTTNDEKDLG--PALLRRRFDRRIVL 144
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
7-253 |
2.49e-06 |
|
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: 49.47 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 7 VWRQYRWPFISVIALSLLSAALGIGLIAFINLRLMTVvdtslavlpeflglllllmvvtlgsqlalttLGHHFVFRLRGE 86
Cdd:cd07346 29 VIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAAR-------------------------------LGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 87 FIKRILDTQIEKVEKIGSASLLAGLTSDIRNITIAFVR-LPELVQGIILTFGSAAYLAWLSGKMMMVTALWMALTIWGGF 165
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 166 VLVARVYRHMATLRETEDKLYHDYQTVLEGRKEL-TLNRERAEYvfnQLYLPDAREYRHHIIRADTfhLSAVNWSNIMML 244
Cdd:cd07346 158 YFRRRIRKASREVRESLAELSAFLQESLSGIRVVkAFAAEEREI---ERFREANRDLRDANLRAAR--LSALFSPLIGLL 232
|
250
....*....|.
gi 491003152 245 GAIG--LVFWM 253
Cdd:cd07346 233 TALGtaLVLLY 243
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
323-482 |
2.50e-06 |
|
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: 49.08 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAV-GPINLTLQRGELVFLIGGNGSGKSTL-AMLLTGLYqpASGQILLDGQPLAADKPEDYRKLFS 400
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 401 AVFTDVWLFD----RLLGPGGKAADSAL------------VDQWMAYLkmthKLQLDNGRIVdlkLSKGQKKRVALLLAL 464
Cdd:cd03289 81 VIPQKVFIFSgtfrKNLDPYGKWSDEEIwkvaeevglksvIEQFPGQL----DFVLVDGGCV---LSHGHKQLMCLARSV 153
|
170
....*....|....*...
gi 491003152 465 AEERDIILLDEWAADQDP 482
Cdd:cd03289 154 LSKAKILLLDEPSAHLDP 171
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
342-398 |
4.79e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 4.79e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTG--LYQPASGQILLDGQPLAADKPEDYRKL 398
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL 84
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
377-543 |
5.38e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 377 SGQILLDGQPLAADKPEDYRKLFSAVFTDVWLF-------------DRLLGPGGKAADSALVDQWMAYLKMTHKLQLDN- 442
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFnmsiyenikfgkeDATREDVKRACKFAAIDEFIESLPNKYDTNVGPy 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 443 GRivdlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQHADRLLEM 522
Cdd:PTZ00265 1356 GK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVF 1431
|
170 180
....*....|....*....|....*.
gi 491003152 523 ----RSGQLTELTGEERE-LATRDAV 543
Cdd:PTZ00265 1432 nnpdRTGSFVQAHGTHEElLSVQDGV 1457
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
316-540 |
7.22e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 316 PHP-HWQTLELRDVCFHYPDN--------SFAVGPinltlqrGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQP 386
Cdd:PTZ00243 1301 PHPvQAGSLVFEGVQMRYREGlplvlrgvSFRIAP-------REKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 387 LAADKPEDYRKLFSAVFTDVWLFD---RL-LGPGGKAAdSALVDQWMAYLKMTHKLQLDNGRIVDLKL------SKGQKK 456
Cdd:PTZ00243 1374 IGAYGLRELRRQFSMIPQDPVLFDgtvRQnVDPFLEAS-SAEVWAALELVGLRERVASESEGIDSRVLeggsnySVGQRQ 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 457 RVALLLALAEE-RDIILLDEWAADQDPHFRREFYQQLLPLLQQMgkTVFAISHDDHYFQHADRLLEMRSGQLTELtGEER 535
Cdd:PTZ00243 1453 LMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQYDKIIVMDHGAVAEM-GSPR 1529
|
....*
gi 491003152 536 ELATR 540
Cdd:PTZ00243 1530 ELVMN 1534
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
322-475 |
7.35e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 322 TLELRDVCFHYPDNSFAVGPiNLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSA 401
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 402 VF----TDvwlfdrLLGPG----GKAA---------DSALVDQWMAYLKMTHKLqldNGRIVdlKLSKGQKKRVALLLAL 464
Cdd:PRK10938 82 EWqrnnTD------MLSPGeddtGRTTaeiiqdevkDPARCEQLAQQFGITALL---DRRFK--YLSTGETRKTLLCQAL 150
|
170
....*....|.
gi 491003152 465 AEERDIILLDE 475
Cdd:PRK10938 151 MSEPDLLILDE 161
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
323-475 |
7.90e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.18 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLA------------AD 390
Cdd:PRK11614 6 LSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqtakimreavAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 391 KPEDyRKLFSAVftdvwLFDRLLGPGGKAADSalvDQWMAYLKMTHKL--QLDNGRIVDL-KLSKGQKKRVALLLALAEE 467
Cdd:PRK11614 85 VPEG-RRVFSRM-----TVEENLAMGGFFAER---DQFQERIKWVYELfpRLHERRIQRAgTMSGGEQQMLAIGRALMSQ 155
|
....*...
gi 491003152 468 RDIILLDE 475
Cdd:PRK11614 156 PRLLLLDE 163
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
342-386 |
8.77e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 8.77e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYqPA---SGQILLDGQP 386
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEV 66
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
323-399 |
8.77e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 45.99 E-value: 8.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 323 LELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQIlldgqplaaDKPEDYRKLF 399
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEGEDLLF 68
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
342-533 |
9.82e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQplAADKPEDYRKLFSAVFTDVWLFD-----RLlgpg 416
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--IAYVPQQAWIMNATVRGNILFFDeedaaRL---- 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 417 gkaADSALVDQWMAYLKmthklQLDNGRIVDL-----KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFrREFYQQ 491
Cdd:PTZ00243 753 ---ADAVRVSQLEADLA-----QLGGGLETEIgekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV-GERVVE 823
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491003152 492 LLPLLQQMGKTVFAISHDDHYFQHADRLLEMRSGQLtELTGE 533
Cdd:PTZ00243 824 ECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRV-EFSGS 864
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
324-380 |
1.14e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 1.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 491003152 324 ELRDVCFHYPDNSFaVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQI 380
Cdd:PRK11147 321 EMENVNYQIDGKQL-VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
342-541 |
1.16e-05 |
|
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: 48.40 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQplAADKPEdyrklfSAVFTDVWLFDRLLGpgGKAAD 421
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--VAYVPQ------QAWIQNDSLRENILF--GKALN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 422 SALVDQWMAYLKMTHKLQL----DNGRIVD--LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPL 495
Cdd:TIGR00957 727 EKYYQQVLEACALLPDLEIlpsgDRTEIGEkgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGP 806
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491003152 496 LQQM-GKTVFAISHDDHYFQHADRLLEMRSGQLTELtGEERELATRD 541
Cdd:TIGR00957 807 EGVLkNKTRILVTHGISYLPQVDVIIVMSGGKISEM-GSYQELLQRD 852
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
342-482 |
1.26e-05 |
|
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: 47.87 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGL--YQPASGQIL----------------LDGQPLAA-------------- 389
Cdd:TIGR03269 19 ISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVcggtlepeevdfwn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 390 -DKPEDYR----------KLFsAVFTDVWLFDRLLG-------PGGKAADSA--LVDQWMAYLKMTHklqldngriVDLK 449
Cdd:TIGR03269 99 lSDKLRRRirkriaimlqRTF-ALYGDDTVLDNVLEaleeigyEGKEAVGRAvdLIEMVQLSHRITH---------IARD 168
|
170 180 190
....*....|....*....|....*....|...
gi 491003152 450 LSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDP 201
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
307-380 |
1.28e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 1.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 307 YRADFPQPEPHPHWQTLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQI 380
Cdd:PLN03073 493 YKFEFPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
323-475 |
1.32e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGpINLTLQRGELVFLIGGNGSGKSTLAMLLTGL--YQPASGQILLDGQPLAADKPED------ 394
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRG-LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 395 -----YRKLFSAVFTDVWLFD--------RLLGPGGKAADSALVDQWMAYLKMTHKLQLdngRIVDLKLSKGQKKRVALL 461
Cdd:PRK09580 81 fmafqYPVEIPGVSNQFFLQTalnavrsyRGQEPLDRFDFQDLMEEKIALLKMPEDLLT---RSVNVGFSGGEKKRNDIL 157
|
170
....*....|....
gi 491003152 462 LALAEERDIILLDE 475
Cdd:PRK09580 158 QMAVLEPELCILDE 171
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
342-474 |
1.49e-05 |
|
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: 46.77 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGqplaadkpedyRKLFSAVFTdvWLFDrllgpgGKAAD 421
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------RISFSSQFS--WIMP------GTIKE 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 422 SALV----DQWMaYLKMTHKLQL----------DNGRIVD--LKLSKGQKKRVALLLALAEERDIILLD 474
Cdd:cd03291 117 NIIFgvsyDEYR-YKSVVKACQLeeditkfpekDNTVLGEggITLSGGQRARISLARAVYKDADLYLLD 184
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
325-387 |
1.64e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 1.64e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491003152 325 LRDVCFHYPDNSfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPL 387
Cdd:PRK10982 1 MSNISKSFPGVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI 62
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
323-475 |
1.69e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.57 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLY--QP---ASGQILLDGQPLAADK--PEDY 395
Cdd:COG1117 12 IEVRNLNVYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGEDIYDPDvdVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 396 RKLFSAVF--------TdvwLFD------RLLGPGGKAADSALVDQwmaYLKMT-------HKLQlDNGrivdLKLSKGQ 454
Cdd:COG1117 91 RRRVGMVFqkpnpfpkS---IYDnvayglRLHGIKSKSELDEIVEE---SLRKAalwdevkDRLK-KSA----LGLSGGQ 159
|
170 180
....*....|....*....|.
gi 491003152 455 KKRVALLLALAEERDIILLDE 475
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDE 180
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
342-526 |
1.87e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLamLLTGLYqpASGQILLdgqplaadkpEDYRKLFSAvfTDVWLFDRLlgpggkaad 421
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARL----------ISFLPKFSR--NKLIFIDQL--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 422 SALVDQWMAYLKMTHKLQldngrivdlKLSKGQKKRVALL--LALAEERDIILLDEWAADQDPHFRREFyQQLLPLLQQM 499
Cdd:cd03238 69 QFLIDVGLGYLTLGQKLS---------TLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQL-LEVIKGLIDL 138
|
170 180
....*....|....*....|....*..
gi 491003152 500 GKTVFAISHDDHYFQHADRLLEMRSGQ 526
Cdd:cd03238 139 GNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
311-394 |
2.10e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 311 FPQpEPHPHWQT-LELRDVCFHYPDNSFA--VGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPAS-GQILLDGQP 386
Cdd:PRK13549 248 YPR-EPHTIGEViLEVRNLTAWDPVNPHIkrVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKP 326
|
....*...
gi 491003152 387 LAADKPED 394
Cdd:PRK13549 327 VKIRNPQQ 334
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
330-384 |
2.47e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 2.47e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 491003152 330 FHYpdnsfAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDG 384
Cdd:PRK13545 36 YHY-----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
334-387 |
2.67e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 2.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 491003152 334 DNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYqPASGQILLDGQPL 387
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPL 349
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
322-399 |
3.14e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.72 E-value: 3.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491003152 322 TLELRDVCFHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLdgqplaadkPEDYRKLF 399
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLF 430
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
349-394 |
5.24e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 5.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 491003152 349 GELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED 394
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS 75
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
338-390 |
5.68e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 5.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 491003152 338 AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAAD 390
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAG 333
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-540 |
6.78e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.52 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSFAVGpINLTLQRGELVFLIGGNGSGKSTLAML---LTGLYQPA--SGQILLDGQPLAADKPEDYRK 397
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDG-VNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 398 LFSAVFT------DVWLFDRL-LGP------GGKAADSALVDQWM--AYLKMTHKLQLDNGRIvdlKLSKGQKKRVALLL 462
Cdd:PRK14247 83 RVQMVFQipnpipNLSIFENVaLGLklnrlvKSKKELQERVRWALekAQLWDEVKDRLDAPAG---KLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 463 ALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMgkTVFAIShddHYFQHADRLLE----MRSGQLTElTGEERELA 538
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVT---HFPQQAARISDyvafLYKGQIVE-WGPTREVF 233
|
..
gi 491003152 539 TR 540
Cdd:PRK14247 234 TN 235
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
330-385 |
7.22e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 7.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 330 FHYPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQ 385
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE 86
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
323-543 |
1.03e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.70 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHY------------PDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAAD 390
Cdd:PRK15079 9 LEVADLKVHFdikdgkqwfwqpPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 391 KPEDY---RKLFSAVFTDvwlfdrllgPGGKAADSALVDQWMAYLKMTHKLQLDNGRIVD------LKL----------- 450
Cdd:PRK15079 89 KDDEWravRSDIQMIFQD---------PLASLNPRMTIGEIIAEPLRTYHPKLSRQEVKDrvkammLKVgllpnlinryp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 451 ---SKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLEMrsgq 526
Cdd:PRK15079 160 hefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVM---- 235
|
250
....*....|....*..
gi 491003152 527 lteLTGEERELATRDAV 543
Cdd:PRK15079 236 ---YLGHAVELGTYDEV 249
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
226-538 |
1.04e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 226 IRADTFHLSAVNWSNIMMLGAIGLVFW-------MANSLGWANTAVAATYSLTLLFLR--TPLLSAVgalptLLSAQVAF 296
Cdd:PLN03130 1126 IRFTLVNMSSNRWLAIRLETLGGLMIWltasfavMQNGRAENQAAFASTMGLLLSYALniTSLLTAV-----LRLASLAE 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 297 NKLNTFSLAPYRADFPQP--------EPHPHWQT---LELRDVCFHY-PDNSFAVGPINLTLQRGELVFLIGGNGSGKST 364
Cdd:PLN03130 1201 NSLNAVERVGTYIDLPSEaplviennRPPPGWPSsgsIKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSS 1280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 365 LAMLLTGLYQPASGQILLDGQPLAADKPEDYRKLFSAV------FTDVWLFDrlLGPGGKAADsalVDQW----MAYLKM 434
Cdd:PLN03130 1281 MLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIpqapvlFSGTVRFN--LDPFNEHND---ADLWesleRAHLKD 1355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 435 THKlqlDNGRIVDLKLSK-------GQKKRVALLLALAEERDIILLDEWAADQD--------PHFRREFYQQllpllqqm 499
Cdd:PLN03130 1356 VIR---RNSLGLDAEVSEagenfsvGQRQLLSLARALLRRSKILVLDEATAAVDvrtdaliqKTIREEFKSC-------- 1424
|
330 340 350
....*....|....*....|....*....|....*....
gi 491003152 500 gkTVFAISHDDHYFQHADRLLEMRSGQLTELTGEERELA 538
Cdd:PLN03130 1425 --TMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
342-475 |
1.05e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.48 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPL--AADK---PEDYRKLfSAVFTDVWLFD--RLLG 414
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKGiclPPEKRRI-GYVFQDARLFPhyKVRG 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491003152 415 P---GGKAADSALVDQWMAYLKMTHKLqldnGRIvDLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK11144 96 NlryGMAKSMVAQFDKIVALLGIEPLL----DRY-PGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
319-380 |
1.08e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 1.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491003152 319 HWQTLELRDVCFHYPDNSFAVGpINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQI 380
Cdd:PRK15064 316 HRNALEVENLTKGFDNGPLFKN-LNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
306-382 |
1.29e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 1.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 306 PYRADFPQPE--PHPhwqTLELRDVCFHYPDNSFaVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILL 382
Cdd:PRK10636 297 PFHFSFRAPEslPNP---LLKMEKVSAGYGDRII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
342-474 |
1.41e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.90 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGqplaadkpedyRKLFSAVFTdvWLFdrllgPG----- 416
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------RISFSPQTS--WIM-----PGtikdn 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 417 ---GKAAD---------SALVDQWMAYLKMTHKLQLDNGRIVdlkLSKGQKKRVALLLALAEERDIILLD 474
Cdd:TIGR01271 507 iifGLSYDeyrytsvikACQLEEDIALFPEKDKTVLGEGGIT---LSGGQRARISLARAVYKDADLYLLD 573
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
342-380 |
1.71e-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: 44.16 E-value: 1.71e-04
10 20 30
....*....|....*....|....*....|....*....
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQI 380
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
343-380 |
2.81e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 2.81e-04
10 20 30
....*....|....*....|....*....|....*...
gi 491003152 343 NLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQI 380
Cdd:PRK11819 344 SFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
342-482 |
6.12e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 42.98 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTlamLLTGLYQPAS--GQILLDGQPLAADKPEDYRKLFSAVFTDVWL----FDRLLGP 415
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKST---LLSALLRLLSteGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIfsgtFRKNLDP 1314
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 416 GGKAADS------------ALVDQWMAYLkmthKLQLDNGRIVdlkLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:TIGR01271 1315 YEQWSDEeiwkvaeevglkSVIEQFPDKL----DFVLVDGGYV---LSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
318-383 |
1.25e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 1.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491003152 318 PHWQTLELRDVCFHYpDNSFAV---GPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLD 383
Cdd:PTZ00265 378 KDIKKIQFKNVRFHY-DTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN 445
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
311-387 |
1.36e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 311 FPQPEPHPHWQTLELRDVCFHYPDNS--FAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTG-LY-QPASGQILLDGQP 386
Cdd:NF040905 246 YPERTPKIGEVVFEVKNWTVYHPLHPerKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYgRNISGTVFKDGKE 325
|
.
gi 491003152 387 L 387
Cdd:NF040905 326 V 326
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
315-394 |
1.55e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 41.35 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 315 EPHPHWQT-LELRDVCFHYPDNSFA--VGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPA-SGQILLDGQPLAAD 390
Cdd:TIGR02633 249 EPHEIGDViLEARNLTCWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIR 328
|
....
gi 491003152 391 KPED 394
Cdd:TIGR02633 329 NPAQ 332
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
79-185 |
2.44e-03 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) 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: 349992 [Multi-domain] Cd Length: 292 Bit Score: 40.07 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 79 FVFRLRGEFIKRILDTQIEKVEKIGSASLLAGLTSDIRNI---TIAFVRLpeLVQGIILTFGSAAYLAWLSGKMMMVTAL 155
Cdd:cd18548 70 FGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVqnfVMMLLRM--LVRAPIMLIGAIIMAFRINPKLALILLV 147
|
90 100 110
....*....|....*....|....*....|
gi 491003152 156 WMALTIWGGFVLVARVYRHMATLRETEDKL 185
Cdd:cd18548 148 AIPILALVVFLIMKKAIPLFKKVQKKLDRL 177
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
318-537 |
2.49e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.61 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 318 PHWQTLELRDV--------CFHYPDNSF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLA 388
Cdd:PRK10261 2 PHSDELDARDVlavenlniAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 389 ADKPE--DYRKLFSAVFTDVWLFDRL---------LGP----GGKAADSALVDQWMAYLK--MTHKLQLDNGRIVDLK-- 449
Cdd:PRK10261 82 RRSRQviELSEQSAAQMRHVRGADMAmifqepmtsLNPvftvGEQIAESIRLHQGASREEamVEAKRMLDQVRIPEAQti 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 450 -------LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQQLLPLLQQMGKTVFAISHDDHYFQH-ADRLLE 521
Cdd:PRK10261 162 lsryphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLV 241
|
250
....*....|....*.
gi 491003152 522 MRSGQLTElTGEEREL 537
Cdd:PRK10261 242 MYQGEAVE-TGSVEQI 256
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
323-372 |
3.67e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 39.71 E-value: 3.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 491003152 323 LELRD--VCFHYPD-NSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGL 372
Cdd:PRK09473 13 LDVKDlrVTFSTPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL 65
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
354-383 |
3.76e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 3.76e-03
10 20 30
....*....|....*....|....*....|
gi 491003152 354 LIGGNGSGKSTLAMLLTGLYQPASGQILLD 383
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
332-509 |
3.84e-03 |
|
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: 38.71 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 332 YPDNSFAVGPINLTLQ-----RGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAAdKPEDyrklfsavftdv 406
Cdd:cd03222 3 YPDCVKRYGVFFLLVElgvvkEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY-KPQY------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 407 wlfdrllgpggkaadsalvdqwmaylkmthklqldngrivdLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRR 486
Cdd:cd03222 70 -----------------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRL 108
|
170 180
....*....|....*....|...
gi 491003152 487 EFYQQLLPLLQQMGKTVFAISHD 509
Cdd:cd03222 109 NAARAIRRLSEEGKKTALVVEHD 131
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
332-513 |
4.00e-03 |
|
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: 39.92 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 332 YPDNSFAVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQ--------------------------ILLDGQ 385
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgikvgylpqepqldptktvreNVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 386 PLAADKPEDYRKLFSAVFTDVWLFDRLLGPGGKAADsaLVDQWMAY-----LKMT-HKLQLDNGRIVDLKLSKGQKKRVA 459
Cdd:TIGR03719 94 AEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQE--IIDAADAWdldsqLEIAmDALRCPPWDADVTKLSGGERRRVA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491003152 460 LLLALAEERDIILLDEWAADQDP-------HFRREFyqqllpllqqmGKTVFAISHdDHYF 513
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLDAesvawleRHLQEY-----------PGTVVAVTH-DRYF 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
342-394 |
4.18e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.99 E-value: 4.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPED 394
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD 323
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
323-489 |
4.39e-03 |
|
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: 40.00 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 323 LELRDVCFHYPDNSF-AVGPINLTLQRGELVFLIGGNGSGKSTLAMLLTGLYQPASGQILLDGQPLAADKPEDYRKL--- 398
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgyc 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491003152 399 --FSAV------FTDVWLFDRLLGPGGKAADSalVDQWMAylkMTHKLQLDNGRIVDlKLSKGQKKRVALLLALAEERDI 470
Cdd:TIGR01257 2018 pqFDAIddlltgREHLYLYARLRGVPAEEIEK--VANWSI---QSLGLSLYADRLAG-TYSGGNKRKLSTAIALIGCPPL 2091
|
170
....*....|....*....
gi 491003152 471 ILLDEWAADQDPHFRREFY 489
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLW 2110
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
342-389 |
7.58e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 38.27 E-value: 7.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 491003152 342 INLTLQRGELVFLIGGNGSGKSTLAMLLTG-LYQPA-------SGQILLDGQPLAA 389
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAA 75
|
|
| |
