|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-566 |
0e+00 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 1071.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 20 MQLLLLVWRQYRWPFIAVMALSLASAALGIGLIAFINVRLIEMTDTSLSVLPEFLGLLLLLMAVTLGSQLALTTLGHHFV 99
Cdd:PRK10522 1 MELLRLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 100 FRLRSEFIKRILDTQIERVEQLGSASLLAGLTSDVRAITIAFVRLPELVQGIILTFGSAAYLAWLSSKMLAVTALWIVIT 179
Cdd:PRK10522 81 YRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITIAFVRLPELVQGIILTLGSAAYLAWLSPKMLLVTAIWMAVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 180 IWGGFMLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKELTLNRERAEHIFNHLYIPDAREYRHHIIRADTFHLSAVNWSN 259
Cdd:PRK10522 161 IWGGFVLVARVYKHMATLRETEDKLYNDYQTVLEGRKELTLNRERAEYVFENEYEPDAQEYRHHIIRADTFHLSAVNWSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 260 IMMLGAIGLVFWMANGLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLKKFDLAPFKAEFPRPQAFPNW 339
Cdd:PRK10522 241 IMMLGAIGLVFYMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKLALAPYKAEFPRPQAFPDW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 340 QTLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFS 419
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFTDVWLFDRLLGPEGQQANPALVEKWLAQLQMSHKLELQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQ 499
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 500 DPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKLSELTGEDRDAASRDAVARTA 566
Cdd:PRK10522 481 DPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAVARTA 547
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-558 |
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: 748.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 20 MQLLLLVWRQYRWPFIAVMALSLASAALGIGLIAFINVRLIEMTDTSLSVLPEFLGLLLLLMAVTLGSQLALTTLGHHFV 99
Cdd:COG4615 1 MNLLRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 100 FRLRSEFIKRILDTQIERVEQLGSASLLAGLTSDVRAITIAFVRLPELVQGIILTFGSAAYLAWLSSKMLAVTALWIVIT 179
Cdd:COG4615 81 ARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 180 IWGGFMLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKELTLNRERAEHIFNHLYIPDAREYRHHIIRADTFHLSAVNWSN 259
Cdd:COG4615 161 VAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAFFDEDLQPTAERYRDLRIRADTIFALANNWGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 260 IMMLGAIGLVFWMANGLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLKKFDLA-----PFKAEFPRPQ 334
Cdd:COG4615 241 LLFFALIGLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELAlaaaePAAADAAAPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 335 AFPNWQTLELRNVKFHYQ----DSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEK 410
Cdd:COG4615 321 APADFQTLELRGVTYRYPgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 411 PEDYRKLFSAVFTDVWLFDRLLGPEGqQANPALVEKWLAQLQMSHKLELQDGKILNLKLSKGQKKRVALLLALAEERDII 490
Cdd:COG4615 401 REAYRQLFSAVFSDFHLFDRLLGLDG-EADPARARELLERLELDHKVSVEDGRFSTTDLSQGQRKRLALLVALLEDRPIL 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 491 LLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKLSELTGEDRDAAS 558
Cdd:COG4615 480 VFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
16-546 |
4.47e-110 |
|
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: 340.01 E-value: 4.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 16 RIACMQLLLLVWRQYRWPFIAVMALSLASAALGIGLIAFINVRLIEMTDTSLSVLPEFLGLLLLLMAVTLGSQLALTTLG 95
Cdd:TIGR01194 2 KAAIGEILALLRSPFPAITAFSIALGLAGGLAIIALLASINNAIHEENFLGQGSLFSFGGLCLLALLFRIGADIFPAYAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 96 HHFVFRLRSEFIKRILDTQIERVEQLGSASLLAGLTSDVRAITIAFVRLPELVQGIILTFGSAAYLAWLSSKMLAVTALW 175
Cdd:TIGR01194 82 MHIIANLRIALCEKILGAPIEEIDRRGAHNLIPLLTHDIDQINAFLFIFPPIAIALAIFFFCIAYLAYLSVPMFAITISA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 176 IVITIWGGFMLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKELTLNRERAEHiFNHLYIPDA--REYRHHIIRADTFHLs 253
Cdd:TIGR01194 162 IIIGTAAQLLAFMGGFKFFHAARDEEDAFNEHTHAIAFGAKELKIHGIRRLS-FAHGAIQESanNIADLHIIEILIFIA- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 254 AVNWSNIMMLGAIGLVFWMANGLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLKKFDlapFKAEFPRP 333
Cdd:TIGR01194 240 AENFGQLLFFLLIGCALFAAAMFASIDAAAISAFVLALLYIKGPLEMLVSALPILAQAQIACQRLADFG---ERFNEPEP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 334 QAF-------------PNWQTLELRNVKFHYQD----SAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQS 396
Cdd:TIGR01194 317 ELElsdadnvlllahdKSVDSIELKDVHMNPKApegsEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 397 GEILLDGKALSAEKPEDYRKLFSAVFTDVWLFDRLLGP-EGQQANPALVEKWLAQLQMSHKLELQDGKI-LNLKLSKGQK 474
Cdd:TIGR01194 397 GEILLDGAAVSADSRDDYRDLFSAIFADFHLFDDLIGPdEGEHASLDNAQQYLQRLEIADKVKIEDGGFsTTTALSTGQQ 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 475 KRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:TIGR01194 477 KRLALICAWLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDDQYFELADQIIKLAAGCI 548
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-548 |
1.04e-54 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 194.61 E-value: 1.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 20 MQLLLLVWRQYRWPFIAVMALSLASAALGIgLIAFINVRLIE--MTDTSLSVLPEFLGLLLLLMAV----TLGSQLALTT 93
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLEL-LLPLLLGRIIDalLAGGDLSALLLLLLLLLGLALLrallSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 94 LGHHFVFRLRSEFIKRILDTQIERVEQLGSASLLAGLTSDVRAITIAFVR-LPELVQGIILTFGSAAYLAWLSSKMLAVT 172
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLFVIDWRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 173 ALWIVITIWGGFMLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKEL-TLNRERAE-HIFNHLyipdAREYRHHIIRAdtF 250
Cdd:COG1132 168 LLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVkAFGREERElERFREA----NEELRRANLRA--A 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 251 HLSAVNWSNIMMLGAIG--LVFWMANGL---GWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLKKF-DLA 324
Cdd:COG1132 242 RLSALFFPLMELLGNLGlaLVLLVGGLLvlsGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELlDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 325 PFKAEFPRPQAFPNWQ-TLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG 403
Cdd:COG1132 322 PEIPDPPGAVPLPPVRgEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 404 KALSAEKPEDYRKLFSAVFTDVWLFDR------LLGPEGqqANPALVEKWLAQLQMSHKLE-LQDGkiLN-------LKL 469
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGtireniRYGRPD--ATDEEVEEAAKAAQAHEFIEaLPDG--YDtvvgergVNL 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 470 SKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
342-545 |
1.01e-46 |
|
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: 161.40 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDS-AFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFDRLLGPegqqanpalvekwlaqlqmshklelqdgkilNLkLSKGQKKRVALLLALAEERDIILLDEWAADQD 500
Cdd:cd03228 81 VPQDPFLFSGTIRE-------------------------------NI-LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2131440126 501 PHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRDGK 545
Cdd:cd03228 129 PETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
342-546 |
8.75e-42 |
|
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: 150.18 E-value: 8.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRK----- 416
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 417 -------LFSA-VFTDVwlfdrLLGPEGQQANPA----LVEKWLAQLQMSHKLElqdgKILNlKLSKGQKKRVALLLALA 484
Cdd:COG1122 81 fqnpddqLFAPtVEEDV-----AFGPENLGLPREeireRVEEALELVGLEHLAD----RPPH-ELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 485 EERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDlDLVAELADRVIVLDDGRI 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
343-545 |
1.61e-41 |
|
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: 148.77 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHYQDSAFSVG-PVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAV 421
Cdd:cd03225 1 ELKNLSFSYPDGARPALdDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 F--TDVWLF------DRLLGPEGQQANPALVEK----WLAQLQMSHkleLQDGKILNlkLSKGQKKRVALLLALAEERDI 489
Cdd:cd03225 81 FqnPDDQFFgptveeEVAFGLENLGLPEEEIEErveeALELVGLEG---LRDRSPFT--LSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 490 ILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHYFI-HADRLLEMRDGK 545
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
23-548 |
5.11e-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: 147.61 E-value: 5.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 23 LLLVWRQYRWPFIAVMALSLASAALGIGLIA----FInvrliemtdTSLSVLPEFLGLLLLLMAVTLgsqLALT------ 92
Cdd:COG4987 6 LLRLLRPHRGRLLLGVLLGLLTLLAGIGLLAlsgwLI---------AAAALAPPILNLFVPIVGVRA---FAIGrtvfry 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 93 ---TLGHHFVFR----LRSEFIKRILDTQIERVEQLGSASLLAGLTSDVRAITIAFVRL--PELVqGIILTFGSAAYLAW 163
Cdd:COG4987 74 lerLVSHDATLRlladLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVllPLLV-ALLVILAAVAFLAF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 164 LSSKMLAVTALWIVITIWGGFMLVSRVYKHMAV-LRETEDKLYNDYQTVLEGRKELTLN------RERAEHIFNHLyipD 236
Cdd:COG4987 153 FSPALALVLALGLLLAGLLLPLLAARLGRRAGRrLAAARAALRARLTDLLQGAAELAAYgaldraLARLDAAEARL---A 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 237 AREYRHHIIRAdtFHLSAVNWsnIMMLGAIGLVFWMANGLGWADTNVAATYSLTLLFLR-----TPLLSAVGALPTLLSA 311
Cdd:COG4987 230 AAQRRLARLSA--LAQALLQL--AAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALAlfealAPLPAAAQHLGRVRAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 312 QVAFNKLkkFDLAPFKAEFPRPQAFPNWQTLELRNVKFHYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTG 390
Cdd:COG4987 306 ARRLNEL--LDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 391 LYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFD-------RLLGPEgqqANPALVEKWLAQLQMSHKLE-LQDG 462
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDttlrenlRLARPD---ATDEELWAALERVGLGDWLAaLPDG 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 463 kiLNL-------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHA 535
Cdd:COG4987 461 --LDTwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM 536
|
570
....*....|...
gi 2131440126 536 DRLLEMRDGKLSE 548
Cdd:COG4987 537 DRILVLEDGRIVE 549
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
342-546 |
8.66e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.71 E-value: 8.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAV 421
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTD-VWL-------FDRLLGPEGQQANPALVEKWLAQLQMSHKLELQDGKilnlKLSKGQKKRVALLLALAEERDIILLD 493
Cdd:COG4619 80 PQEpALWggtvrdnLPFPFQLRERKFDRERALELLERLGLPPDILDKPVE----RLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 494 EWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYF-IHADRLLEMRDGKL 546
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
342-546 |
3.37e-36 |
|
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: 136.02 E-value: 3.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSA-FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG-KALSAEKPEDYRKLFS 419
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFT-------------DVwLFdrllGPEGQQANPA----LVEKWLAQLQMSHKLELQDgkilnLKLSKGQKKRVALLLA 482
Cdd:TIGR04520 81 MVFQnpdnqfvgatvedDV-AF----GLENLGVPREemrkRVDEALKLVGMEDFRDREP-----HLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 483 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKI 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
23-548 |
5.44e-36 |
|
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: 141.82 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 23 LLLVWRQYRWPFIAVMALSLASAALGIG---LIAFINVRLIEMTDTSLSVLPEFLGlllllMAVTLGSQLALTTLGHHFV 99
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAqawLLASLLAGLIIGGAPLSALLPLLGL-----LLAVLLLRALLAWLRERAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 100 FR--------LRSEFIKRILDTQIERVEQLGSASLLAGLTSDVRAITIAFVR-LPELVQGII---LTFGSAAYLAWLSSK 167
Cdd:COG4988 83 FRaaarvkrrLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARyLPQLFLAALvplLILVAVFPLDWLSGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 168 MLAVTALWIVITIWG-GFMLVSRVYKHMAVLRetedKLYNDYQTVLEGRKELTL-NRERAEHifNHLYIpDAREYRHHII 245
Cdd:COG4988 163 ILLVTAPLIPLFMILvGKGAAKASRRQWRALA----RLSGHFLDRLRGLTTLKLfGRAKAEA--ERIAE-ASEDFRKRTM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 246 R----AdtFHLSAVnwSNIMMLGAIGLVFWMAnGLGWADTNVAATYSLTLLFLR----TPL--LSA---VGAlptllSAQ 312
Cdd:COG4988 236 KvlrvA--FLSSAV--LEFFASLSIALVAVYI-GFRLLGGSLTLFAALFVLLLApeffLPLrdLGSfyhARA-----NGI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 313 VAFNKLKKFDLAPFKAEFPRPQAFPNWQ--TLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTG 390
Cdd:COG4988 306 AAAEKIFALLDAPEPAAPAGTAPLPAAGppSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 391 LYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFD-------RLLGPEgqqANPALVEKWLAQLQMSHKLE-LQDG 462
Cdd:COG4988 386 FLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAgtirenlRLGRPD---ASDEELEAALEAAGLDEFVAaLPDG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 463 kiLN-------LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHA 535
Cdd:COG4988 463 --LDtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA 538
|
570
....*....|...
gi 2131440126 536 DRLLEMRDGKLSE 548
Cdd:COG4988 539 DRILVLDDGRIVE 551
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
342-546 |
9.48e-36 |
|
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: 131.75 E-value: 9.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALsAEKPEDYRKLFSAV 421
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRLLGPEgqqanpalvekwlaqlqmshklelqdgkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 501
Cdd:cd03230 79 PEEPSLYENLTVRE------------------------------NLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2131440126 502 HFRREFYQVLLPLMQEmGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03230 129 ESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
28-548 |
2.27e-35 |
|
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: 141.12 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 28 RQYRWPFIAVMALSLASAALGIGLIAFINV---RLIEMTDTS-LSVLpeflgllLLLMAVTLGSQLALTTLGHHFV---- 99
Cdd:COG2274 152 RRYRRLLLQVLLASLLINLLALATPLFTQVvidRVLPNQDLStLWVL-------AIGLLLALLFEGLLRLLRSYLLlrlg 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 100 ----FRLRSEFIKRILDTQIERVEQLGSASLLAGLtSDVRAITIAFV-RLPELVQGIILTFGSAAYLAWLSSKMLAVTAL 174
Cdd:COG2274 225 qridLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgSLLTALLDLLFVLIFLIVLFFYSPPLALVVLL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 175 WIVITIWGGFMLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKEL-TLNRE-RAEHIFNHLYipdaREYRHHIIRADTFHL 252
Cdd:COG2274 304 LIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIkALGAEsRFRRRWENLL----AKYLNARFKLRRLSN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 253 SAVNWSN-IMMLGAIGLVFW-----MANGLgwadtNVA---ATYSLTLLFLrTPLLSAVGALPTLLSAQVAFNKLKK-FD 322
Cdd:COG2274 380 LLSTLSGlLQQLATVALLWLgaylvIDGQL-----TLGqliAFNILSGRFL-APVAQLIGLLQRFQDAKIALERLDDiLD 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 323 LAPFKAEFPRPQAFPNWQ-TLELRNVKFHY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL 400
Cdd:COG2274 454 LPPEREEGRSKLSLPRLKgDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 401 LDGKALSAEKPEDYRKLFSAVFTDVWLFDR------LLGpeGQQANPALVEK--WLAQL-----QMSHKLELQ---DGKi 464
Cdd:COG2274 534 IDGIDLRQIDPASLRRQIGVVLQDVFLFSGtireniTLG--DPDATDEEIIEaaRLAGLhdfieALPMGYDTVvgeGGS- 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 465 lnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRDG 544
Cdd:COG2274 611 ---NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKG 685
|
....
gi 2131440126 545 KLSE 548
Cdd:COG2274 686 RIVE 689
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
343-545 |
3.48e-33 |
|
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: 123.89 E-value: 3.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHYQDSaFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVF 422
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 423 tdvwlfdrllgpegQqanpalvekwlaqlqmshklelqdgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 502
Cdd:cd00267 80 --------------Q-------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2131440126 503 FRREFYQVLLPLMQEmGKTIFAISHDDHYFIHA-DRLLEMRDGK 545
Cdd:cd00267 115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
343-546 |
4.49e-33 |
|
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: 124.47 E-value: 4.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHYQDSaFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFsavf 422
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 423 tdvwlfdrllgpegqqanpALVEKWLAQLQMSHKLElqdgKILNlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 502
Cdd:cd03214 76 -------------------AYVPQALELLGLAHLAD----RPFN-ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2131440126 503 FRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDlNLAARYADRVILLKDGRI 176
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
343-546 |
9.67e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.64 E-value: 9.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAV 421
Cdd:PRK13632 9 KVENVSFSYpNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FT------------DvwlfDRLLGPEGQQANP----ALVEKWLAQLQMSHKLELQDgkilnLKLSKGQKKRVALLLALAE 485
Cdd:PRK13632 89 FQnpdnqfigatveD----DIAFGLENKKVPPkkmkDIIDDLAKKVGMEDYLDKEP-----QNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 486 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
360-497 |
1.65e-31 |
|
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: 119.29 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 360 PVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFDRLLGPE---- 435
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVREnlrl 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 436 -------GQQANPALVEKWLAQLQMSHKLELQDGKILNlKLSKGQKKRVALLLALAEERDIILLDEWAA 497
Cdd:pfam00005 83 glllkglSKREKDARAEEALEKLGLGDLADRPVGERPG-TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
342-546 |
3.05e-31 |
|
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: 120.67 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSV----GpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPED---- 413
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkG-VSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 414 YRKLFSAVFTDVWLFDRL-----------LGPEGQQANPALVEKWLAQLQMSHKLELQDGKilnlkLSKGQKKRVALLLA 482
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDLtalenvelpllLAGVPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 483 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
342-546 |
8.94e-31 |
|
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: 120.10 E-value: 8.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAV 421
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRLLGPEgqqaNPALV---EKWLAQLQMSHKLELQdgKILNL-----------KLSKGQKKRVALLLALAEER 487
Cdd:cd03295 81 IQQIGLFPHMTVEE----NIALVpklLKWPKEKIRERADELL--ALVGLdpaefadryphELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 488 DIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEI 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
342-546 |
8.94e-31 |
|
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: 120.35 E-value: 8.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSaFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAlSAEKPEDYRKLFSAV 421
Cdd:COG4555 2 IEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED-VRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRL-----------LGPEGQQANPALVEKWLAQLQMShklELQDGKIlnLKLSKGQKKRVALLLALAEERDII 490
Cdd:COG4555 80 PDERGLYDRLtvreniryfaeLYGLFDEELKKRIEELIELLGLE---EFLDRRV--GELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 491 LLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDdhyfIH-----ADRLLEMRDGKL 546
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHI----MQevealCDRVVILHKGKV 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
342-548 |
3.74e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 117.84 E-value: 3.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL- 417
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 -----FsaVFTDVWLFDRL-----------LGPEGQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLL 481
Cdd:COG1136 85 rrhigF--VFQFFNLLPELtalenvalpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----QLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 482 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
342-546 |
1.07e-29 |
|
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: 116.83 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL---- 417
Cdd:cd03261 1 IELRGLTKSFGGRTVLKG-VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 -----FSAVFTD--------VWLFDRLLGPEGQQAnpALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALA 484
Cdd:cd03261 80 gmlfqSGALFDSltvfenvaFPLREHTRLSEEEIR--EIVLEKLEAVGLRGAEDLYPA-----ELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 485 EERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDH--YFIhADRLLEMRDGKL 546
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDtaFAI-ADRIAVLYDGKI 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
342-546 |
1.83e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 116.32 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEkPEDYRKLFSAV 421
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD-PAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRLLGPE-----------GQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDII 490
Cdd:COG1131 79 PQEPALYPDLTVREnlrffarlyglPRKEARERIDELLELFGLTDAADRKVG-----TLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 491 LLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD----DHYfihADRLLEMRDGKL 546
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYleeaERL---CDRVAIIDKGRI 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
342-546 |
2.52e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 116.30 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAV 421
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 ---------FT--DVWLFDRL--LGPEGQ--QANPALVEKWLAQLQMSHkleLQDgKILNlKLSKGQKKRVALLLALAEE 486
Cdd:COG1120 81 pqeppapfgLTvrELVALGRYphLGLFGRpsAEDREAVEEALERTGLEH---LAD-RPVD-ELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 487 RDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDlNLAARYADRLVLLKDGRI 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-548 |
2.62e-28 |
|
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: 118.47 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFS----VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---ALSAEKPEDY 414
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 415 RKLFSAVFTDV----------------WLfdRLLGPEGQQANPALVEKWLAQLQMSHKL------ElqdgkilnlkLSKG 472
Cdd:COG1123 341 RRRVQMVFQDPysslnprmtvgdiiaePL--RLHGLLSRAERRERVAELLERVGLPPDLadryphE----------LSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 473 QKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD----DHYfihADRLLEMRDGKLSE 548
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlavvRYI---ADRVAVMYDGRIVE 485
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-548 |
4.47e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.57 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFT-------------DVwlfdrLLGPEGQQ-ANPALVEK--W-LAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLAL 483
Cdd:PRK13635 86 VFQnpdnqfvgatvqdDV-----AFGLENIGvPREEMVERvdQaLRQVGMEDFLNREPH-----RLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 484 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
94-528 |
4.63e-28 |
|
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: 117.85 E-value: 4.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 94 LGHHFVFR----LRSEFIKRILDTQIERVEQLGSASLLAGLTSDVRAITIAFVR--LPELVQG--IILTFGSAAYLAWLS 165
Cdd:TIGR02868 76 VGHDAALRslgaLRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRviVPAGVALvvGAAAVAAIAVLSVPA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 166 SKMLAVTALWIVITIWGGFMLVSRvyKHMAVLRETEDKLYNDYQTVLEGRKELTLNRERAEhifnhlYIPDAREYRHHII 245
Cdd:TIGR02868 156 ALILAAGLLLAGFVAPLVSLRAAR--AAEQALARLRGELAAQLTDALDGAAELVASGALPA------ALAQVEEADRELT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 246 RADTFHLSAVNWSNIMMLGAIGLVFWM---ANGLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSA--QVAFNKLKK 320
Cdd:TIGR02868 228 RAERRAAAATALGAALTLLAAGLAVLGalwAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQltRVRAAAERI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 321 FDLAPFK-----AEFPRPQAFPNWQ-TLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQP 394
Cdd:TIGR02868 308 VEVLDAAgpvaeGSAPAAGAVGLGKpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 395 QSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFD-------RLLGPE--GQQANPAL----VEKWLAQLQMSHKLELQD 461
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDttvrenlRLARPDatDEELWAALervgLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 462 GKILnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHD 528
Cdd:TIGR02868 468 GGAR---LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
343-548 |
6.54e-28 |
|
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: 111.55 E-value: 6.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVF 422
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 423 TDVWLFDR------LLGpeGQQANPALVEKWLAQLQMSHKLE-LQDGKILNLK-----LSKGQKKRVALLLALAEERDII 490
Cdd:cd03254 84 QDTFLFSGtimeniRLG--RPNATDEEVIEAAKEAGAHDFIMkLPNGYDTVLGenggnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 491 LLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
342-548 |
1.49e-27 |
|
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: 110.67 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFS---VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---ALSAEKPEDYR 415
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 416 KLFSAVFTDV-----------WLFDRLLgpEGQQANPALVEKWLAQLQMSHKLELqDGKILNLK---LSKGQKKRVALLL 481
Cdd:cd03257 82 KEIQMVFQDPmsslnprmtigEQIAEPL--RIHGKLSKKEARKEAVLLLLVGVGL-PEEVLNRYpheLSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 482 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDH--YFIhADRLLEMRDGKLSE 548
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGvvAKI-ADRVAVMYAGKIVE 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
343-546 |
1.84e-27 |
|
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: 109.65 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEK--------PED- 413
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErrksigyvMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 414 YRKLFSA-VFTDVWLFDRLLGPEGQQANPALVEKWLAQLQMSHKLELqdgkilnlklSKGQKKRVALLLALAEERDIILL 492
Cdd:cd03226 81 DYQLFTDsVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSL----------SGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2131440126 493 DEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHyFIH--ADRLLEMRDGKL 546
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYE-FLAkvCDRVLLLANGAI 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
342-545 |
2.57e-27 |
|
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: 108.43 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDsAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAE--KPEDYRKLFS 419
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFTDVWLFdrllgpegqqanpalvekwlaqlqmSHKLELQDgkiLNLKLSKGQKKRVALLLALAEERDIILLDEWAADQ 499
Cdd:cd03229 80 MVFQDFALF-------------------------PHLTVLEN---IALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2131440126 500 DPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRDGK 545
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
342-559 |
4.82e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.59 E-value: 4.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSA--FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFS 419
Cdd:PRK13650 5 IEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFTDvwlfdrllgPEGQQANpALVE---------KWLAQLQM----SHKLEL---QDGKILN-LKLSKGQKKRVALLLA 482
Cdd:PRK13650 85 MVFQN---------PDNQFVG-ATVEddvafglenKGIPHEEMkervNEALELvgmQDFKEREpARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 483 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKLsELTGEDRDAASR 559
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV-ESTSTPRELFSR 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
342-546 |
1.14e-26 |
|
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: 107.61 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEdyRKLFSAV 421
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLF-------------DRLLGPEGQQAnpALVEKWLAQLQMSHKLELqdgkiLNLKLSKGQKKRVALLLALAEERD 488
Cdd:cd03259 78 FQDYALFphltvaeniafglKLRGVPKAEIR--ARVRELLELVGLEGLLNR-----YPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 489 IILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD--DHYFIhADRLLEMRDGKL 546
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDqeEALAL-ADRIAVMNEGRI 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
361-546 |
1.44e-26 |
|
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: 108.88 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL----FSAVFTDVWLFDRL----- 431
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPHRtvlen 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 432 --LGPEGQQANPAL-VEKWLAQLQM------SHKLELQdgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 502
Cdd:cd03294 123 vaFGLEVQGVPRAErEERAAEALELvglegwEHKYPDE--------LSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2131440126 503 FRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDlDEALRLGDRIAIMKDGRL 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-548 |
4.03e-26 |
|
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: 111.92 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSA-FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGKALSAEKPEDYRKL 417
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 FSAVFTDVW--------LFDRLLGPEGQQANP----ALVEKWLAQLQMSHKLELQDGKilnlkLSKGQKKRVALLLALAE 485
Cdd:COG1123 85 IGMVFQDPMtqlnpvtvGDQIAEALENLGLSRaearARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 486 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKLSE 548
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIVE 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
342-541 |
8.87e-26 |
|
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: 105.25 E-value: 8.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEdyrklF 418
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 419 SAVFTDVWLFDRL-------LGPEGQQANPA----LVEKWLAQLQMS---HKLELQdgkilnlkLSKGQKKRVALLLALA 484
Cdd:cd03293 76 GYVFQQDALLPWLtvldnvaLGLELQGVPKAeareRAEELLELVGLSgfeNAYPHQ--------LSGGMRQRVALARALA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 485 EERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEM 541
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVL 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-565 |
8.87e-26 |
|
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: 106.04 E-value: 8.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFS---VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLF 418
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 419 SAVFTDvwlfdrllgPEGqQANPAL-VEKWLAQLQMSHKLELQDGKILNL----------------KLSKGQKKRVALLL 481
Cdd:COG1124 82 QMVFQD---------PYA-SLHPRHtVDRILAEPLRIHGLPDREERIAELleqvglppsfldryphQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 482 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRDGKLSE-LTGEDRDAASR 559
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEeLTVADLLAGPK 231
|
....*.
gi 2131440126 560 DAVART 565
Cdd:COG1124 232 HPYTRE 237
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
342-546 |
1.18e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.37 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQ-DSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:PRK13648 8 IVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTD--------VWLFDRLLGPEgQQANP-----ALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEER 487
Cdd:PRK13648 88 VFQNpdnqfvgsIVKYDVAFGLE-NHAVPydemhRRVSEALKQVDMLERADYEPN-----ALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 488 DIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-565 |
1.64e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.17 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDS-AFSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKP--------E 412
Cdd:COG1121 7 IELENLTVSYGGRpVLE--DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrigyvpqrA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 413 DYRKLFSA-VFtDV----------WLfdRLLGPEGQQAnpalVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLL 481
Cdd:COG1121 85 EVDWDFPItVR-DVvlmgrygrrgLF--RRPSRADREA----VDEALERVGLEDLADRPIG-----ELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 482 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHyFI--HADRLLEMRDGKLSEltGEDRDAASR 559
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLG-AVreYFDRVLLLNRGLVAH--GPPEEVLTP 228
|
....*.
gi 2131440126 560 DAVART 565
Cdd:COG1121 229 ENLSRA 234
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
351-528 |
2.17e-25 |
|
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: 103.27 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 351 YQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEK----------------PEDy 414
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkgllerrqrvglvfqdPDD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 415 rKLFSA-VFTDVWLFDRLLGPEGQQANpALVEKWLAQLQMSHkLELQdgkiLNLKLSKGQKKRVALLLALAEERDIILLD 493
Cdd:TIGR01166 80 -QLFAAdVDQDVAFGPLNLGLSEAEVE-RRVREALTAVGASG-LRER----PTHCLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 2131440126 494 EWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD 528
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAE-GMTVVISTHD 186
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
342-546 |
2.85e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.65 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAF-SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE---ILLDGKALSAEKPEDYRKL 417
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 FSAVF------------TDvwlfDRLLGPEGQQAN----PALVEKWLAQLQMshkLELQDGKILNLklSKGQKKRVALLL 481
Cdd:PRK13640 86 VGIVFqnpdnqfvgatvGD----DVAFGLENRAVPrpemIKIVRDVLADVGM---LDYIDSEPANL--SGGQKQRVAIAG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 482 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
342-545 |
2.90e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.70 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAL--SAEKPEDYRKLFS 419
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFT--DVWLF------DRLLGPegqqANPALVEKWLaQLQMSHKLELQDGKILNLK----LSKGQKKRVALLLALAEER 487
Cdd:PRK13636 86 MVFQdpDNQLFsasvyqDVSFGA----VNLKLPEDEV-RKRVDNALKRTGIEHLKDKpthcLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 488 DIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGK 545
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGR 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
342-546 |
8.29e-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: 101.14 E-value: 8.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFdrllgpegqqanpalvekwlaqlqmshklelqDGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 500
Cdd:cd03246 81 LPQDDELF--------------------------------SGSIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2131440126 501 PHFRREFYQVLLpLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:cd03246 129 VEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
342-546 |
9.03e-25 |
|
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: 102.67 E-value: 9.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAF-SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:cd03245 3 IEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLF-----------------DRLLgpegQQANPALVEKWLAQLQMSHKLELQDGkilNLKLSKGQKKRVALLLAL 483
Cdd:cd03245 83 VPQDVTLFygtlrdnitlgapladdERIL----RAAELAGVTDFVNKHPNGLDLQIGER---GRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 484 AEERDIILLDEWAADQDPHFRREFYQVLlplmQEM--GKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERL----RQLlgDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
343-541 |
9.28e-25 |
|
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: 102.23 E-value: 9.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKalsaeKPEDYRKLFSAV- 421
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 ---------------------FTDVWLFDRLlgpegQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALL 480
Cdd:cd03235 75 qrrsidrdfpisvrdvvlmglYGHKGLFRRL-----SKADKAKVDEALERVGLSELADRQIG-----ELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 481 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEM 541
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDlGLVLEYFDRVLLL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
342-545 |
1.77e-24 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 101.40 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSA-FSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALsAEKPEDYRKLFSA 420
Cdd:COG4133 3 LEAENLSCRRGERLlFS--GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFDRLLGPE---------GQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIIL 491
Cdd:COG4133 80 LGHADGLKPELTVREnlrfwaalyGLRADREAIDEALEAVGLAGLADLPVR-----QLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 492 LDEWAADQDPHFRREFYQvllpLMQEM---GKTIFAISHDDhYFIHADRLLEMRDGK 545
Cdd:COG4133 155 LDEPFTALDAAGVALLAE----LIAAHlarGGAVLLTTHQP-LELAAARVLDLGDFK 206
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
342-548 |
5.33e-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: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGP-VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRdISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFDRLL------GPEGqqANPALVEKwLAQLQMSHKL--ELQDGKILNL-----KLSKGQKKRVALLLALAEER 487
Cdd:cd03251 81 VSQDVFLFNDTVaeniayGRPG--ATREEVEE-AARAANAHEFimELPEGYDTVIgergvKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 488 DIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
342-546 |
5.80e-24 |
|
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: 100.82 E-value: 5.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYqdsafsvGP------VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---ALSAEKPE 412
Cdd:COG1127 6 IEVRNLTKSF-------GDrvvldgVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 413 DYRK----LF--SAVFTDVWLFDRLLGP--EGQQANPALVEKwLAQLqmshKLELqdgkiLNLK---------LSKGQKK 475
Cdd:COG1127 79 ELRRrigmLFqgGALFDSLTVFENVAFPlrEHTDLSEAEIRE-LVLE----KLEL-----VGLPgaadkmpseLSGGMRK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 476 RVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDH--YFIhADRLLEMRDGKL 546
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDsaFAI-ADRVAVLADGKI 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
342-546 |
3.75e-23 |
|
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: 97.56 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVgpvNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDyrKLFSAV 421
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRL---------------LGPEGQQAnpalVEKWLAQLQMSHKLelqdgKILNLKLSKGQKKRVALLLALAEE 486
Cdd:cd03298 76 FQENNLFAHLtveqnvglglspglkLTAEDRQA----IEVALARVGLAGLE-----KRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 487 RDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISH--DDHYFIhADRLLEMRDGKL 546
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHqpEDAKRL-AQRVVFLDNGRI 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
342-548 |
4.18e-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: 96.61 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKpEDYRKLFSA 420
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFDRLLGPEgqqanpalvekwlaqlqmshklelqdgkiLNLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 500
Cdd:cd03247 80 LNQRPYLFDTTLRNN-----------------------------LGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2131440126 501 PHFRREfyqvLLPLMQEM--GKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:cd03247 131 PITERQ----LLSLIFEVlkDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-546 |
6.00e-23 |
|
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: 95.57 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKlfsav 421
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 ftdvwlfdrlLGpegqqanpalvekwlaqLQMSHklelQdgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDP 501
Cdd:cd03216 75 ----------AG-----------------IAMVY----Q--------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2131440126 502 HFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03216 116 AEVERLFKVIRRL-RAQGVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
342-546 |
6.09e-23 |
|
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: 97.19 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAF-SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL--- 417
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 --FSAVFTD------VWLFDRLLGPEGQQANpALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDI 489
Cdd:cd03263 81 pqFDALFDEltvrehLRFYARLKGLPKSEIK-EEVELLLRVLGLTDKANKRAR-----TLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 490 ILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSmDEAEALCDRIAIMSDGKL 210
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
342-548 |
7.05e-23 |
|
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: 97.69 E-value: 7.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAV 421
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRLLGPEGQQANPALVEkwlAQLQMSHKLELQDGKILN-------------LKLSKGQKKRVALLLALAEERD 488
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATD---EEVIEAAKAAQIHDKIMRfpdgydtivgergLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 489 IILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVE 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
342-548 |
8.45e-23 |
|
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: 97.56 E-value: 8.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQ-DSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFDRLLGPEGQQANPAL-VEK--WLAQLQMSHK--LELQDG--KILNLK---LSKGQKKRVALLLALAEERDII 490
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMsMERviEAAKLAGAHDfiSELPEGydTIVGEQgagLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 491 LLDEWAADQDphfrrefYQVLLPLMQEM-----GKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:cd03252 161 IFDEATSALD-------YESEHAIMRNMhdicaGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
342-558 |
9.52e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.14 E-value: 9.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG-KALSAEKPEDYRKLFSA 420
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTD--------VWLFDRLLGPEGQQANP----ALVEKWLAQLQMShKLELQDGKilnlKLSKGQKKRVALLLALAEERD 488
Cdd:PRK13644 82 VFQNpetqfvgrTVEEDLAFGPENLCLPPieirKRVDRALAEIGLE-KYRHRSPK----TLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 489 IILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHYFIHADRLLEMRDGKLSeLTGEDRDAAS 558
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHDADRIIVMDRGKIV-LEGEPENVLS 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
342-546 |
1.18e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.84 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPE--DYRKLFS 419
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFT--DVWLF------DRLLGPEGQQANPALVEKWLAQLQMSHKLELQDGKILNlKLSKGQKKRVALLLALAEERDIIL 491
Cdd:PRK13639 82 IVFQnpDDQLFaptveeDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPH-HLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2131440126 492 LDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDvDLVPVYADKVYVMSDGKI 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
342-546 |
1.22e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 99.40 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDyRKlFSAV 421
Cdd:COG3842 6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-RN-VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFD------------RLLGPEGQQANpALVEKWLAQLQMSHkleLQDGKIlnLKLSKGQKKRVALLLALAEERDI 489
Cdd:COG3842 83 FQDYALFPhltvaenvafglRMRGVPKAEIR-ARVAELLELVGLEG---LADRYP--HQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 490 ILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqEEALALADRIAVMNDGRI 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
342-546 |
1.23e-22 |
|
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: 96.92 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPedYRKLFSAV 421
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRL-------LGPEGQQANPAL----VEKWLAQLQMShklELQDGKIlnLKLSKGQKKRVALLLALAEERDII 490
Cdd:cd03300 78 FQNYALFPHLtvfeniaFGLRLKKLPKAEikerVAEALDLVQLE---GYANRKP--SQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 491 LLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGKI 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
342-560 |
1.32e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.75 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVgpvNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPedYRKLFSAV 421
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF---DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRL---------------LGPEGQQAnpalVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEE 486
Cdd:COG3840 77 FQENNLFPHLtvaqniglglrpglkLTAEQRAQ----VEQALERVGLAGLLDRLPG-----QLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 487 RDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD--------DHY-FIHADRLLEmrDGKLSELTGEDRDAA 557
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDpedaariaDRVlLVADGRIAA--DGPTAALLDGEPPPA 225
|
...
gi 2131440126 558 SRD 560
Cdd:COG3840 226 LAA 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
342-549 |
2.01e-22 |
|
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: 96.11 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFS---VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRK-- 416
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 417 -----------LFSA--VFTDVWLFDRLLGPEGQQAnPALVEKWLAQLQMSHKlelqdGKILNLKLSKGQKKRVALLLAL 483
Cdd:cd03258 82 rrigmifqhfnLLSSrtVFENVALPLEIAGVPKAEI-EERVLELLELVGLEDK-----ADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 484 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDdhyfIH-----ADRLLEMRDGKLSEL 549
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHE----MEvvkriCDRVAVMEKGEVVEE 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
342-528 |
3.27e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 96.31 E-value: 3.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEdyrklF 418
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtalDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 419 SAVFTDvwlfDRL-----------LGPEGQQANPA----LVEKWLAQLQMSHKLEL---QdgkilnlkLSKGQKKRVALL 480
Cdd:COG1116 83 GVVFQE----PALlpwltvldnvaLGLELRGVPKAerreRARELLELVGLAGFEDAyphQ--------LSGGMRQRVAIA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 481 LALAEERDIILLDEwaadqdPhF-------RREFYQVLLPLMQEMGKTIFAISHD 528
Cdd:COG1116 151 RALANDPEVLLMDE------P-FgaldaltRERLQDELLRLWQETGKTVLFVTHD 198
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
331-552 |
6.98e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.60 E-value: 6.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 331 PRPQAFPNWQT---LELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALS 407
Cdd:PRK11607 6 PRPQAKTRKALtplLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 408 AEKPedYRKLFSAVFTDVWLF---------------DRLlgPEGQQAnpALVEKWLAqlqMSHKLELQDGKilNLKLSKG 472
Cdd:PRK11607 85 HVPP--YQRPINMMFQSYALFphmtveqniafglkqDKL--PKAEIA--SRVNEMLG---LVHMQEFAKRK--PHQLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 473 QKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKLSELtG 551
Cdd:PRK11607 154 QRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGKFVQI-G 232
|
.
gi 2131440126 552 E 552
Cdd:PRK11607 233 E 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
361-528 |
7.98e-22 |
|
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: 95.11 E-value: 7.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL-----F--SAVFTD--------- 424
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiartFqnPRLFPEltvlenvlv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 425 -------VWLFDRLLGP----EGQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILLD 493
Cdd:COG0411 103 aaharlgRGLLAALLRLprarREEREARERAEELLERVGLADRADEPAG-----NLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190
....*....|....*....|....*....|....*
gi 2131440126 494 EWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD 528
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRDERGITILLIEHD 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
342-555 |
1.31e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 94.17 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFS-- 419
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 -------------AVFTDV-----------WLFDRLLGPEGQQANPALvekwLAQLQMSHKLELQDGkilnlKLSKGQKK 475
Cdd:cd03256 81 gmifqqfnlierlSVLENVlsgrlgrrstwRSLFGLFPKEEKQRALAA----LERVGLLDKAYQRAD-----QLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 476 RVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFI-HADRLLEMRDGKL------SE 548
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAReYADRIVGLKDGRIvfdgppAE 231
|
....*..
gi 2131440126 549 LTGEDRD 555
Cdd:cd03256 232 LTDEVLD 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
342-552 |
1.33e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVkfHYQ-DSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFS- 419
Cdd:PRK10247 8 LQLQNV--GYLaGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSy 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 -----AVFTDVwLFDRLLGP---EGQQANPALVEKWLAQLQMSHKLeLQdgKILNlKLSKGQKKRVALLLALAEERDIIL 491
Cdd:PRK10247 86 caqtpTLFGDT-VYDNLIFPwqiRNQQPDPAIFLDDLERFALPDTI-LT--KNIA-ELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 492 LDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRL--LEMRDGKLSELTGE 552
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVitLQPHAGEMQEARYE 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
342-546 |
1.74e-21 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 92.98 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPE--DYRKLFS 419
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKG-IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFTDVWLFDRL-------LGP-----EGQQANPALVEKWLAQLQMSHKlelQDGKIlnLKLSKGQKKRVALLLALAEER 487
Cdd:cd03262 80 MVFQQFNLFPHLtvlenitLAPikvkgMSKAEAEERALELLEKVGLADK---ADAYP--AQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 488 DIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHdDHYFIH--ADRLLEMRDGKL 546
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTH-EMGFARevADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
342-548 |
3.05e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.42 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPED---YRKLF 418
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 419 SAVFTDVWLFD------------RLLGPEGQQANpALVEKWLAQLQMSHKLELqdgkiLNLKLSKGQKKRVALLLALAEE 486
Cdd:COG2884 82 GVVFQDFRLLPdrtvyenvalplRVTGKSRKEIR-RRVREVLDLVGLSDKAKA-----LPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 487 RDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHyFIHA--DRLLEMRDGKLSE 548
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
343-546 |
3.14e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.22 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDY-RKL---- 417
Cdd:COG4604 3 EIKNVSKRYGGKV-VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELaKRLailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 ----FSAVFT--DVWLFDRL------LGPEGQQAnpalVEKWLAQLQMShklELQDgKILNlKLSKGQKKRVALLLALAE 485
Cdd:COG4604 82 qenhINSRLTvrELVAFGRFpyskgrLTAEDREI----IDEAIAYLDLE---DLAD-RYLD-ELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2131440126 486 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDdhyfI-----HADRLLEMRDGKL 546
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD----InfascYADHIVAMKDGRV 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
30-541 |
3.21e-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: 97.36 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 30 YRWPFIAVMALSLASAALGIG---LIAFINVRLIEMTDTSLSVLPEFLGlllllMAVTLGSQLALTTLGHHFVFRLRSEF 106
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAqawLLARVVDGLISAGEPLAELLPALGA-----LALVLLLRALLGWLQERAAARAAAAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 107 IKRILDTQIERVEQLG--------SASLLAGLTSDVRAITIAFVR-LPELVQGII--LTFGSAAYLA-WLSSKMLAVTAL 174
Cdd:TIGR02857 76 KSQLRERLLEAVAALGprwlqgrpSGELATLALEGVEALDGYFARyLPQLVLAVIvpLAILAAVFPQdWISGLILLLTAP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 175 WIVITIW-GGFMLVSRVYKHMAVLreteDKLYNDYQTVLEGRKEL-TLNRERAEHifNHLYiPDAREYRHHIIRA--DTF 250
Cdd:TIGR02857 156 LIPIFMIlIGWAAQAAARKQWAAL----SRLSGHFLDRLRGLPTLkLFGRAKAQA--AAIR-RSSEEYRERTMRVlrIAF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 251 HLSAVnwsnIMMLGAIGLVFwmanglgwadtnVAATYSLTLLFLRTPLLSAvgaLPTLLSAQVAFNKLKKF--------- 321
Cdd:TIGR02857 229 LSSAV----LELFATLSVAL------------VAVYIGFRLLAGDLDLATG---LFVLLLAPEFYLPLRQLgaqyharad 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 322 ------DLAPFKAEFPRPQ-------AFPNWQtLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLL 388
Cdd:TIGR02857 290 gvaaaeALFAVLDAAPRPLagkapvtAAPASS-LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 389 TGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFD-------RLLGPEgqqANPALVEKWLAQ---------LQ 452
Cdd:TIGR02857 369 LGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAgtiaeniRLARPD---ASDAEIREALERagldefvaaLP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 453 MSHKLELQDGkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYF 532
Cdd:TIGR02857 446 QGLDTPIGEG---GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA 520
|
....*....
gi 2131440126 533 IHADRLLEM 541
Cdd:TIGR02857 521 ALADRIVVL 529
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
342-545 |
4.35e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.26 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAV 421
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTD---------VWLfDRLLGPEGQQANPALVEKwlaqlQMSHKLELQDGKILNLK----LSKGQKKRVALLLALAEERD 488
Cdd:PRK13647 85 FQDpddqvfsstVWD-DVAFGPVNMGLDKDEVER-----RVEEALKAVRMWDFRDKppyhLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 489 IILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD-DHYFIHADRLLEMRDGK 545
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDvDLAAEWADQVIVLKEGR 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
361-546 |
7.06e-21 |
|
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: 91.73 E-value: 7.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL-FSAVFTDVWLFDRL-------L 432
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPELtvlenvmV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 433 GPEGQQANPAL--------------VEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILLDEWAAD 498
Cdd:cd03219 99 AAQARTGSGLLlararreerearerAEELLERVGLADLADRPAG-----ELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2131440126 499 QDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03219 174 LNPEETEELAELIREL-RERGITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
286-555 |
7.85e-21 |
|
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: 96.73 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 286 TYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLKKFDLAPfkAEFPRPQAFPNWQTL----ELRNVKFHYQDSAFSVGPV 361
Cdd:TIGR01193 416 TFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVD--SEFINKKKRTELNNLngdiVINDVSYSYGYGSNILSDI 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 362 NLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLF-----DRLLgpeg 436
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFsgsilENLL---- 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 437 QQANP-------------ALVEKWLAQLQMSHKLELQDGkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF 503
Cdd:TIGR01193 570 LGAKEnvsqdeiwaaceiAEIKDDIENMPLGYQTELSEE---GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 504 RREFYQVLLPLMQemgKTIFAISHDDHYFIHADRLLEMRDGKLSElTGEDRD 555
Cdd:TIGR01193 647 EKKIVNNLLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKIIE-QGSHDE 694
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
342-546 |
2.35e-20 |
|
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: 89.84 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFS--VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFS 419
Cdd:cd03248 12 VKFQNVTFAYPTRPDTlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFTDVWLFDRLLGPE---GQQANPALVEKWLAQLQMSHKL--ELQDGKILNL-----KLSKGQKKRVALLLALAEERDI 489
Cdd:cd03248 92 LVGQEPVLFARSLQDNiayGLQSCSFECVKEAAQKAHAHSFisELASGYDTEVgekgsQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 490 ILLDEWAADQDPHFRREFYQVLLPLMQEmgKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
342-546 |
2.60e-20 |
|
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: 90.09 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDsaFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEdyRKLFSAV 421
Cdd:cd03299 1 LKVENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRL-------LGPEGQQANPALVEKWLaqLQMSHKLELqdGKILNLK---LSKGQKKRVALLLALAEERDIIL 491
Cdd:cd03299 77 PQNYALFPHMtvykniaYGLKKRKVDKKEIERKV--LEIAEMLGI--DHLLNRKpetLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2131440126 492 LDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKL 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
342-546 |
3.11e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.92 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQD-----SAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPE-DYR 415
Cdd:PRK13633 5 IKCKNVSYKYESneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 416 KLFSAVFT--DVWLF------DRLLGPEGQQANP----ALVEKWLAQLQMS----HKLELqdgkilnlkLSKGQKKRVAL 479
Cdd:PRK13633 85 NKAGMVFQnpDNQIVativeeDVAFGPENLGIPPeeirERVDESLKKVGMYeyrrHAPHL---------LSGGQKQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 480 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
342-545 |
3.51e-20 |
|
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: 88.88 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEK-------PED- 413
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEEr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 414 --YRKLfsAVFTDVWLFDRLLGPEGQQANPAlVEKWLAQLQMSHKLElqdgKILNlKLSKGQKKRVALLLALAEERDIIL 491
Cdd:cd03269 80 glYPKM--KVIDQLVYLAQLKGLKKEEARRR-IDEWLERLELSEYAN----KRVE-ELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 492 LDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRDGK 545
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQmELVEELCDRVLLLNKGR 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
361-546 |
6.52e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 6.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKP----EDYRKLFSAVF--TDVWLF------ 428
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFqfPEAQLFentvlk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 429 DRLLGP------EGQQANPALveKWLAQLQMSHKLELQDgkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 502
Cdd:PRK13641 106 DVEFGPknfgfsEDEAKEKAL--KWLKKVGLSEDLISKS----PFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2131440126 503 FRREFYQVLLPlMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:PRK13641 180 GRKEMMQLFKD-YQKAGHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
340-562 |
1.09e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.38 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 340 QTLELRNVKFHYQDSA--FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL 417
Cdd:PRK13642 3 KILEVENLVFKYEKESdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 FSAVFTD--------VWLFDRLLGPEGQQ-ANPALVEKWLAQLQMSHKLELQDGKilNLKLSKGQKKRVALLLALAEERD 488
Cdd:PRK13642 83 IGMVFQNpdnqfvgaTVEDDVAFGMENQGiPREEMIKRVDEALLAVNMLDFKTRE--PARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 489 IILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGK-LSELTGEDRDAASRDAV 562
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEiIKEAAPSELFATSEDMV 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
361-544 |
2.16e-19 |
|
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: 87.14 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPE------DYRKL-FSAVFTDVWL-FDRLL 432
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvvfqNYSLLpWLTVRENIALaVDRVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 433 GPEGQQANPALVEKWLAQLQMSHKLELQDGKilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLL 512
Cdd:TIGR01184 84 PDLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190
....*....|....*....|....*....|...
gi 2131440126 513 PLMQEMGKTIFAISHD-DHYFIHADRLLEMRDG 544
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
361-555 |
2.23e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.57 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAE--KPEDYRKLFSAVFT--DVWLF------DR 430
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvKLSDIRKKVGLVFQypEYQLFeetiekDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 431 LLGPEGQQANPALVEKWLAQLQMSHKLELQDGKILN-LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQ 509
Cdd:PRK13637 106 AFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSpFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILN 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2131440126 510 VLLPLMQEMGKTIFAISH--DDHYFIhADRLLEMRDGKLsELTGEDRD 555
Cdd:PRK13637 186 KIKELHKEYNMTIILVSHsmEDVAKL-ADRIIVMNKGKC-ELQGTPRE 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
342-546 |
6.65e-19 |
|
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: 85.54 E-value: 6.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKP---------- 411
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipylrrki 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 412 ----EDYRKLFS-AVFTDVWLFDRLLGPEGQQAnPALVEKWLAQLQMSHKlelqdGKILNLKLSKGQKKRVALLLALAEE 486
Cdd:cd03292 81 gvvfQDFRLLPDrNVYENVAFALEVTGVPPREI-RKRVPAALELVGLSHK-----HRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 487 RDIILLDEWAADQDPHFRREFYQvLLPLMQEMGKTIFAISHDDHYF-IHADRLLEMRDGKL 546
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
342-548 |
7.80e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.88 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFDRLLGPEGQQANPALVEKWLAQLQMSHKLE--LQDGKILNL-------KLSKGQKKRVALLLALAEERDIIL 491
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEklLEDDKGLNAwlgeggrQLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 492 LDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
341-546 |
1.00e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSa 420
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 vftdvWLFDRLLGPEG---------------------QQANPALVEKWLAQLQMSHkleLQDGKILNlkLSKGQKKRVAL 479
Cdd:PRK11231 80 -----LLPQHHLTPEGitvrelvaygrspwlslwgrlSAEDNARVNQAMEQTRINH---LADRRLTD--LSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 480 LLALAEERDIILLDEWAADQDPHfrrefYQV-LLPLMQEM---GKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDIN-----HQVeLMRLMRELntqGKTVVTVLHDlNQASRYCDHLVVLANGHV 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
341-546 |
1.51e-18 |
|
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: 85.08 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFsa 420
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFDRL-----------LGPEGQQANPALV-EKWLAQLQMSHKLELQDGkiLNLKLSKGQKKRVALLLALAEERD 488
Cdd:cd03296 79 VFQHYALFRHMtvfdnvafglrVKPRSERPPEAEIrAKVHELLKLVQLDWLADR--YPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 489 IILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRDGKL 546
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
342-548 |
1.70e-18 |
|
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: 85.63 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFS--------VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPED 413
Cdd:TIGR02769 3 LEVRDVTHTYRTGGLFgakqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 414 ---YRKLFSAVFTDVWlfdrllgpegQQANPALVEKWLAQLQMSHKLEL----QDGKILNL----------------KLS 470
Cdd:TIGR02769 83 rraFRRDVQLVFQDSP----------SAVNPRMTVRQIIGEPLRHLTSLdeseQKARIAELldmvglrsedadklprQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 471 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD---DHYFihADRLLEMRDGKLS 547
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDlrlVQSF--CQRVAVMDKGQIV 230
|
.
gi 2131440126 548 E 548
Cdd:TIGR02769 231 E 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
342-555 |
1.90e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.57 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGP----VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAE-KPEDYRK 416
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRalfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 417 L-------F----SAVFTDVWLFDRLLGPE----GQQANPALVEKWLAQLQMSHKLELQDgkilNLKLSKGQKKRVALLL 481
Cdd:PRK13649 83 IrkkvglvFqfpeSQLFEETVLKDVAFGPQnfgvSQEEAEALAREKLALVGISESLFEKN----PFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 482 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISH--DD--HYfihADRLLEMRDGKLSeLTGEDRD 555
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHlmDDvaNY---ADFVYVLEKGKLV-LSGKPKD 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
341-548 |
3.40e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.97 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYqdSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL-F 418
Cdd:COG1118 2 SIEVRNISKRF--GSFTLlDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVgF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 419 saVFTDVWLF-------------DRLLGPEGQQAnpALVEKWLAQLQMSHklelqdgkilnLK------LSKGQKKRVAL 479
Cdd:COG1118 80 --VFQHYALFphmtvaeniafglRVRPPSKAEIR--ARVEELLELVQLEG-----------LAdrypsqLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 480 LLALAEERDIILLDE-WAAdQDPHFRREFYQVLLPLMQEMG-KTIFaISHD--DHYFIhADRLLEMRDGKLSE 548
Cdd:COG1118 145 ARALAVEPEVLLLDEpFGA-LDAKVRKELRRWLRRLHDELGgTTVF-VTHDqeEALEL-ADRVVVMNQGRIEQ 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
361-546 |
5.26e-18 |
|
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: 82.97 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKalsaekpedyrklfsavftDVWLFD----------- 429
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-------------------VSSLLGlgggfnpeltg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 430 --------RLLG---PEGQQANPALVEkwLAQLqmshklelqdGKILNLKL---SKGQKKRVALLLALAEERDIILLDEW 495
Cdd:cd03220 102 reniylngRLLGlsrKEIDEKIDEIIE--FSEL----------GDFIDLPVktySSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 496 AADQDPHFRREFYQVLLPlMQEMGKTIFAISHDDHYFI-HADRLLEMRDGKL 546
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKrLCDRALVLEKGKI 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
342-548 |
5.82e-18 |
|
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: 82.93 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFD---RL-LGPEGQQANPALvekWLAqLQMSHKLEL--QDGKILNLK-------LSKGQKKRVALLLALAEER 487
Cdd:cd03244 83 IPQDPVLFSgtiRSnLDPFGEYSDEEL---WQA-LERVGLKEFveSLPGGLDTVveeggenLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 488 DIILLDEWAADQDPHFRRefyqvllpLMQEM------GKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:cd03244 159 KILVLDEATASVDPETDA--------LIQKTireafkDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
342-546 |
6.79e-18 |
|
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: 82.69 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDyRKLfSAV 421
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDI-AMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRL-------LGPEGQQANPALVEK---WLAQLqmshkleLQDGKILNLK---LSKGQKKRVALLLALAEERD 488
Cdd:cd03301 78 FQNYALYPHMtvydniaFGLKLRKVPKDEIDErvrEVAEL-------LQIEHLLDRKpkqLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 489 IILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqVEAMTMADRIAVMNDGQI 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
361-559 |
1.24e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.37 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFS----AVFTDVWLFD------R 430
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVfqhyALFRHMTVFDniafglT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 431 LLgPEGQQANPALVEKWLAQL----QMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE 506
Cdd:PRK10851 101 VL-PRRERPNAAAIKAKVTQLlemvQLAHLADRYPA-----QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 507 FYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRDGKLSEL-TGED--RDAASR 559
Cdd:PRK10851 175 LRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAgTPDQvwREPATR 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
342-554 |
3.11e-17 |
|
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: 80.94 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVG---PVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAeKPEDYRKLF 418
Cdd:COG4181 9 IELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA-LDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 419 SA-----VFTDVWLFDRL-----------LGPEGQQANPAlvEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLA 482
Cdd:COG4181 88 RArhvgfVFQSFQLLPTLtalenvmlpleLAGRRDARARA--RALLERVGLGHRLDHYPA-----QLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 483 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKLSELTGEDR 554
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
361-555 |
3.16e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 82.38 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEK-PEDYRKLFSAV-----FTDVWLF------ 428
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKkNKKLKPLRKKVgivfqFPEHQLFeetvek 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 429 DRLLGPEG----QQANPALVEKWLAQLQMSHKLELQDgkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 504
Cdd:PRK13634 106 DICFGPMNfgvsEEDAKQKAREMIELVGLPEELLARS----PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 505 REFYQVLLPLMQEMGKTIFAISH--DD--HYfihADRLLEMRDGKLsELTGEDRD 555
Cdd:PRK13634 182 KEMMEMFYKLHKEKGLTTVLVTHsmEDaaRY---ADQIVVMHKGTV-FLQGTPRE 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
342-545 |
7.19e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.69 E-value: 7.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPED-------- 413
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENrhvntvfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 414 -YrKLFS--AVFTDVWLFDRLLGPEGQQANPALVEKwlaqLQMSHKLELQDGKILNlkLSKGQKKRVALLLALAEERDII 490
Cdd:PRK09452 94 sY-ALFPhmTVFENVAFGLRMQKTPAAEITPRVMEA----LRMVQLEEFAQRKPHQ--LSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2131440126 491 LLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGK 545
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGR 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
342-548 |
7.38e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.14 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkaLSAEKPE----DYRKL 417
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHN-IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKvderLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 FSAVFTDVWLFDRL-------LGP-----EGQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAE 485
Cdd:PRK09493 79 AGMVFQQFYLFPHLtalenvmFGPlrvrgASKEEAEKQARELLAKVGLAERAHHYPS-----ELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 486 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHyFIH--ADRLLEMRDGKLSE 548
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIG-FAEkvASRLIFIDKGRIAE 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
345-527 |
9.40e-17 |
|
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: 79.33 E-value: 9.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 345 RNVKFHYQdsafSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL--FSA-- 420
Cdd:cd03266 12 RDVKKTVQ----AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLgfVSDst 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 -------VFTDVWLFDRLLGPEGQQANPALveKWLA-QLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILL 492
Cdd:cd03266 88 glydrltARENLEYFAGLYGLKGDELTARL--EELAdRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 2131440126 493 DEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISH 527
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTH 194
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
361-564 |
9.46e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 9.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL--------FSavftdvwLFDRL- 431
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgigmvhqhFM-------LVPNLt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 432 ------LGPEGQQA---NPALVEKWLAQLqmSHKLELQ---DGKILNlkLSKGQKKRVALLLALAEERDIILLDEWAADQ 499
Cdd:COG3845 97 vaenivLGLEPTKGgrlDRKAARARIREL--SERYGLDvdpDAKVED--LSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 500 DPHFRREFYQVLLpLMQEMGKTIFAISHDdhyfIH-----ADRLLEMRDGKlseLTGE-DRDAASRDAVAR 564
Cdd:COG3845 173 TPQEADELFEILR-RLAAEGKSIIFITHK----LRevmaiADRVTVLRRGK---VVGTvDTAETSEEELAE 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
341-546 |
1.80e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 80.89 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDyRKLfSA 420
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI-AM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFD------------RLLGPEGQQANpALVEKWLAQLQMSHklelqdgkILNLK---LSKGQKKRVALLLALAE 485
Cdd:COG3839 80 VFQSYALYPhmtvyeniafplKLRKVPKAEID-RRVREAAELLGLED--------LLDRKpkqLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2131440126 486 ERDIILLDEWAADQDPH----FRREFYQvllpLMQEMGKTIFAISHDdhy-fihADRLLEMRDGKL 546
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKlrveMRAEIKR----LHRRLGTTTIYVTHDqveamtlADRIAVMNDGRI 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
341-548 |
2.50e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.44 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDSA----FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDY-- 414
Cdd:PRK13646 2 TIRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 415 --RKLFSAVFT--DVWLFDR------LLGPEGQQANPALVEKWLAQLQMSHKLELQDGKILNLKLSKGQKKRVALLLALA 484
Cdd:PRK13646 82 pvRKRIGMVFQfpESQLFEDtvereiIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 485 EERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKLSE 548
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVS 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
361-546 |
2.60e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.05 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLfSAV----------FT--DVWLF 428
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAVlpqhsslsfpFTveEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 429 DRLLGPEGQQANPALVEKWLAQLQMSHkleLQDGKIlnLKLSKGQKKRVALLLALA------EERDIILLDEWAADQDPH 502
Cdd:PRK13548 100 GRAPHGLSRAEDDALVAAALAQVDLAH---LAGRDY--PQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2131440126 503 FRREFYQVLLPLMQEMGKTIFAISHD----DHYfihADRLLEMRDGKL 546
Cdd:PRK13548 175 HQHHVLRLARQLAHERGLAVIVVLHDlnlaARY---ADRIVLLHQGRL 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
361-528 |
2.80e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.97 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDyrklfSAVFTDvwlfDRLLGPEGQQAN 440
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQN----EGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 441 PAL---------VEKWLAQLQMSHKLELQD-GKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQV 510
Cdd:PRK11248 91 VAFglqlagvekMQRLEIAHQMLKKVGLEGaEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
|
170
....*....|....*...
gi 2131440126 511 LLPLMQEMGKTIFAISHD 528
Cdd:PRK11248 171 LLKLWQETGKQVLLITHD 188
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
342-545 |
3.01e-16 |
|
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: 77.51 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGP----VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK-ALSAEKPEdyrk 416
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiAYVSQEPW---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 417 LFSAVFTDVWLFdrllgpeGQQANPALVEKWL--AQLQmshklelQDGKILNLK-----------LSKGQKKRVALLLAL 483
Cdd:cd03250 77 IQNGTIRENILF-------GKPFDEERYEKVIkaCALE-------PDLEILPDGdlteigekginLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 484 AEERDIILLDEWAADQDPHFRRE-FYQVLLPLMQEmGKTIFAISHDDHYFIHADRLLEMRDGK 545
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHiFENCILGLLLN-NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
342-537 |
3.19e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.04 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQD-SAFSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---ALSAEKPEDYRKL 417
Cdd:PRK11831 8 VDMRGVSFTRGNrCIFD--NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 FS------AVFTDVWLFDRLLGPEGQQANpaLVEKWLAQLQMShKLEL----QDGKILNLKLSKGQKKRVALLLALAEER 487
Cdd:PRK11831 86 MSmlfqsgALFTDMNVFDNVAYPLREHTQ--LPAPLLHSTVMM-KLEAvglrGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 488 DIILLDEWAADQDPhfrrEFYQVLLPLMQE----MGKTIFAISHD--------DHYFIHADR 537
Cdd:PRK11831 163 DLIMFDEPFVGQDP----ITMGVLVKLISElnsaLGVTCVVVSHDvpevlsiaDHAYIVADK 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
358-546 |
3.30e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 78.34 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 358 VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYqPQSGEILLDGKALSAEKPED---YRKLFS-----AVFTDVWLFD 429
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElarHRAYLSqqqspPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 430 RLLGPEGqqANPALVEKWLAQLqmSHKLELQD--GKILNlKLSKGQKKRV---ALLL----ALAEERDIILLDEWAADQD 500
Cdd:COG4138 91 ALHQPAG--ASSEAVEQLLAQL--AEALGLEDklSRPLT-QLSGGEWQRVrlaAVLLqvwpTINPEGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2131440126 501 PHFRREFYQvLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:COG4138 166 VAQQAALDR-LLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-549 |
3.31e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.08 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 21 QLLLLVWRQyrWPFIAVMALSLASAALGIGLIAFINVRLIEMTDTSLSVlPEFLGLLLLLMAVTLGSQLALTTLGHHFVF 100
Cdd:TIGR00958 151 RLLGLSGRD--WPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGP-PALASAIFFMCLLSIASSVSAGLRGGSFNY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 101 -------RLRSEFIKRILDTQIERVEQLGSASLLAGLTSDVRAI--TIAFvRLPELVQGIILTFGSAAYLAWLSSKMLAV 171
Cdd:TIGR00958 228 tmarinlRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsrSLSL-NVNVLLRNLVMLLGLLGFMLWLSPRLTMV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 172 TALWIVITIwggfmLVSRVY--KHMAVLRETEDKLYNDYQTVLEG-------------RKELTLNRERAEHIFNhlyipd 236
Cdd:TIGR00958 307 TLINLPLVF-----LAEKVFgkRYQLLSEELQEAVAKANQVAEEAlsgmrtvrsfaaeEGEASRFKEALEETLQ------ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 237 areyrhhIIRADTFHLSAVNWSN-IMMLGAIGLVFW------MANGLGWADTNVAATYSL-------TLLFLRTPLLSAV 302
Cdd:TIGR00958 376 -------LNKRKALAYAGYLWTTsVLGMLIQVLVLYyggqlvLTGKVSSGNLVSFLLYQEqlgeavrVLSYVYSGMMQAV 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 303 GAlptllsaqvafnKLKKFDLAPFKAEFPRP--QAFPNWQTL-ELRNVKFHYQDSafSVGPV----NLTIRRGELLFLIG 375
Cdd:TIGR00958 449 GA------------SEKVFEYLDRKPNIPLTgtLAPLNLEGLiEFQDVSFSYPNR--PDVPVlkglTFTLHPGEVVALVG 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 376 GNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFDRLLgpegqQANPA--LVEKWLAQLQM 453
Cdd:TIGR00958 515 PSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSV-----RENIAygLTDTPDEEIMA 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 454 SHKLELQDGKILNL-------------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQvllpLMQEMGK 520
Cdd:TIGR00958 590 AAKAANAHDFIMEFpngydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE----SRSRASR 665
|
570 580
....*....|....*....|....*....
gi 2131440126 521 TIFAISHDDHYFIHADRLLEMRDGKLSEL 549
Cdd:TIGR00958 666 TVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
297-546 |
3.32e-16 |
|
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: 81.72 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 297 PLLSAVGALPTLLSAQVAFNKLKKFdLAPFKAEF-----PRPQAfpnwqTLELRNVKFHYQDS-AFSVGPVNLTIRRGEL 370
Cdd:COG4618 287 PIEQAIGGWKQFVSARQAYRRLNEL-LAAVPAEPermplPRPKG-----RLSVENLTVVPPGSkRPILRGVSFSLEPGEV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 371 LFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFD--------RLlgpegQQANPA 442
Cdd:COG4618 361 LGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDgtiaeniaRF-----GDADPE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 443 LVEKwLAQLQMSHKLelqdgkILNL-------------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQ 509
Cdd:COG4618 436 KVVA-AAKLAGVHEM------ILRLpdgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA 508
|
250 260 270
....*....|....*....|....*....|....*..
gi 2131440126 510 VLLpLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:COG4618 509 AIR-ALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
349-546 |
4.09e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 349 FHYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPE--DYRKLFSAVFTDvw 426
Cdd:PRK13638 9 FRYQDEPVLKG-LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 427 lfdrllgPEGQ-------------QANPALVEKWLAQlQMSHKLELQDGKILNLK----LSKGQKKRVALLLALAEERDI 489
Cdd:PRK13638 86 -------PEQQifytdidsdiafsLRNLGVPEAEITR-RVDEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 490 ILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDiDLIYEISDAVYVLRQGQI 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
361-546 |
9.34e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.04 E-value: 9.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK-----ALSAEkpedyrklFSAVFT---DVWLFDRLL 432
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallELGAG--------FHPELTgreNIYLNGRLL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 433 GpegqqanpalvekwLAQLQMSHKL-------ELqdGKILNLKL---SKGQKKRVALLLALAEERDIILLDEWAADQDPH 502
Cdd:COG1134 117 G--------------LSRKEIDEKFdeivefaEL--GDFIDQPVktySSGMRARLAFAVATAVDPDILLVDEVLAVGDAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2131440126 503 FRREFYQVLLPLMQEmGKTIFAISHdDHYFI--HADRLLEMRDGKL 546
Cdd:COG1134 181 FQKKCLARIRELRES-GRTVIFVSH-SMGAVrrLCDRAIWLEKGRL 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
342-548 |
1.04e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.42 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGP--------VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSA---EK 410
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGKHqhqtvlnnVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnrAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 411 PEDYRKLFSAVFTDVwlfdrlLGpegqQANPALVEKWLAQLQMSHKLELQD-------GKILNL-------------KLS 470
Cdd:PRK10419 84 RKAFRRDIQMVFQDS------IS----AVNPRKTVREIIREPLRHLLSLDKaerlaraSEMLRAvdlddsvldkrppQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 471 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD---DHYFIHadRLLEMRDGKLS 547
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDlrlVERFCQ--RVMVMDNGQIV 231
|
.
gi 2131440126 548 E 548
Cdd:PRK10419 232 E 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
361-548 |
1.05e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 76.36 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA----VFTDVWLFDRLLGPEG 436
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhvgfVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 437 QQAnPALVE------------KWLAQLQMSHKLelqdgKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 504
Cdd:PRK10584 109 VEL-PALLRgessrqsrngakALLEQLGLGKRL-----DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2131440126 505 REFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-546 |
1.17e-15 |
|
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: 75.16 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQdsafsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAV 421
Cdd:cd03215 5 LEVRGLSVKGA-----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDvwlfDRLLgpEGqqanpaLVekwlaqLQMShkleLQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 501
Cdd:cd03215 80 VPE----DRKR--EG------LV------LDLS----VAENIALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2131440126 502 HFRREFYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRDGKL 546
Cdd:cd03215 138 GAKAEIYRLIRELADA-GKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
338-550 |
1.57e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.01 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 338 NWQTLELRNVKFhyqdsafsvgpvnlTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL 417
Cdd:PRK11629 19 SVQTDVLHNVSF--------------SIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 FSAVFTDVWLFDRLLgPE----GQQANPALVEKWLAQLQMSHKLEL-------QDGKILNLKLSKGQKKRVALLLALAEE 486
Cdd:PRK11629 85 RNQKLGFIYQFHHLL-PDftalENVAMPLLIGKKKPAEINSRALEMlaavgleHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 487 RDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKLS-ELT 550
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTaELS 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
361-530 |
3.46e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 75.06 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEdYRKLFSAVF---TDVW----------L 427
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK-FLRRIGVVFgqkTQLWwdlpvidsfyL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 428 FDRLLGPEGQQANPALVEkwLAQLqmshkleLQDGKILNL---KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 504
Cdd:cd03267 119 LAAIYDLPPARFKKRLDE--LSEL-------LDLEELLDTpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180
....*....|....*....|....*.
gi 2131440126 505 REFYQVLLPLMQEMGKTIFAISHDDH 530
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMK 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
342-548 |
3.67e-15 |
|
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: 74.91 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLY-----QPQSGEILLDGKALSA--EKPEDY 414
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 415 RK----------LFSA-VFTDVWLFDRLLGPEGQQANPALVEKWLAQLQMSHklELQDgKILNLKLSKGQKKRVALLLAL 483
Cdd:cd03260 80 RRrvgmvfqkpnPFPGsIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWD--EVKD-RLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 484 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMgkTIFAISHDdhyfIH-----ADRLLEMRDGKLSE 548
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHN----MQqaarvADRTAFLLNGRLVE 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
342-546 |
4.78e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.23 E-value: 4.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE--------ILLDGKALSAEK 410
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVevlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 411 pedyRKLFSAVFTDVWLFDRLLGPE-----------GQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVAL 479
Cdd:PRK10535 85 ----REHFGFIFQRYHLLSHLTAAQnvevpavyaglERKQRLLRAQELLQRLGLEDRVEYQPS-----QLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 480 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
341-507 |
5.05e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.06 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGKALSAEKPEDyRKL 417
Cdd:COG4136 1 MLSLENLTITLGGRPL-LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQ-RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 fSAVFTDVWLFDRL-----LG---PE--GQQANPALVEKWLAQLQMSHkLELQDGKilnlKLSKGQKKRVALLLALAEER 487
Cdd:COG4136 79 -GILFQDDLLFPHLsvgenLAfalPPtiGRAQRRARVEQALEEAGLAG-FADRDPA----TLSGGQRARVALLRALLAEP 152
|
170 180
....*....|....*....|
gi 2131440126 488 DIILLDEWAADQDPHFRREF 507
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQF 172
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
342-543 |
5.33e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAV 421
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 F--TDVWLF------DRLLGPEGQQANPALVEKWLAQ-LQMSHKLELQDGkiLNLKLSKGQKKRVALLLALAEERDIILL 492
Cdd:PRK13652 84 FqnPDDQIFsptveqDIAFGPINLGLDEETVAHRVSSaLHMLGLEELRDR--VPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 493 DEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHddhyfiHADRLLEMRD 543
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTH------QLDLVPEMAD 206
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
355-553 |
5.34e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 355 AFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG----KALSAEKPEDYRKLFSAVFTDVWLFDR 430
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiaKISDAELREVRRKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 431 LLGPEG-----QQANPALVEKWLAQLQMSHKLELQD-GKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 504
Cdd:PRK10070 121 MTVLDNtafgmELAGINAEERREKALDALRQVGLENyAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2131440126 505 REFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKLSELTGED 553
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQVGTPD 250
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
343-548 |
5.91e-15 |
|
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: 74.50 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHYqDSAFSVG---PVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFS 419
Cdd:cd03249 2 EFKNVSFRY-PSRPDVPilkGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFTDVWLFDR------LLGpegqqANPALVE--KWLAQLQMSHKLelqdgkILNL-------------KLSKGQKKRVA 478
Cdd:cd03249 81 LVSQEPVLFDGtiaeniRYG-----KPDATDEevEEAAKKANIHDF------IMSLpdgydtlvgergsQLSGGQKQRIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 479 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMqeMGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
368-546 |
6.26e-15 |
|
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: 73.87 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 368 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAL-SAEK----PEDYRKLfSAVFTDVWLFDRL---------LG 433
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKkinlPPQQRKI-GLVFQQYALFPHLnvrenlafgLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 434 PEGQQANPALVEKWLAQLQMSHkleLQDGKIlnLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREfyqvLLP 513
Cdd:cd03297 102 RKRNREDRISVDELLDLLGLDH---LLNRYP--AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ----LLP 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 2131440126 514 LMQEMGK-----TIFaISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03297 173 ELKQIKKnlnipVIF-VTHDlSEAEYLADRIVVMEDGRL 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
344-546 |
6.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.43 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 344 LRNVKFHY-QDSAFSVGPVN---LTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSA-----EKPEDY 414
Cdd:PRK13645 9 LDNVSYTYaKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 415 RKLFSAVFT--DVWLF------DRLLGPEGQQANPALVEKWLAQLQMSHKLELQDGKILNLKLSKGQKKRVALLLALAEE 486
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFqetiekDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 487 RDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
361-546 |
1.24e-14 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 73.02 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKalSAEKPEDYRKLFSAVFTDVWLFDRLLGPE----- 435
Cdd:cd03268 19 ISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALIEAPGFYPNLTAREnlrll 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 436 --GQQANPALVEKWLAQLQMSHklelqDGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLP 513
Cdd:cd03268 97 arLLGIRKKRIDEVLDVVGLKD-----SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILS 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 2131440126 514 LMQEmGKTIFAISHddhyFIH-----ADRLLEMRDGKL 546
Cdd:cd03268 172 LRDQ-GITVLISSH----LLSeiqkvADRIGIINKGKL 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-494 |
1.33e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 74.76 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEK-------PED---YRKLfsAVFTDVWLFDR 430
Cdd:COG4152 20 VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEErglYPKM--KVGEQLVYLAR 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 431 LLGPEGQQANPALvEKWLAQLQMSH----KLElqdgkilnlKLSKGQKKRVALLLALAEERDIILLDE 494
Cdd:COG4152 98 LKGLSKAEAKRRA-DEWLERLGLGDrankKVE---------ELSKGNQQKVQLIAALLHDPELLILDE 155
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
342-494 |
1.52e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 73.56 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFhyqdsafSVGP------VNLTIRRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGKALSAEKPED 413
Cdd:COG0396 1 LEIKNLHV-------SVEGkeilkgVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 414 YRK--LFSAvFTD------VWLFD--------RLLGPEGQQANPALVEKWLAQLQMSHKLeLQDGkiLNLKLSKGQKKRV 477
Cdd:COG0396 74 RARagIFLA-FQYpveipgVSVSNflrtalnaRRGEELSAREFLKLLKEKMKELGLDEDF-LDRY--VNEGFSGGEKKRN 149
|
170
....*....|....*..
gi 2131440126 478 ALLLALAEERDIILLDE 494
Cdd:COG0396 150 EILQMLLLEPKLAILDE 166
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
361-541 |
1.68e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.27 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---ALSAEKPEDYRKL----FSAVFTDVWLFDRLLG 433
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGarvAYVPQRSEVPDSLpltvRDLVAMGRWARRGLWR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 434 PEGQQANpALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLP 513
Cdd:NF040873 91 RLTRDDR-AAVDDALERVGLADLAGRQLG-----ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAE 164
|
170 180
....*....|....*....|....*...
gi 2131440126 514 LMQEmGKTIFAISHDDHYFIHADRLLEM 541
Cdd:NF040873 165 EHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
361-546 |
2.16e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 72.40 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEkPEDYRKLFSAVFTD------------VWLF 428
Cdd:cd03265 19 VSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE-PREVRRRIGIVFQDlsvddeltgwenLYIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 429 DRLLGPEGQQANPALVE--KWLAQLQMSHKLElqdgkilnLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE 506
Cdd:cd03265 98 ARLYGVPGAERRERIDEllDFVGLLEAADRLV--------KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2131440126 507 FYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:cd03265 170 VWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRI 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
343-548 |
2.56e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 75.77 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVF 422
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 423 TDVWLFDR------LLGPEGqqANPALVEKWLAQLQMSHKLELQDGKILNL------KLSKGQKKRVALLLALAEERDII 490
Cdd:PRK13657 416 QDAGLFNRsiedniRVGRPD--ATDEEMRAAAERAQAHDFIERKPDGYDTVvgergrQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 491 LLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
361-546 |
2.87e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.58 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdgkALSAEKPEDYRKLFSAVFTDVWL------------- 427
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW---IFKDEKNKKKTKEKEKVLEKLVIqktrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 428 FDRLLGPEGQQANPAL----VEKWLAQLQMSHKLELQDGKILNLK------------------LSKGQKKRVALLLALAE 485
Cdd:PRK13651 103 IRRRVGVVFQFAEYQLfeqtIEKDIIFGPVSMGVSKEEAKKRAAKyielvgldesylqrspfeLSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 486 ERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDlDNVLEWTKRTIFFKDGKI 243
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
342-548 |
2.98e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDS-AFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFDRLLG-----PEGQQANPALVEKwlaQLQMSHKLE----LQDGkiLN-------LKLSKGQKKRVALLLALA 484
Cdd:PRK11176 422 VSQNVHLFNDTIAnniayARTEQYSREQIEE---AARMAYAMDfinkMDNG--LDtvigengVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 485 EERDIILLDEWAADQDPHFRREFYQVLLPLMQEmgKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
364-546 |
3.13e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.73 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 364 TIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI----LLDGKALSAEKPEDY------------RKLFSAVFT--DV 425
Cdd:PRK13631 48 TFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNpyskkiknfkelRRRVSMVFQfpEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 426 WLF------DRLLGPE--GQQANPA--LVEKWLAQLQMSHK-LELQDgkilnLKLSKGQKKRVALLLALAEERDIILLDE 494
Cdd:PRK13631 128 QLFkdtiekDIMFGPValGVKKSEAkkLAKFYLNKMGLDDSyLERSP-----FGLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 495 WAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:PRK13631 203 PTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-528 |
3.27e-14 |
|
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: 73.55 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSV----GpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGKALSAEKPEDY 414
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkavdG-VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 415 RKL----FSAVFtdvwlfdrllgpegQQA----NPAL-VEKWLAQLQMSHK--------------LEL----QDGKILNL 467
Cdd:COG0444 81 RKIrgreIQMIF--------------QDPmtslNPVMtVGDQIAEPLRIHGglskaeareraielLERvglpDPERRLDR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 468 ---KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD 528
Cdd:COG0444 147 yphELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
361-546 |
3.99e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.05 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL-FSAVFTDVWLFDRL-------L 432
Cdd:COG1129 23 VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNLsvaenifL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 433 GPEgqQANPALV---------EKWLAQLQMShklelqdgkiLNLK-----LSKGQKKRVALLLALAEERDIILLDEWAAD 498
Cdd:COG1129 103 GRE--PRRGGLIdwramrrraRELLARLGLD----------IDPDtpvgdLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2131440126 499 QDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:COG1129 171 LTEREVERLFRIIRRL-KAQGVAIIYISHRlDEVFEIADRVTVLRDGRL 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
359-546 |
4.04e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 359 GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYqPQSGEILLDGKALSAEKPED---YRKLFS----AVFT-DVWLFDR 430
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElarHRAYLSqqqtPPFAmPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 431 LLGPEGqqANPALVEKWLAQLqmSHKLELQD--GKILNlKLSKGQKKRV---ALLL----ALAEERDIILLDEWAADQDP 501
Cdd:PRK03695 92 LHQPDK--TRTEAVASALNEV--AEALGLDDklGRSVN-QLSGGEWQRVrlaAVVLqvwpDINPAGQLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2131440126 502 HFRREFYQvLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:PRK03695 167 AQQAALDR-LLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
361-548 |
5.83e-14 |
|
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: 70.90 E-value: 5.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFD---RL-LGPEG 436
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSgtiRSnLDPFD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 437 QQANPALVEkwlaqlqmshKLELQDGkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQ 516
Cdd:cd03369 107 EYSDEEIYG----------ALRVSEG---GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT 173
|
170 180 190
....*....|....*....|....*....|..
gi 2131440126 517 emGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:cd03369 174 --NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-566 |
6.66e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVkfHYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL-FS 419
Cdd:PRK15439 12 LCARSI--SKQYSGVEVlKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFTDVWLF-------DRLLGPEGQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILL 492
Cdd:PRK15439 90 LVPQEPLLFpnlsvkeNILFGLPKRQASMQKMKQLLAALGCQLDLDSSAG-----SLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 493 DEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRDGK--LSELTGEDRDAASRDAVARTA 566
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQlADRISVMRDGTiaLSGKTADLSTDDIIQAITPAA 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
342-545 |
7.47e-14 |
|
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: 71.65 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG-EILLDGKALSAEKPEDYRK---L 417
Cdd:COG1119 4 LELRNVTVRRGGKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKrigL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 FSAVFTD-------VW------LFDRL-LGPEGQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLAL 483
Cdd:COG1119 83 VSPALQLrfprdetVLdvvlsgFFDSIgLYREPTDEQRERARELLELLGLAHLADRPFG-----TLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 484 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHA-DRLLEMRDGK 545
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
342-546 |
7.96e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.15 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVgpvNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEdyRKLFSAV 421
Cdd:PRK10771 2 LKLTDITWLYHHLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 FTDVWLFDRL-------LGpegqqANPALvekwlaQLQMSHKLELQD--GKI--------LNLKLSKGQKKRVALLLALA 484
Cdd:PRK10771 77 FQENNLFSHLtvaqnigLG-----LNPGL------KLNAAQREKLHAiaRQMgiedllarLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 485 EERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISH--DDHYFIhADRLLEMRDGKL 546
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHslEDAARI-APRSLVVADGRI 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
342-538 |
1.00e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL---- 417
Cdd:PRK13537 8 IDFRNVEKRYGDKLV-VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 --------FSaVFTDVWLFDRLLGPEGQQANpALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDI 489
Cdd:PRK13537 87 qfdnldpdFT-VRENLLVFGRYFGLSAAAAR-ALVPPLLEFAKLENKADAKVG-----ELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2131440126 490 ILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAIShddHYFIHADRL 538
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTT---HFMEEAERL 204
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-550 |
1.58e-13 |
|
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: 70.51 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 364 TIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAeKPE----DY----RKLFSAVFTDVWLFDRLlgpE 435
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-KPQyikaDYegtvRDLLSSITKDFYTHPYF---K 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 436 GQQANPALVEKWLAQlqmshklELQDgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLM 515
Cdd:cd03237 97 TEIAKPLQIEQILDR-------EVPE-------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 2131440126 516 QEMGKTIFAISHdDHYFIH--ADRLLeMRDGKLSELT 550
Cdd:cd03237 163 ENNEKTAFVVEH-DIIMIDylADRLI-VFEGEPSVNG 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
358-545 |
2.08e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.40 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 358 VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALsAEKP--EDYRKLFSAVFTDVWLF------D 429
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-EGLPghQIARMGVVRTFQHVRLFremtviE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 430 RLLGPEGQQAN----------PALVEK----------WLAQLQMshkLELQDGKILNlkLSKGQKKRVALLLALAEERDI 489
Cdd:PRK11300 100 NLLVAQHQQLKtglfsgllktPAFRRAesealdraatWLERVGL---LEHANRQAGN--LAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 490 ILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRDGK 545
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGT 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-538 |
2.46e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.40 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 318 LKKFDLAPFKAEFPRPQAFPNwQTLELRNVKFHYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG 397
Cdd:PRK13536 19 IERKHQGISEAKASIPGSMST-VAIDLAGVSKSYGDKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 398 EILLDG-----KALSAEK-----PE-DYRKLFSAVFTDVWLFDRLLG---PEGQQANPALVEkwLAQLQMSHKLELQDgk 463
Cdd:PRK13536 97 KITVLGvpvpaRARLARArigvvPQfDNLDLEFTVRENLLVFGRYFGmstREIEAVIPSLLE--FARLESKADARVSD-- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 464 ilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAIShddHYFIHADRL 538
Cdd:PRK13536 173 -----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTT---HFMEEAERL 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
314-551 |
2.89e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 314 AFNKLKKFDLAP----FKAEFPRPQAFPNwQTLELRNVKFHYQDSA-FSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLL 388
Cdd:COG0488 285 ALEKLEREEPPRrdktVEIRFPPPERLGK-KVLELEGLSKSYGDKTlLD--DLSLRIDRGDRIGLIGPNGAGKSTLLKLL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 389 TGLYQPQSGEILL-----------DGKALSAEKpedyrklfsavftDVWLFDRLLGPEGQQANpalVEKWLAQLQMSHkl 457
Cdd:COG0488 362 AGELEPDSGTVKLgetvkigyfdqHQEELDPDK-------------TVLDELRDGAPGGTEQE---VRGYLGRFLFSG-- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 458 ELQDGKIlnLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRrefyQVLLPLMQEMGKTIFAISHdDHYFI--HA 535
Cdd:COG0488 424 DDAFKPV--GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL----EALEEALDDFPGTVLLVSH-DRYFLdrVA 496
|
250
....*....|....*.
gi 2131440126 536 DRLLEMRDGKLSELTG 551
Cdd:COG0488 497 TRILEFEDGGVREYPG 512
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
342-546 |
2.92e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 69.14 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYqDSAFSVGPVNLTIRRGeLLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL---- 417
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIgylp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 ----FSAVFTdVWLFDRLLG-----PEGQQanPALVEKWLAQLQMshkLELQDGKIlnLKLSKGQKKRVALLLALAEERD 488
Cdd:cd03264 79 qefgVYPNFT-VREFLDYIAwlkgiPSKEV--KARVDEVLELVNL---GDRAKKKI--GSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 489 IILLDEWAADQDPHFRREFYQVLlplmQEMGKT-IFAIS-H--DDHYFIhADRLLEMRDGKL 546
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLL----SELGEDrIVILStHivEDVESL-CNQVAVLNKGKL 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
360-562 |
3.17e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 360 PVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDyrklfsAVFTDVwlfdrLLGPEGQQA 439
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD------AIRAGI-----MLCPEDRKA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 440 ---------------------NPA---LVEKWLAQL------QMSHKLELQDGKILNlkLSKGQKKRVALLLALAEERDI 489
Cdd:PRK11288 340 egiipvhsvadninisarrhhLRAgclINNRWEAENadrfirSLNIKTPSREQLIMN--LSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 490 ILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHDDHYFIH-ADRLLEMRDGklsELTGE-DRDAASRDAV 562
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGvADRIVVMREG---RIAGElAREQATERQA 488
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
342-548 |
3.75e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.82 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVK--FHYQDSAF------SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALS----AE 409
Cdd:PRK15112 5 LEVRNLSktFRYRTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 410 KPEDYRKLFSAVFTDV-------WLFDRLLGPEGQQANPALVEKWLAQLQMSHKLELQDGKILNLkLSKGQKKRVALLLA 482
Cdd:PRK15112 85 RSQRIRMIFQDPSTSLnprqrisQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM-LAPGQKQRLGLARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 483 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRDGKLSE 548
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVE 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
361-546 |
3.92e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.71 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEiLLDGKALSAEKPEDYRKLFS--------AVFTDVWLfdRLL 432
Cdd:PRK11247 31 LDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEAREDTRLMFQdarllpwkKVIDNVGL--GLK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 433 GPEGQQANPALVEKWLAqlqmSHKLELQDGkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLL 512
Cdd:PRK11247 108 GQWRDAALQALAAVGLA----DRANEWPAA------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 2131440126 513 PLMQEMGKTIFAISHDDHYFIH-ADRLLEMRDGKL 546
Cdd:PRK11247 178 SLWQQHGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
361-551 |
4.53e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKA----LSAEKPED-YRKLFSAV---FTDVW-LFDRL 431
Cdd:COG0488 17 VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigyLPQEPPLDdDLTVLDTVldgDAELRaLEAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 432 LGPEGQQANPALVEKWLAQLQmsHKLELQDG--------KILN-LK------------LSKGQKKRVALLLALAEERDII 490
Cdd:COG0488 97 EELEAKLAEPDEDLERLAELQ--EEFEALGGweaearaeEILSgLGfpeedldrpvseLSGGWRRRVALARALLSEPDLL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 491 LLDE-----------WAADqdpHFRRefYQvllplmqemgKTIFAISHdDHYFIH--ADRLLEMRDGKLSELTG 551
Cdd:COG0488 175 LLDEptnhldlesieWLEE---FLKN--YP----------GTVLVVSH-DRYFLDrvATRILELDRGKLTLYPG 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
342-545 |
4.59e-13 |
|
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: 66.70 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSA-FSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdgkalsaekpedyrklfsa 420
Cdd:cd03221 1 IELENLSKTYGGKLlLK--DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 vftdvwlfdrllgpeGQQANPALVEkwlaqlqmshklelqdgkilnlKLSKGQKKRVALLLALAEERDIILLDEwaadqd 500
Cdd:cd03221 60 ---------------GSTVKIGYFE----------------------QLSGGEKMRLALAKLLLENPNLLLLDE------ 96
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2131440126 501 P--HFRREFYQVLLPLMQEMGKTIFAISHdDHYFIH--ADRLLEMRDGK 545
Cdd:cd03221 97 PtnHLDLESIEALEEALKEYPGTVILVSH-DRYFLDqvATKIIELEDGK 144
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
361-544 |
5.10e-13 |
|
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: 68.51 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDY--RKLFSAVFT--DVWLFDRLL---- 432
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsRNRYSVAYAaqKPWLLNATVeeni 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 433 ---GPEGQQANPALVEKWLAQ-----LQMSHKLELQDGKIlnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 504
Cdd:cd03290 100 tfgSPFNKQRYKAVTDACSLQpdidlLPFGDQTEIGERGI---NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2131440126 505 REFYQV-LLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDG 544
Cdd:cd03290 177 DHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
341-548 |
6.31e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.29 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTD-VWLFDRLLG--PEGQQANPALVEKWLAQLQ-------MSHKLELQDGKILNlKLSKGQKKRVALLLALAEERDII 490
Cdd:PRK10790 420 VQQDpVVLADTFLAnvTLGRDISEEQVWQALETVQlaelarsLPDGLYTPLGEQGN-NLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 491 LLDEWAADQDPHFRREFYQVLLPLMQEmgKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
342-527 |
7.19e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 69.38 E-value: 7.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQ-DSAFS---VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKALSAEKPEDYRK 416
Cdd:PRK13643 2 IKFEKVNYTYQpNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 417 LF-----------SAVFTDVWLFDRLLGPEGQQANPALVEKWLAQLQMSHKLELQDGKILNLKLSKGQKKRVALLLALAE 485
Cdd:PRK13643 82 VRkkvgvvfqfpeSQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2131440126 486 ERDIILLDEWAADQDPHFRREFYQvLLPLMQEMGKTIFAISH 527
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTH 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
342-546 |
8.36e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.99 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHY----QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE--ILLDGKALSAEKPEDYR 415
Cdd:TIGR03269 280 IKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 416 K---------LFS--AVFTDVWLFDRLLGPEGQQANPAL-VEKWLAQLQMSHKLELQDGKILNL---KLSKGQKKRVALL 480
Cdd:TIGR03269 360 RgrakryigiLHQeyDLYPHRTVLDNLTEAIGLELPDELaRMKAVITLKMVGFDEEKAEEILDKypdELSEGERHRVALA 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 481 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:TIGR03269 440 QVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKI 506
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
342-546 |
1.65e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.98 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAL--SAEKPEDYRKLFS 419
Cdd:PRK11432 7 VVLKNITKRFGSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 --AVFTDVWLFD------RLLGpegqqanpalVEKWLAQLQMSHKLELQDgkilnL---------KLSKGQKKRVALLLA 482
Cdd:PRK11432 86 syALFPHMSLGEnvgyglKMLG----------VPKEERKQRVKEALELVD-----LagfedryvdQISGGQQQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 483 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDD-HYFIHADRLLEMRDGKL 546
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQsEAFAVSDTVIVMNKGKI 215
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
361-528 |
2.03e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWL---FD-------- 429
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDvrqvvemg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 430 -----RLLGPEGqQANPALVEKWLAQLQMShklELQDGKILNlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHfr 504
Cdd:PRK09536 102 rtphrSRFDTWT-ETDRAAVERAMERTGVA---QFADRPVTS--LSGGERQRVLLARALAQATPVLLLDEPTASLDIN-- 173
|
170 180
....*....|....*....|....*...
gi 2131440126 505 refYQV-LLPLMQEM---GKTIFAISHD 528
Cdd:PRK09536 174 ---HQVrTLELVRRLvddGKTAVAAIHD 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
361-546 |
2.19e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAL----SAEKPEDYRKLFSAVFTDVWLFDRLLGPEG 436
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyaSKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 437 QQANPALVEKWLAQLQMSHKLELQDGKILNL------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQV 510
Cdd:PRK10253 106 RYPHQPLFTRWRKEDEEAVTKAMQATGITHLadqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 2131440126 511 LLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDlNQACRYASHLIALREGKI 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
364-544 |
2.28e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 364 TIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAlsAEKPEdYRKLFSAVFTDVWLFdrllgpegqQANPAL 443
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI--SYKPQ-YIKPDYDGTVEDLLR---------SITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 444 VEKWLaQLQMSHKLELQdgKIL--NLK-LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGK 520
Cdd:PRK13409 429 GSSYY-KSEIIKPLQLE--RLLdkNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREA 505
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2131440126 521 TIFAISHdDHYFIH--ADRLL----------------EMRDG 544
Cdd:PRK13409 506 TALVVDH-DIYMIDyiSDRLMvfegepgkhghasgpmDMREG 546
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
361-494 |
2.96e-12 |
|
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: 65.63 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGKALSAEKPEDYRKLfsAVFTdvwlfdrllgpeGQQ 438
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARL--GIFL------------AFQ 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2131440126 439 ANPALVEKWLAQLqmshkleLQDgkiLNLKLSKGQKKRVALLLALAEERDIILLDE 494
Cdd:cd03217 85 YPPEIPGVKNADF-------LRY---VNEGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-554 |
4.22e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.65 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAeKPEDYR-KLFSAVFTDVWL------------ 427
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-LPEYKRaKYIGRVFQDPMMgtapsmtieenl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 428 -------FDRLLGPEGQQANPALVEKWLAQLQMShkLELQdgkiLNLK---LSKGQKKRVALLLALAEERDIILLDEWAA 497
Cdd:COG1101 104 alayrrgKRRGLRRGLTKKRRELFRELLATLGLG--LENR----LDTKvglLSGGQRQALSLLMATLTKPKLLLLDEHTA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2131440126 498 DQDPHfRREFyqvllpLMQ-------EMGKTIFAISHDDHYFI-HADRLLEMRDGK-LSELTGEDR 554
Cdd:COG1101 178 ALDPK-TAAL------VLEltekiveENNLTTLMVTHNMEQALdYGNRLIMMHEGRiILDVSGEEK 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
342-533 |
5.41e-12 |
|
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: 65.53 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPED-------Y 414
Cdd:cd03224 1 LEVENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragigY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 415 ----RKLFSA--VFTDVWLFDRLLGPEGQQAN--------PALVEKW--LAQLqmshklelqdgkilnlkLSKGQKKRVA 478
Cdd:cd03224 80 vpegRRIFPEltVEENLLLGAYARRRAKRKARlervyelfPRLKERRkqLAGT-----------------LSGGEQQMLA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 479 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTI--------FAISHDDHYFI 533
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTIllveqnarFALEIADRAYV 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
364-549 |
7.93e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.89 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 364 TIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIllDGKALSAEKP-----------EDY-RKLFSAVFTDVWLFDRL 431
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPqyispdydgtvEEFlRSANTDDFGSSYYKTEI 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 432 LGPegqqanpalvekwlaqlqmshkleLQDGKIL--NLK-LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFY 508
Cdd:COG1245 440 IKP------------------------LGLEKLLdkNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 509 QVLLPLMQEMGKTIFAISHdDHYFIH--ADRLL----------------EMRDGK---LSEL 549
Cdd:COG1245 496 KAIRRFAENRGKTAMVVDH-DIYLIDyiSDRLMvfegepgvhghasgpmDMREGMnrfLKEL 556
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
344-528 |
1.34e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.21 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 344 LRNVKFHYQDSAFSvGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDyrKLFSAVFT 423
Cdd:PRK11000 6 LRNVTKAYGDVVIS-KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 424 DVWLFDRL-------LGPEGQQANPALVEKWLAQ----LQMSHKLELQDGKilnlkLSKGQKKRVALLLALAEERDIILL 492
Cdd:PRK11000 83 SYALYPHLsvaenmsFGLKLAGAKKEEINQRVNQvaevLQLAHLLDRKPKA-----LSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 2131440126 493 DEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD 528
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
301-548 |
1.61e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.79 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 301 AVGA---LPTLLSAQVAFNKLKKFDLAPFKAEfprpqafpnwqTLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGN 377
Cdd:PRK11174 317 AVGAaesLVTFLETPLAHPQQGEKELASNDPV-----------TIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPS 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 378 GSGKSTLAMLLTGlYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLF------DRLLGpeGQQANPALVEKWLAQL 451
Cdd:PRK11174 386 GAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPhgtlrdNVLLG--NPDASDEQLQQALENA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 452 QMSHKLELQ----DGKI--LNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAI 525
Cdd:PRK11174 463 WVSEFLPLLpqglDTPIgdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMV 540
|
250 260
....*....|....*....|...
gi 2131440126 526 SHDDHYFIHADRLLEMRDGKLSE 548
Cdd:PRK11174 541 THQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
361-548 |
3.28e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.62 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG-----EILLDG-KALSAEKP--EDYRKLFSAVFTDVWLF---- 428
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTaRSLSQQKGliRQLRQHVGFVFQNFNLFphrt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 429 ---DRLLGP-----EGQQANPALVEKWLAQLQMSHKlelQDGkiLNLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 500
Cdd:PRK11264 102 vleNIIEGPvivkgEPKEEATARARELLAKVGLAGK---ETS--YPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2131440126 501 PHFRREFYQVLLPLMQEMgKTIFAISHDDHYFIH-ADRLLEMRDGKLSE 548
Cdd:PRK11264 177 PELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
361-544 |
4.04e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTL----AMLLTGLYQPQSgEILLDGKALSAEK--PEDYRKLFS---AVFTDVWLFDRL 431
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITGDKSAGS-HIELLGRTVQREGrlARDIRKSRAntgYIFQQFNLVNRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 432 -------LGPEGQQANPALVEKWLAQLQMSHKLE-LQDGKILNL------KLSKGQKKRVALLLALAEERDIILLDEWAA 497
Cdd:PRK09984 102 svlenvlIGALGSTPFWRTCFSWFTREQKQRALQaLTRVGMVHFahqrvsTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2131440126 498 DQDPHFRREFYQVLLPLMQEMGKTIFAISHD-DHYFIHADRLLEMRDG 544
Cdd:PRK09984 182 SLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQG 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
361-501 |
4.09e-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: 62.95 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAeKPEDYRKLF--------SAVFTDVWLFDRLL 432
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-LPMHKRARLgigylpqeASIFRKLTVEENIL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 433 GpegqqanpALVEKWLAQLQMSHKLE--LQDGKILNLK------LSKGQKKRVALLLALAEERDIILLDEWAADQDP 501
Cdd:cd03218 98 A--------VLEIRGLSKKEREEKLEelLEEFHITHLRkskassLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
361-562 |
4.23e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 4.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL-FSAVFTDVWLFDRLLGPEGQQA 439
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLENLYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 440 NPALVEKWL-------------AQLqMSHKLELQ---DGKILNLKLSKGQKKRVALLLALaeERDIILLDEWAADQDPHF 503
Cdd:PRK09700 104 GRHLTKKVCgvniidwremrvrAAM-MLLRVGLKvdlDEKVANLSISHKQMLEIAKTLML--DAKVIIMDEPTSSLTNKE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 504 RREFYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRDGKlSELTGEDRDAASRDAV 562
Cdd:PRK09700 181 VDYLFLIMNQLRKE-GTAIVYISHKLAEIRRiCDRYTVMKDGS-SVCSGMVSDVSNDDIV 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
361-548 |
4.63e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPED-------------YRKLFSAVFTDVWL 427
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 428 FDRLLGPEGQQANPALV------------EKWLAQLQMShklELQDGKiLNLKLSKGQKKRVALLLALAEERDIILLDEW 495
Cdd:PRK10619 104 WSHMTVLENVMEAPIQVlglskqeareraVKYLAKVGID---ERAQGK-YPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 496 AADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRDGKLSE 548
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHvSSHVIFLHQGKIEE 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
343-527 |
4.98e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.44 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFHYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRK--- 416
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 417 ----------LFSA--VFTDVWLFDRLLGpegqqANPALVEKWLAQLqmshkLELQDgkiLNLK-------LSKGQKKRV 477
Cdd:PRK11153 83 qigmifqhfnLLSSrtVFDNVALPLELAG-----TPKAEIKARVTEL-----LELVG---LSDKadrypaqLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2131440126 478 ALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISH 527
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
276-548 |
8.99e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 276 LGWADTNVAATYSLTLL-FLRTPLlsavGALPTLLS----AQVAFNKLKKFDLAPFKAEFPRPQAFPNWQTLELRNVKFH 350
Cdd:PLN03232 548 LGGDLTPARAFTSLSLFaVLRSPL----NMLPNLLSqvvnANVSLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFS 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 351 YqDSAFS---VGPVNLTIRRGELLFLIGGNGSGKSTL-AMLLTGLYQPQSGEILLDGKAlsAEKPEdYRKLFSAVFTDVW 426
Cdd:PLN03232 624 W-DSKTSkptLSDINLEIPVGSLVAIVGGTGEGKTSLiSAMLGELSHAETSSVVIRGSV--AYVPQ-VSWIFNATVRENI 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 427 LFdrllgpeGQQANPALVEKWLAQLQMSHKLELQDGKILN------LKLSKGQKKRVALLLALAEERDIILLDEWAADQD 500
Cdd:PLN03232 700 LF-------GSDFESERYWRAIDVTALQHDLDLLPGRDLTeigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2131440126 501 PHFRRefyQVLLPLMQE--MGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:PLN03232 773 AHVAH---QVFDSCMKDelKGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
34-192 |
9.15e-11 |
|
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: 62.84 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 34 FIAVMALSLASAALGIGLIAFINvRLIEMTDTSLSVLPeflglLLLLMAVTLGSQLALTTL--------GHHFVFRLRSE 105
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVK-NLIDALSAGGSSGG-----LLALLVALFLLQAVLSALssyllgrtGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 106 FIKRILDTQIERVEQLGSASLLAGLTSDV----RAITIAfvrLPELVQGIILTFGSAAYLAWLSSKMLAVTALWIVITIW 181
Cdd:cd18551 75 LWRRLLRLPVSFFDRRRSGDLVSRVTNDTtllrELITSG---LPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170
....*....|.
gi 2131440126 182 GGFMLVSRVYK 192
Cdd:cd18551 152 IILPLGRRIRK 162
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
358-566 |
9.34e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 358 VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKP------------EDyRK---LFS--- 419
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdairagiayvpED-RKgegLVLdls 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 ----------AVFTDVWLFDRllgpeGQQAnpALVEKWLAQLQMshKLELQDGKILNlkLSKG--QKkrVALLLALAEER 487
Cdd:COG1129 347 irenitlaslDRLSRGGLLDR-----RRER--ALAEEYIKRLRI--KTPSPEQPVGN--LSGGnqQK--VVLAKWLATDP 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 488 DIILLDEwaadqdPhFR-------REFYQvllpLMQEM---GKTIFAISHDDHYFIH-ADRLLEMRDGKlseLTGE-DRD 555
Cdd:COG1129 414 KVLILDE------P-TRgidvgakAEIYR----LIRELaaeGKAVIVISSELPELLGlSDRILVMREGR---IVGElDRE 479
|
250
....*....|.
gi 2131440126 556 AASRDAVARTA 566
Cdd:COG1129 480 EATEEAIMAAA 490
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
362-494 |
1.48e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 362 NLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFsavftdvWL-----FDRLLGPE- 435
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLL-------YLghqpgIKTELTALe 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 436 --------GQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALL-LALAeERDIILLDE 494
Cdd:PRK13538 94 nlrfyqrlHGPGDDEALWEALAQVGLAGFEDVPVR-----QLSAGQQRRVALArLWLT-RAPLWILDE 155
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-548 |
1.49e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 62.79 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRK-- 416
Cdd:COG1135 2 IELENLSKTFPTKGGPVtalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 417 -----------LFSA--VFTDVWLFDRLLGPEGQQANP------ALV------EKWLAQlqmshklelqdgkilnlkLSK 471
Cdd:COG1135 82 rkigmifqhfnLLSSrtVAENVALPLEIAGVPKAEIRKrvaellELVglsdkaDAYPSQ------------------LSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 472 GQKKRVALLLALAEERDIILLDEwaADQ--DPHFRREFYQVLLPLMQEMGKTIFAISHDdhyfIH-----ADRLLEMRDG 544
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDE--ATSalDPETTRSILDLLKDINRELGLTIVLITHE----MDvvrriCDRVAVLENG 217
|
....
gi 2131440126 545 KLSE 548
Cdd:COG1135 218 RIVE 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
358-501 |
1.49e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.45 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 358 VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALS-------AEKPEDYRKLFSAVFTDVWLFDR 430
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplharARRGIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 431 LLG--------PEGQQANPAlvEKWLAQLQMSHkleLQDGkiLNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 501
Cdd:PRK10895 99 LMAvlqirddlSAEQREDRA--NELMEEFHIEH---LRDS--MGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
357-546 |
1.62e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.26 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 357 SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAL---------SAEKPEDYRKLFS--AVFTDV 425
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnldavrqSLGMCPQHNILFHhlTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 426 WLFDRLLGPEGQQANPALvEKWLAQLQMSHKL--ELQDgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF 503
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEM-EAMLEDTGLHHKRneEAQD-------LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2131440126 504 RREFYQVLLPLMQemGKTIFAISHD-DHYFIHADRLLEMRDGKL 546
Cdd:TIGR01257 1097 RRSIWDLLLKYRS--GRTIIMSTHHmDEADLLGDRIAIISQGRL 1138
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
341-548 |
2.34e-10 |
|
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: 63.30 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:COG5265 357 EVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFDRLLG-------PEgqqANPALVEKW--LAQLqmshklelqDGKILN-------------LKLSKGQKKRVA 478
Cdd:COG5265 437 VPQDTVLFNDTIAyniaygrPD---ASEEEVEAAarAAQI---------HDFIESlpdgydtrvgergLKLSGGEKQRVA 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 479 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
341-548 |
2.54e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 60.80 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKA--LSAE-KPEDYRKL 417
Cdd:PRK11124 2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTpSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 418 ---FSAVFT--DVW--------LFD---RLLGPEGQQANpALVEKWLAQLQMSHKLELqdgkiLNLKLSKGQKKRVALLL 481
Cdd:PRK11124 81 rrnVGMVFQqyNLWphltvqqnLIEapcRVLGLSKDQAL-ARAEKLLERLRLKPYADR-----FPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 482 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQEMGKTIFAISHD-DHYFIHADRLLEMRDGKLSE 548
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEvEVARKTASRVVYMENGHIVE 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-527 |
3.19e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.70 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQ--PQ---SGEILLDGKALSAEKPEDYRK 416
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDG-VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 417 LFSAVFT------DVWLFDRL-LGP----------EGQQANPALVEKwlAQL--QMSHKLELQDGKilnlkLSKGQKKRV 477
Cdd:PRK14247 83 RVQMVFQipnpipNLSIFENVaLGLklnrlvkskkELQERVRWALEK--AQLwdEVKDRLDAPAGK-----LSGGQQQRL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2131440126 478 ALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMgkTIFAISH 527
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTH 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
361-555 |
6.04e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 6.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILldgkalsAEK-----PEDYRKLFSAVFTDVWLFDrllgpE 435
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------AERsiayvPQQAWIMNATVRGNILFFD-----E 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 436 GQQANPALV------EKWLAQLqmSHKLELQDG-KILNLklSKGQKKRVALLLALAEERDIILLDEWAADQDPHF-RREF 507
Cdd:PTZ00243 747 EDAARLADAvrvsqlEADLAQL--GGGLETEIGeKGVNL--SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVV 822
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2131440126 508 YQVLLPLMQemGKTIFAISHDDHYFIHADRLLEMRDGKLsELTGEDRD 555
Cdd:PTZ00243 823 EECFLGALA--GKTRVLATHQVHVVPRADYVVALGDGRV-EFSGSSAD 867
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
361-529 |
7.82e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 7.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLY--QPQSGEILLDGKALSAEKPedyrkLFSAVF--TDVWLFDRLLGPEG 436
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS-----LIDAIGrkGDFKDAVELLNAVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 437 QQANPALVEKWlaqlqmSHklelqdgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQ 516
Cdd:COG2401 124 LSDAVLWLRRF------KE-------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLAR 184
|
170
....*....|...
gi 2131440126 517 EMGKTIFAISHDD 529
Cdd:COG2401 185 RAGITLVVATHHY 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
341-528 |
7.84e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.90 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDSAFSVgpvnltiRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG--------KALSAEKP- 411
Cdd:PRK15056 13 TVTWRNGHTALRDASFTV-------PGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqptrqalqKNLVAYVPq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 412 -EDYRKLFSAVFTDVWLFDRLlGPEGQQANP-----ALVEKWLAQLQMSHKLELQDGKilnlkLSKGQKKRVALLLALAE 485
Cdd:PRK15056 86 sEEVDWSFPVLVEDVVMMGRY-GHMGWLRRAkkrdrQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2131440126 486 ERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHD 528
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHN 201
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-494 |
1.03e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEdYRKLFSAVF---TDVWlFD-------R 430
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKE-FARRIGVVFgqrSQLW-WDlpaidsfR 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 431 LLG-----PEgqqanpALVEKWLAQLqmSHKLELQDgkILNL---KLSKGQKKRVALLLALAEERDIILLDE 494
Cdd:COG4586 119 LLKaiyriPD------AEYKKRLDEL--VELLDLGE--LLDTpvrQLSLGQRMRCELAAALLHRPKILFLDE 180
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
340-565 |
1.33e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 340 QTLELRNVKFhyQDSAFSVGPVNLTIRRGELLFLIGGNGSGKS-----TLAMLLTGLYQpQSGEILLDGKALSAEK---- 410
Cdd:PRK10418 3 QQIELRNIAL--QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVAPCAlrgr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 411 -----PEDYRKLFSAVFTDVWLFDRLLGPEGQQANPAlvekwlaqlQMSHKLE---LQD-GKILNL---KLSKGQKKRVA 478
Cdd:PRK10418 80 kiatiMQNPRSAFNPLHTMHTHARETCLALGKPADDA---------TLTAALEavgLENaARVLKLypfEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 479 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRDGKLSElTGEDRD-- 555
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVE-QGDVETlf 229
|
250
....*....|
gi 2131440126 556 AASRDAVART 565
Cdd:PRK10418 230 NAPKHAVTRS 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
361-566 |
1.39e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDyrKLFSAVftdVWLfdrllgPEGQQAN 440
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ--RLARGL---VYL------PEDRQSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 441 PALVEK----------------WLAQLQMSHKLElQDGKILNLK----------LSKGQKKRVALLLALAEERDIILLDE 494
Cdd:PRK15439 351 GLYLDAplawnvcalthnrrgfWIKPARENAVLE-RYRRALNIKfnhaeqaartLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 495 WAADQDPHFRREFYQVLLPLMQEMGKTIFaISHDDHYFIH-ADRLLEMRDGKLS-ELTGEdrdAASRDAVARTA 566
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVLF-ISSDLEEIEQmADRVLVMHQGEISgALTGA---AINVDTIMRLA 499
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
342-494 |
1.39e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLF--- 418
Cdd:PRK13540 2 LDVIELDFDYHDQPL-LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCfvg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2131440126 419 --SAVFTDVWLFDRLLGPEGQQANPALVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILLDE 494
Cdd:PRK13540 81 hrSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCG-----LLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
358-548 |
1.53e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 60.47 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 358 VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGKALSAEKPEDYRKLFSA---VFTDVW-------- 426
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRPLRRRmqvVFQDPFgslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 427 --------LfdRLLGPE-GQQANPALVEKWLAQLQMS--------HklelqdgkilnlKLSKGQKKRVALLLALAEERDI 489
Cdd:COG4172 381 vgqiiaegL--RVHGPGlSAAERRARVAEALEEVGLDpaarhrypH------------EFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 490 ILLDEWAADQDPHFRREFYQVLLPLMQEMGKT-IFaISHDdhyfIH-----ADRLLEMRDGKLSE 548
Cdd:COG4172 447 LVLDEPTSALDVSVQAQILDLLRDLQREHGLAyLF-ISHD----LAvvralAHRVMVMKDGKVVE 506
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
361-530 |
1.77e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRkLFSAVFTDVWLFDRLL-GPEGQQA 439
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY-LDTTLPLTVNRFLRLRpGTKKEDI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 440 NPAlvekwLAQLQMSHKLE--LQdgkilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQE 517
Cdd:PRK09544 102 LPA-----LKRVQAGHLIDapMQ-------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
170
....*....|...
gi 2131440126 518 MGKTIFAISHDDH 530
Cdd:PRK09544 170 LDCAVLMVSHDLH 182
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
283-500 |
1.79e-09 |
|
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: 60.73 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 283 VAATYSLTLLFLRTPLLSAVGALPTLLsaqVAFNKLKKFDL----APFKAEFPRP-QAFPNWQTLELRNVKFHYQ-DSAF 356
Cdd:TIGR00957 1224 LSVSYSLQVTFYLNWLVRMSSEMETNI---VAVERLKEYSEtekeAPWQIQETAPpSGWPPRGRVEFRNYCLRYReDLDL 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 357 SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFD---RL-L 432
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSgslRMnL 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 433 GPEGQQANPalvEKWLAqLQMSH----------KLELQ--DGkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 500
Cdd:TIGR00957 1381 DPFSQYSDE---EVWWA-LELAHlktfvsalpdKLDHEcaEG---GENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
285-549 |
3.85e-09 |
|
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: 59.96 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 285 ATYSLTLL-FLRTPLlsavGALPTLLS----AQVAFNKLKKF----DLAPFKAEfPRPQAFPNWQTLELRNVKFHY-QDS 354
Cdd:TIGR00957 576 AFVSLALFnILRFPL----NILPMVISsivqASVSLKRLRIFlsheELEPDSIE-RRTIKPGEGNSITVHNATFTWaRDL 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 355 AFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAlsAEKPEdyrklfSAVFTDVWLFDRLLGp 434
Cdd:TIGR00957 651 PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AYVPQ------QAWIQNDSLRENILF- 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 435 eGQQANPALVEKWLAQLQMSHKLELQDG--------KILNLklSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE 506
Cdd:TIGR00957 722 -GKALNEKYYQQVLEACALLPDLEILPSgdrteigeKGVNL--SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2131440126 507 -FYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRDGKLSEL 549
Cdd:TIGR00957 799 iFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEM 842
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
361-494 |
4.05e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.81 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKP---------EDYRKLFSAVFTDVWLFDRL 431
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeachylghRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 432 LGPEGQQANPAlvekwLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILLDE 494
Cdd:PRK13539 101 LGGEELDIAAA-----LEAVGLAPLAHLPFG-----YLSAGQKRRVALARLLVSNRPIWILDE 153
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
252-548 |
4.23e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 252 LSAVNwsnIMMLGAIGLV-----FWMANGLGWADTNVAATYSLTLL-FLRTPLLsavgALPTLLS----AQVAFNKLKKF 321
Cdd:PLN03130 522 LSAFN---SFILNSIPVLvtvvsFGVFTLLGGDLTPARAFTSLSLFaVLRFPLF----MLPNLITqavnANVSLKRLEEL 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 322 DLAPFKAEFPRPQAFPNWQTLELRNVKFHYQDSA--FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-GE 398
Cdd:PLN03130 595 LLAEERVLLPNPPLEPGLPAISIKNGYFSWDSKAerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdAS 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 399 ILLDGKAlsAEKPEdYRKLFSAVFTDVWLFdrllgpeGQQANPALVEKWLAQLQMSHKLELQDGKILN------LKLSKG 472
Cdd:PLN03130 675 VVIRGTV--AYVPQ-VSWIFNATVRDNILF-------GSPFDPERYERAIDVTALQHDLDLLPGGDLTeigergVNISGG 744
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 473 QKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPlmQEM-GKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:PLN03130 745 QKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK--DELrGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
341-413 |
9.03e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.55 E-value: 9.03e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 341 TLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPED 413
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD 75
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
342-549 |
1.04e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSA--FS-------VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAL---SAE 409
Cdd:PRK11308 6 LQAIDLKKHYPVKRglFKperlvkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 410 KPEDYRKLFSAVFTDVWlfdRLLGPE---GQQ-ANPALVEKWLAQLQMSHKLeLQDGKILNLK----------LSKGQKK 475
Cdd:PRK11308 86 AQKLLRQKIQIVFQNPY---GSLNPRkkvGQIlEEPLLINTSLSAAERREKA-LAMMAKVGLRpehydryphmFSGGQRQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 476 RVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRDGKLSEL 549
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEK 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
341-546 |
1.36e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.95 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDY-RKLfs 419
Cdd:PRK10575 11 TFALRNVSFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 avftdVWLFDRLLGPEGQQANpALVE----KW---LAQLQMSHKLELQDG-KILNLK---------LSKGQKKRVALLLA 482
Cdd:PRK10575 88 -----AYLPQQLPAAEGMTVR-ELVAigryPWhgaLGRFGAADREKVEEAiSLVGLKplahrlvdsLSGGERQRAWIAML 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 483 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFI-HADRLLEMRDGKL 546
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEM 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
361-494 |
1.83e-08 |
|
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: 54.81 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA-----------VFTDVWLFD 429
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLghapgikttlsVLENLRFWH 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 430 RLLGPEGqqanpalVEKWLAQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILLDE 494
Cdd:cd03231 99 ADHSDEQ-------VEEALARVGLNGFEDRPVA-----QLSAGQQRRVALARLLLSGRPLWILDE 151
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
342-549 |
2.02e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.25 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQ---DSAF---------SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAL--- 406
Cdd:PRK15079 9 LEVADLKVHFDikdGKQWfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgm 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 407 SAEKPEDYRKLFSAVFTDvwlfdrllgPEGqQANPAL-VEKWLAQ-LQMSH----KLELQD---------GKILNL---- 467
Cdd:PRK15079 89 KDDEWRAVRSDIQMIFQD---------PLA-SLNPRMtIGEIIAEpLRTYHpklsRQEVKDrvkammlkvGLLPNLinry 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 468 --KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLEMRDG 544
Cdd:PRK15079 159 phEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLG 238
|
....*
gi 2131440126 545 KLSEL 549
Cdd:PRK15079 239 HAVEL 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
342-417 |
2.07e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 2.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL 417
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
368-528 |
2.19e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 368 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---ALSAEKPEDYRKLFSAVFTDVW-----------------L 427
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYasldprqtvgdsimeplR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 428 FDRLLGPEGQQANPAlvekWLAQ---LQMSHKLELQDgkilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 504
Cdd:PRK10261 430 VHGLLPGKAAAARVA----WLLErvgLLPEHAWRYPH------EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180
....*....|....*....|....
gi 2131440126 505 REFYQVLLPLMQEMGKTIFAISHD 528
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHD 523
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
361-406 |
2.34e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 2.34e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAL 406
Cdd:PRK11288 23 ISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM 68
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
361-545 |
2.44e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYqPQ---SGEILLDGKALSAEKPEDY-RKLFSAVFTDVWLFDRL----- 431
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKELsvlen 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 432 --LGPE----GQQANPALV---EKWLAQLQMSHKLELqdgKILNLKLskGQKKRVALLLALAEERDIILLDEWAAdqdPH 502
Cdd:PRK13549 103 ifLGNEitpgGIMDYDAMYlraQKLLAQLKLDINPAT---PVGNLGL--GQQQLVEIAKALNKQARLLILDEPTA---SL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2131440126 503 FRREFyQVLLPLMQEM---GKTIFAISHD-DHYFIHADRLLEMRDGK 545
Cdd:PRK13549 175 TESET-AVLLDIIRDLkahGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
361-546 |
6.36e-08 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 52.94 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGKALSaekPEDYRKLFSAVFTDVWLFDRLLGPEgqq 438
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHPTLTVRE--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 439 anpalvekwlaQLQMSHKLElqdgkilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPhFRREFYQVLLPLMQEM 518
Cdd:cd03213 102 -----------TLMFAAKLR---------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS-SSALQVMSLLRRLADT 160
|
170 180 190
....*....|....*....|....*....|
gi 2131440126 519 GKTIFAISHDDHYFIHA--DRLLEMRDGKL 546
Cdd:cd03213 161 GRTIICSIHQPSSEIFElfDKLLLLSQGRV 190
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
342-494 |
6.78e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGKALSAEKPED------ 413
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRG-LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 414 -----YRKLFSAVFTDVWLFDRLLGPEGQQANPAL--------VEKWLAQLQMSHKLELQDgkiLNLKLSKGQKKRVALL 480
Cdd:PRK09580 81 fmafqYPVEIPGVSNQFFLQTALNAVRSYRGQEPLdrfdfqdlMEEKIALLKMPEDLLTRS---VNVGFSGGEKKRNDIL 157
|
170
....*....|....
gi 2131440126 481 LALAEERDIILLDE 494
Cdd:PRK09580 158 QMAVLEPELCILDE 171
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
349-544 |
7.13e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.10 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 349 FHY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWL 427
Cdd:PRK10789 321 FTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 428 FDRLLGpegqqANPALVEKWLAQLQMSHKLELQD--GKILNLK-------------LSKGQKKRVALLLALAEERDIILL 492
Cdd:PRK10789 401 FSDTVA-----NNIALGRPDATQQEIEHVARLASvhDDILRLPqgydtevgergvmLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 493 DEWAADQDPhfrREFYQVLLPLMQ-EMGKTIFAISHDDHYFIHADRLLEMRDG 544
Cdd:PRK10789 476 DDALSAVDG---RTEHQILHNLRQwGEGRTVIISAHRLSALTEASEILVMQHG 525
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
361-417 |
7.13e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.88 E-value: 7.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTG--LYQPQSGEILLDGKALSAEKPEDYRKL 417
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL 84
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
335-530 |
1.02e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.71 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 335 AFPNWQTLELRNVKFHYqdsafSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILLDGKALSAEKPED- 413
Cdd:PRK15134 284 AFPIRKGILKRTVDHNV-----VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQl 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 414 --YRKLFSAVFTDvwlfdrllgPEGqQANPAL-VEKWLAQ-LQMSHKL---ELQDGKILNL----------------KLS 470
Cdd:PRK15134 358 lpVRHRIQVVFQD---------PNS-SLNPRLnVLQIIEEgLRVHQPTlsaAQREQQVIAVmeevgldpetrhrypaEFS 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 471 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDH 530
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
361-545 |
1.03e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALS-AEK----PEDYRKLfSAVFTDVWLFdrllgpe 435
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKgiclPPEKRRI-GYVFQDARLF------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 436 gqqanPAL-VEKWLaQLQMSHKLELQDGKILNL------------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 502
Cdd:PRK11144 89 -----PHYkVRGNL-RYGMAKSMVAQFDKIVALlgieplldrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2131440126 503 FRREfyqvLLPLMQEMGKT----IFAISHDDHYFIH-ADRLLEMRDGK 545
Cdd:PRK11144 163 RKRE----LLPYLERLAREinipILYVSHSLDEILRlADRVVVLEQGK 206
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
361-546 |
1.81e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.18 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPED---YRKLFSAVFTD-VWLFDRLLgpEG 436
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhHLLMDRTV--YD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 437 QQANPALVEKWLAQ---LQMSHKLE----LQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDphfrREFYQ 509
Cdd:PRK10908 99 NVAIPLIIAGASGDdirRRVSAALDkvglLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2131440126 510 VLLPLMQE---MGKTIFAISHDDHYFIHAD-RLLEMRDGKL 546
Cdd:PRK10908 175 GILRLFEEfnrVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
342-545 |
1.86e-07 |
|
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: 53.68 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNV--KFhyqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYqPQ---SGEILLDGKALSAEKPEDY-R 415
Cdd:TIGR02633 2 LEMKGIvkTF---GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 416 KLFS------------AVFTDVWLFDRLLGPEGQQANPALV---EKWLAQLQMShklELQDGKILNlKLSKGQKKRVALL 480
Cdd:TIGR02633 78 AGIViihqeltlvpelSVAENIFLGNEITLPGGRMAYNAMYlraKNLLRELQLD---ADNVTRPVG-DYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 481 LALAEERDIILLDEWAADqdphFRREFYQVLLPLMQEM---GKTIFAISHD-DHYFIHADRLLEMRDGK 545
Cdd:TIGR02633 154 KALNKQARLLILDEPSSS----LTEKETEILLDIIRDLkahGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
81-272 |
1.96e-07 |
|
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: 52.94 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 81 MAVTLGSQLALTTLGHHFVFRLRSEFIKRILDTQIERVEQLGSASLLAGLTSDVRAITIAFVR-LPELVQGIILTFGSAA 159
Cdd:cd07346 53 ALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 160 YLAWLSSKMLAVTALWIVITIWGGFMLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKEL-TLNRERAE-HIFNHLyipdA 237
Cdd:cd07346 133 ILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVkAFAAEEREiERFREA----N 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 2131440126 238 REYRHHIIRADTfhLSAVNWSNIMMLGAIG--LVFWM 272
Cdd:cd07346 209 RDLRDANLRAAR--LSALFSPLIGLLTALGtaLVLLY 243
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
361-494 |
2.33e-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: 51.89 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGKALsaeKPEDYRKLFSAVFTDVWLFD-------- 429
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPgltvretl 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 430 ----RLLGPEgQQANPALVEKWlAQLQMSHkleLQDGKILNLK---LSKGQKKRVALLLALAEERDIILLDE 494
Cdd:cd03234 103 tytaILRLPR-KSSDAIRKKRV-EDVLLRD---LALTRIGGNLvkgISGGERRRVSIAVQLLWDPKVLILDE 169
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
349-527 |
2.43e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 349 FHYqdsafSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAlsaekpedyrklfSAVFTDVWLF 428
Cdd:PRK13545 36 YHY-----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------------ALIAISSGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 429 DRLLGPEGQQANPALVEKWLAQLQ--MSHKLELQD-GKILNLKL---SKGQKKRVALLLALAEERDIILLDEWAADQDPH 502
Cdd:PRK13545 98 GQLTGIENIELKGLMMGLTKEKIKeiIPEIIEFADiGKFIYQPVktySSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180
....*....|....*....|....*...
gi 2131440126 503 FRREfyqvLLPLM---QEMGKTIFAISH 527
Cdd:PRK13545 178 FTKK----CLDKMnefKEQGKTIFFISH 201
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
361-545 |
2.88e-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: 52.80 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAL-SAEKPED---YRKLFSAVFTDVWLFDRL----- 431
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFlppHRRRIGYVFQEARLFPHLsvrgn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 432 ----LGPEGQQANPALVEKWLAQLQMSHKLELQDGKilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREf 507
Cdd:COG4148 98 llygRKRAPRAERRISFDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE- 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2131440126 508 yqvLLP----LMQEMGKTIFAISHDdhyfIH-----ADRLLEMRDGK 545
Cdd:COG4148 172 ---ILPylerLRDELDIPILYVSHS----LDevarlADHVVLLEQGR 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
342-546 |
3.05e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.80 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSA-EKPEDYRKLFSA 420
Cdd:PRK11614 6 LSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFDRLLGPEGQQANPALVEKWLAQLQMSHKLE----LQDGKILNL-KLSKGQKKRVALLLALAEERDIILLDEW 495
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYElfprLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 496 AADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRDGKL 546
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKlADRGYVLENGHV 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
348-527 |
3.67e-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: 53.48 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 348 KFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL-----FSAV- 421
Cdd:TIGR01257 1945 KVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgycpqFDAId 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 422 -----FTDVWLFDRLLGPEGQQANPalVEKWLAQlqmSHKLELQDGKILNlKLSKGQKKRVALLLALAEERDIILLDEWA 496
Cdd:TIGR01257 2025 dlltgREHLYLYARLRGVPAEEIEK--VANWSIQ---SLGLSLYADRLAG-TYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190
....*....|....*....|....*....|.
gi 2131440126 497 ADQDPHFRREFYQVLLPLMQEmGKTIFAISH 527
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSIIRE-GRAVVLTSH 2128
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
361-559 |
3.90e-07 |
|
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: 51.78 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAlsaekpeDYRKLFSAVFTDVWLFDRLLGPEGQQAN 440
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI-------SFSSQFSWIMPGTIKENIIFGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 441 PALVEKwLAQLQMS-HKLELQDGKIL---NLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE-FYQVLLPLM 515
Cdd:cd03291 129 YKSVVK-ACQLEEDiTKFPEKDNTVLgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEiFESCVCKLM 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2131440126 516 QEmgKTIFAISHDDHYFIHADRLLEMRDGK------LSELTGEDRDAASR 559
Cdd:cd03291 208 AN--KTRILVTSKMEHLKKADKILILHEGSsyfygtFSELQSLRPDFSSK 255
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
361-559 |
4.32e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK-----ALSAEKPEDYRK--LFSAVFtDVWLFDRLLg 433
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRisfspQTSWIMPGTIKDniIFGLSY-DEYRYTSVI- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 434 pegqqaNPALVEKWLAQLQMSHKLELQDGKIlnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE-FYQVLL 512
Cdd:TIGR01271 523 ------KACQLEEDIALFPEKDKTVLGEGGI---TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEiFESCLC 593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 513 PLMqeMGKTIFAISHDDHYFIHADRLLEMRD------GKLSELTGEDRDAASR 559
Cdd:TIGR01271 594 KLM--SNKTRILVTSKLEHLKKADKILLLHEgvcyfyGTFSELQAKRPDFSSL 644
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-548 |
4.95e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 52.38 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRN--VKFHYQDSAFS-VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ----SGEILLDGKALSAEKPEDY 414
Cdd:COG4172 7 LSVEDlsVAFGQGGGTVEaVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 415 RKL----FSAVFtdvwlfdrllgpegQQA----NPAL-VEKwlaqlQMSHKLELQDG--------KILNL---------- 467
Cdd:COG4172 87 RRIrgnrIAMIF--------------QEPmtslNPLHtIGK-----QIAEVLRLHRGlsgaaaraRALELlervgipdpe 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 468 --------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHD----DHYfihA 535
Cdd:COG4172 148 rrldayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvvRRF---A 224
|
250
....*....|...
gi 2131440126 536 DRLLEMRDGKLSE 548
Cdd:COG4172 225 DRVAVMRQGEIVE 237
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
343-566 |
6.42e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 6.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 343 ELRNVKFH----YQDSAFSVgpvnltiRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLF 418
Cdd:PRK09700 267 EVRNVTSRdrkkVRDISFSV-------CRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 419 SAVFT----DVWLFDRLLGPEGQQANPAL-VEKW-----LAQLQMSHKLELQDGKILNLK----------LSKGQKKRVA 478
Cdd:PRK09700 340 MAYITesrrDNGFFPNFSIAQNMAISRSLkDGGYkgamgLFHEVDEQRTAENQRELLALKchsvnqniteLSGGNQQKVL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 479 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFIHA-DRLLEMRDGKLSELTgEDRDAA 557
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVcDRIAVFCEGRLTQIL-TNRDDM 497
|
....*....
gi 2131440126 558 SRDAVARTA 566
Cdd:PRK09700 498 SEEEIMAWA 506
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
361-527 |
6.88e-07 |
|
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: 52.11 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEIL----LDGKALSAEKPE------------------DYRK 416
Cdd:TIGR03269 19 ISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvaLCEKCGYVERPSkvgepcpvcggtlepeevDFWN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 417 LFSAVFTDVW-----LFDRL-------------------LGPEGQQANPALVEkWLAQLQMSHKLELqdgkiLNLKLSKG 472
Cdd:TIGR03269 99 LSDKLRRRIRkriaiMLQRTfalygddtvldnvlealeeIGYEGKEAVGRAVD-LIEMVQLSHRITH-----IARDLSGG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2131440126 473 QKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISH 527
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
361-404 |
8.85e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.71 E-value: 8.85e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYqPQ---SGEILLDGK 404
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGE 65
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-494 |
9.19e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.42 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDS-AFSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLY--QPQ---SGEILLDGKALSAEK--PED 413
Cdd:COG1117 12 IEVRNLNVYYGDKqALK--DINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDGEDIYDPDvdVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 414 YRKLFSAVFtdvwlfdrllgpegQQANP-------------------------ALVEKWL--AQL--QMSHKLElQDGki 464
Cdd:COG1117 90 LRRRVGMVF--------------QKPNPfpksiydnvayglrlhgikskseldEIVEESLrkAALwdEVKDRLK-KSA-- 152
|
170 180 190
....*....|....*....|....*....|
gi 2131440126 465 lnLKLSKGQKKRVALLLALAEERDIILLDE 494
Cdd:COG1117 153 --LGLSGGQQQRLCIARALAVEPEVLLMDE 180
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
341-556 |
1.27e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 51.35 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdgkalsaekPEDYRKLF-- 418
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFlp 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 419 -SAVFTDVWLFDRLLGPEG-QQANPALVEKWLAQLQMSHKLE-LQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEW 495
Cdd:COG4178 433 qRPYLPLGTLREALLYPATaEAFSDAELREALEAVGLGHLAErLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 496 AADQDPHFRREFYQVLLPLMQEMgkTIFAISHDDHYFIHADRLLEMRDGKLSELTGEDRDA 556
Cdd:COG4178 513 TSALDEENEAALYQLLREELPGT--TVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
361-404 |
1.41e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 1.41e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK 404
Cdd:PRK10982 17 VNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK 60
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
361-526 |
1.70e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKL------FS-----AVFTDVWLFD 429
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVgymsqaFSlygelTVRQNLELHA 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 430 RLLGPEGQQANPALVEkwlaqlqMSHKLELQDgkILNLK---LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE 506
Cdd:NF033858 365 RLFHLPAAEIAARVAE-------MLERFDLAD--VADALpdsLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180
....*....|....*....|
gi 2131440126 507 FYQVLLPLMQEMGKTIFaIS 526
Cdd:NF033858 436 FWRLLIELSREDGVTIF-IS 454
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
326-555 |
2.16e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 326 FKAEFPRPQAFPNWQTLELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL----- 400
Cdd:PLN03073 493 YKFEFPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakv 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 401 ---------LDGKALSAEKPEDYRKLFSAVftdvwlfdrllgPEGQqanpalVEKWLAQLQMSHKLELQDgkilNLKLSK 471
Cdd:PLN03073 573 rmavfsqhhVDGLDLSSNPLLYMMRCFPGV------------PEQK------LRAHLGSFGVTGNLALQP----MYTLSG 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 472 GQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLpLMQemgKTIFAISHDDHYFIHA-DRLLEMRDGKLSELT 550
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQ---GGVLMVSHDEHLISGSvDELWVVSEGKVTPFH 706
|
....*
gi 2131440126 551 GEDRD 555
Cdd:PLN03073 707 GTFHD 711
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-542 |
2.30e-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: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 367 RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdgkaLSAEKPEDYrklfsavftdvwlfdrllgpegqqanpalvek 446
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----IDGEDILEE-------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 447 wlaqlqmsHKLELQDGKILNLKLSKGQKKRVALLLALAEER--DIILLDEWAADQDPHFRR-----EFYQVLLPLMQEMG 519
Cdd:smart00382 45 --------VLDQLLLIIVGGKKASGSGELRLRLALALARKLkpDVLILDEITSLLDAEQEAlllllEELRLLLLLKSEKN 116
|
170 180
....*....|....*....|...
gi 2131440126 520 KTIFAISHDDHYFIhaDRLLEMR 542
Cdd:smart00382 117 LTVILTTNDEKDLG--PALLRRR 137
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
361-527 |
3.99e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLT--GLYQPQ---SGEILLDGKALSAEKPE--DYRKLFSAVFTDVWLFD---- 429
Cdd:PRK14239 24 VSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQPNPFPmsiy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 430 -------RLLGPEGQQANPALVEKWL--AQLQMSHKLELQDGKilnLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 500
Cdd:PRK14239 104 envvyglRLKGIKDKQVLDEAVEKSLkgASIWDEVKDRLHDSA---LGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
170 180
....*....|....*....|....*..
gi 2131440126 501 PHFRREFYQVLLPLMQEMgkTIFAISH 527
Cdd:PRK14239 181 PISAGKIEETLLGLKDDY--TMLLVTR 205
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
342-546 |
4.72e-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: 48.31 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VFTDVWLFD----RLLGPEGQQANPAL------------VEKWLAQLQmshkLELQDGKILnlkLSKGQKKRVALLLALA 484
Cdd:cd03289 82 IPQKVFIFSgtfrKNLDPYGKWSDEEIwkvaeevglksvIEQFPGQLD----FVLVDGGCV---LSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2131440126 485 EERDIILLDEWAADQDPhfrrEFYQVLLPLMQE--MGKTIFAISHDDHYFIHADRLLEMRDGKL 546
Cdd:cd03289 155 SKAKILLLDEPSAHLDP----ITYQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
342-541 |
5.17e-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: 46.76 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgkalsaEKPEDYRKLF--- 418
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEGEDLLFlpq 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 419 SAVFTDVWLFDRLLGPegqqanpalvekWlaqlqmshklelqdgkilNLKLSKGQKKRVALLLALAEERDIILLDEWAAD 498
Cdd:cd03223 72 RPYLPLGTLREQLIYP------------W------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2131440126 499 QDPHFRREFYQVLlplmQEMGKTIFAISHDDHYFIHADRLLEM 541
Cdd:cd03223 122 LDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDL 160
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
396-527 |
5.30e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 396 SGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFDRLL------GPEG-------QQANPALVEKWLAQLQMSHKLELQD- 461
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIyenikfGKEDatredvkRACKFAAIDEFIESLPNKYDTNVGPy 1355
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2131440126 462 GKilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISH 527
Cdd:PTZ00265 1356 GK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
359-501 |
6.53e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 359 GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK-ALSAEKPE--DYRKLFSAVFTDVWLFDRL---L 432
Cdd:PRK13543 28 GPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtATRGDRSRfmAYLGHLPGLKADLSTLENLhflC 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2131440126 433 GPEGQQA----NPALVEKWLAQLQMShklelqdgkiLNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 501
Cdd:PRK13543 108 GLHGRRAkqmpGSALAIVGLAGYEDT----------LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
365-538 |
8.53e-06 |
|
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: 46.41 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 365 IRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAeKPEdyrklfsavftdvwlfdrllgpegqqanpalv 444
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY-KPQ-------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 445 ekwlaqlqmshklelqdgkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFA 524
Cdd:cd03222 69 ---------------------YIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALV 127
|
170
....*....|....
gi 2131440126 525 ISHDdhyFIHADRL 538
Cdd:cd03222 128 VEHD---LAVLDYL 138
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
334-402 |
9.39e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 9.39e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2131440126 334 QAFPNWQTLELRNVKFHYqDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD 402
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHY-DTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN 445
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
341-559 |
1.26e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDS-AFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFS 419
Cdd:PTZ00243 1308 SLVFEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 420 AVFTDVWLFDrllGPEGQQANPAL----VEKWLAqlqmshkLELQ-------------DGKILN--LKLSKGQKKRVALL 480
Cdd:PTZ00243 1388 MIPQDPVLFD---GTVRQNVDPFLeassAEVWAA-------LELVglrervasesegiDSRVLEggSNYSVGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 481 LALAEE-RDIILLDEWAADQDPHFRRefyQVLLPLMQEMGK-TIFAISHDDHYFIHADRLLEMRDGKLSELtGEDRDAAS 558
Cdd:PTZ00243 1458 RALLKKgSGFILMDEATANIDPALDR---QIQATVMSAFSAyTVITIAHRLHTVAQYDKIIVMDHGAVAEM-GSPRELVM 1533
|
.
gi 2131440126 559 R 559
Cdd:PTZ00243 1534 N 1534
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
347-528 |
1.39e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 347 VKFHYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKAlsaekpedyrklfSAVFTDVW 426
Cdd:PRK13546 29 IPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV-------------SVIAISAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 427 LFDRLLGPEGQQANPALV---EKWLAQLqMSHKLELQD-GKILNL---KLSKGQKKRVALLLALAEERDIILLDEWAADQ 499
Cdd:PRK13546 96 LSGQLTGIENIEFKMLCMgfkRKEIKAM-TPKIIEFSElGEFIYQpvkKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190
....*....|....*....|....*....|..
gi 2131440126 500 DphfrREFYQVLLPLMQEM---GKTIFAISHD 528
Cdd:PRK13546 175 D----QTFAQKCLDKIYEFkeqNKTIFFVSHN 202
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
342-528 |
1.39e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.08 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSaFSVGPVNLTIRRGELLFLIGGNGSGKSTLAM-------LLTGLYQpqSGEILLDGKALSAEK--PE 412
Cdd:PRK14243 11 LRTENLNVYYGSF-LAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLYAPDvdPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 413 DYRKLFSAVFTDVWLFDRLL------GPE--GQQAN-PALVEKWLAQL----QMSHKLElQDGkilnLKLSKGQKKRVAL 479
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIydniayGARinGYKGDmDELVERSLRQAalwdEVKDKLK-QSG----LSLSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 480 LLALAEERDIILLDEWAADQDPHFRREFYQvllpLMQEMGK--TIFAISHD 528
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEE----LMHELKEqyTIIIVTHN 209
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
325-401 |
1.63e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2131440126 325 PFKAEFPRPQAFPNwQTLELRNVKFHYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL 401
Cdd:PRK10636 297 PFHFSFRAPESLPN-PLLKMEKVSAGYGDRII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
343-399 |
1.75e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 1.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 343 ELRNVKFHYQD----SAFSVgpvnlTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 399
Cdd:PRK11147 321 EMENVNYQIDGkqlvKDFSA-----QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
363-413 |
1.98e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 1.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 363 LTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPED 413
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS 75
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
361-548 |
2.10e-05 |
|
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: 46.44 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFD---RL-LGPEG 436
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSgsiRFnLDPEC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 437 QQANPALVEKW-LAQLQMSHK--------LELQDGKilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREF 507
Cdd:cd03288 120 KCTDDRLWEALeIAQLKNMVKslpggldaVVTEGGE----NFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENIL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2131440126 508 YQVLLPLMQEmgKTIFAISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:cd03288 196 QKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
331-548 |
2.17e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.16 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 331 PRPQAFPNWQTLELRNVKFHYQDSAFSVGPV---NLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK--- 404
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVrnlSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 405 -------ALSAEKPEDYRKLFSA----VFTDVWLFDRLLGPEGQQANPALV-------EKWLAQLQ-MSHKLELQDGK-I 464
Cdd:PRK10261 82 rrsrqviELSEQSAAQMRHVRGAdmamIFQEPMTSLNPVFTVGEQIAESIRlhqgasrEEAMVEAKrMLDQVRIPEAQtI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 465 LNL---KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIH-ADRLLE 540
Cdd:PRK10261 162 LSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLV 241
|
....*...
gi 2131440126 541 MRDGKLSE 548
Cdd:PRK10261 242 MYQGEAVE 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-527 |
2.91e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.99 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ-----SGEILLDGKALSAEK--PEDY 414
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKG-VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDvdPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 415 RKLFSAVFT------------DVWLFDRLLG-PEGQQANPALVEKWL--AQLQMSHKLELQDgkiLNLKLSKGQKKRVAL 479
Cdd:PRK14267 84 RREVGMVFQypnpfphltiydNVAIGVKLNGlVKSKKELDERVEWALkkAALWDEVKDRLND---YPSNLSGGQRQRLVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2131440126 480 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEMgkTIFAISH 527
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
342-546 |
3.67e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.36 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 342 LELRNVKFHYQDSAF--SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ-SGEILLDGKALSAEKPEDYRKLF 418
Cdd:TIGR02633 258 LEARNLTCWDVINPHrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 419 SAVFTDvwlfDR-------LLGPeGQQANPALVEKWLAQLQMSHKLELQ--DGKILNLK------------LSKGQKKRV 477
Cdd:TIGR02633 338 IAMVPE----DRkrhgivpILGV-GKNITLSVLKSFCFKMRIDAAAELQiiGSAIQRLKvktaspflpigrLSGGNQQKA 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 478 ALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFIH-ADRLLEMRDGKL 546
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
352-501 |
4.01e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.83 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 352 QDSAFSVGPvnltirrGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFD-- 429
Cdd:TIGR01271 1236 QDLSFSVEG-------GQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSgt 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 430 --RLLGPEGQQANPAL--------VEKWLAQLQMSHKLELQDGKILnlkLSKGQKKRVALLLALAEERDIILLDEWAADQ 499
Cdd:TIGR01271 1308 frKNLDPYEQWSDEEIwkvaeevgLKSVIEQFPDKLDFVLVDGGYV---LSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
..
gi 2131440126 500 DP 501
Cdd:TIGR01271 1385 DP 1386
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
329-555 |
6.26e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 329 EFPRPQAFPNWQTLELRNVkfhyqdSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSA 408
Cdd:PRK10762 245 QYPRLDKAPGEVRLKVDNL------SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 409 EKPED-------Y----RK-----LFSAV-----FTDVWLFDRLLGPEGQQANPALVEKWLAQLQMshKLELQDGKILNl 467
Cdd:PRK10762 319 RSPQDglangivYisedRKrdglvLGMSVkenmsLTALRYFSRAGGSLKHADEQQAVSDFIRLFNI--KTPSMEQAIGL- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 468 kLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQEmGKTIFAISHDDHYFI-HADRLLEMRDGKL 546
Cdd:PRK10762 396 -LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLgMSDRILVMHEGRI 473
|
250
....*....|
gi 2131440126 547 S-ELTGEDRD 555
Cdd:PRK10762 474 SgEFTREQAT 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
341-517 |
1.12e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 341 TLELRNVKFHYQDSAFSVGPvNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSA 420
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 421 VF----TDvwlfdrLLGPE----GQQA---------NPALVEKWLAQLQMSHKLELQdgkilNLKLSKGQKKRVALLLAL 483
Cdd:PRK10938 82 EWqrnnTD------MLSPGeddtGRTTaeiiqdevkDPARCEQLAQQFGITALLDRR-----FKYLSTGETRKTLLCQAL 150
|
170 180 190
....*....|....*....|....*....|....
gi 2131440126 484 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQE 517
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
373-533 |
1.43e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.54 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 373 LIGGNGSGKSTLAMLLTGLYQPQSGEILL------------------------------DGKALSAEKPEDYRKlFSAVF 422
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPqpgikvgylpqepqldptktvrenveegvaEIKDALDRFNEISAK-YAEPD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 423 TDvwlFDRLLGPEGQ-QANPALVEKWLAQLQMS---HKLELQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEwaad 498
Cdd:TIGR03719 115 AD---FDKLAAEQAElQEIIDAADAWDLDSQLEiamDALRCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDE---- 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 2131440126 499 qdP--HFRREFYQVLLPLMQEMGKTIFAISHdDHYFI 533
Cdd:TIGR03719 188 --PtnHLDAESVAWLERHLQEYPGTVVAVTH-DRYFL 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
245-548 |
1.79e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 245 IRADTFHLSAVNWSNIMMLGAIGLVFW-------MANGLGWADTNVAATYSLTLLFLR--TPLLSAVGALPTLlsAQVAF 315
Cdd:PLN03130 1126 IRFTLVNMSSNRWLAIRLETLGGLMIWltasfavMQNGRAENQAAFASTMGLLLSYALniTSLLTAVLRLASL--AENSL 1203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 316 NKLKK----FDL---APFKAEFPRPQ-AFPNWQTLELRNVKFHYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAM 386
Cdd:PLN03130 1204 NAVERvgtyIDLpseAPLVIENNRPPpGWPSSGSIKFEDVVLRYRPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLN 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 387 LLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAV------FTDVWLFDrlLGPEGQQANPALVEkwlaQLQMSHKLELQ 460
Cdd:PLN03130 1284 ALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIpqapvlFSGTVRFN--LDPFNEHNDADLWE----SLERAHLKDVI 1357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 461 DGKILNL---------KLSKGQKKRVALLLALAEERDIILLDEWAADQD--------PHFRREFYQVllplmqemgkTIF 523
Cdd:PLN03130 1358 RRNSLGLdaevseageNFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrtdaliqKTIREEFKSC----------TML 1427
|
330 340
....*....|....*....|....*
gi 2131440126 524 AISHDDHYFIHADRLLEMRDGKLSE 548
Cdd:PLN03130 1428 IIAHRLNTIIDCDRILVLDAGRVVE 1452
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
330-413 |
2.39e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 330 FPRPQAFPNWQTLELRNVKFHYQDSAF--SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-GEILLDGKAL 406
Cdd:PRK13549 248 YPREPHTIGEVILEVRNLTAWDPVNPHikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPV 327
|
....*..
gi 2131440126 407 SAEKPED 413
Cdd:PRK13549 328 KIRNPQQ 334
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
340-399 |
2.90e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 2.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2131440126 340 QTLELRNVKFHYQDSA-FSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 399
Cdd:PRK15064 318 NALEVENLTKGFDNGPlFK--NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
245-559 |
4.44e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 245 IRADTFHLSAVNWSNIMMLGAIGLVFWMANG---LGWADTNVAATYSLTLLFLR------TPLLSavGALPTLLSAQVAF 315
Cdd:PLN03232 1123 IRFTLANTSSNRWLTIRLETLGGVMIWLTATfavLRNGNAENQAGFASTMGLLLsytlniTTLLS--GVLRQASKAENSL 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 316 NKLKK----FDL---APFKAEFPRP-QAFPNWQTLELRNVKFHYQDS--------AFSVGPvnltirrGELLFLIGGNGS 379
Cdd:PLN03232 1201 NSVERvgnyIDLpseATAIIENNRPvSGWPSRGSIKFEDVHLRYRPGlppvlhglSFFVSP-------SEKVGVVGRTGA 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 380 GKSTLAMLLTGLYQPQSGEILLDGKALSAEKPEDYRKLFSAVFTDVWLFDRL----LGPEGQQANPALvekWLAqLQMSH 455
Cdd:PLN03232 1274 GKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTvrfnIDPFSEHNDADL---WEA-LERAH 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 456 KLELQDGKILNL---------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPH--------FRREFYQVllplmqem 518
Cdd:PLN03232 1350 IKDVIDRNPFGLdaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRtdsliqrtIREEFKSC-------- 1421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2131440126 519 gkTIFAISHDDHYFIHADRLLEMRDGKL------SELTGEDRDAASR 559
Cdd:PLN03232 1422 --TMLVIAHRLNTIIDCDKILVLSSGQVleydspQELLSRDTSAFFR 1466
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
309-512 |
4.74e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 309 LSAQVAFN-KLKKFDLaPFKAEFPRPQAFPNWQTL-ELRNVKFHYQDSafsvgPV----NLTIRRGELLFLIGGNGSGKS 382
Cdd:PRK10938 227 LVAQLAHSeQLEGVQL-PEPDEPSARHALPANEPRiVLNNGVVSYNDR-----PIlhnlSWQVNPGEHWQIVGPNGAGKS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 383 TLAMLLTGLYqPQ--------------SGEILLDGKA----LSAEKPEDYRklFSAVFTDVWL---FDRlLG-----PEG 436
Cdd:PRK10938 301 TLLSLITGDH-PQgysndltlfgrrrgSGETIWDIKKhigyVSSSLHLDYR--VSTSVRNVILsgfFDS-IGiyqavSDR 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2131440126 437 QQanpALVEKWLAQLQMSHKLelqdGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR---REFYQVLL 512
Cdd:PRK10938 377 QQ---KLAQQWLDILGIDKRT----ADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLI 448
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
361-399 |
4.76e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 43.00 E-value: 4.76e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 399
Cdd:TIGR03719 341 LSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
361-404 |
7.32e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 41.45 E-value: 7.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2131440126 361 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK 404
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR 68
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
374-399 |
1.13e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 1.13e-03
10 20
....*....|....*....|....*.
gi 2131440126 374 IGGNGSGKSTLAMLLTGLYQPQSGEI 399
Cdd:PRK11819 356 IGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
91-271 |
1.20e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 41.01 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 91 LTTLGHHFVFRLRSEFIKRILDTQIERVEQLGSASLLAGLTSDVRAI-TIAFVRLPELVQGIILTFGSAAYLAWLSSKML 169
Cdd:cd18557 60 FNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLqSAVTDNLSQLLRNILQVIGGLIILFILSWKLT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 170 AVTALWIVItiwggFMLVSRVYK--HMAVLRETEDKLYNDYQTVLEG----RKELTLNRERAEH-IFNHLyIPDAREYRH 242
Cdd:cd18557 140 LVLLLVIPL-----LLIASKIYGryIRKLSKEVQDALAKAGQVAEESlsniRTVRSFSAEEKEIrRYSEA-LDRSYRLAR 213
|
170 180
....*....|....*....|....*....
gi 2131440126 243 HIIRADTFHLSavnWSNIMMLGAIGLVFW 271
Cdd:cd18557 214 KKALANALFQG---ITSLLIYLSLLLVLW 239
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
373-531 |
1.24e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 373 LIGGNGSGKSTLAMLLTGLYQPQSGEILLD-----GKaLSAEK--PEDYRKLFSAVFTDVWLF------DRLLgpegqqA 439
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGK-LRQDQfaFEEFTVLDTVIMGHTELWevkqerDRIY------A 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2131440126 440 NPALVEK---WLAQLQMS------HKLELQDGKIL----------NLKLSK---GQKKRVALLLALAEERDIILLDEWAA 497
Cdd:PRK15064 105 LPEMSEEdgmKVADLEVKfaemdgYTAEARAGELLlgvgipeeqhYGLMSEvapGWKLRVLLAQALFSNPDILLLDEPTN 184
|
170 180 190
....*....|....*....|....*....|....
gi 2131440126 498 DQDPHFRREFYQVLlplmQEMGKTIFAISHDDHY 531
Cdd:PRK15064 185 NLDINTIRWLEDVL----NERNSTMIIISHDRHF 214
|
|
| |
