|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1-547 |
0e+00 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 1063.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 1 MQLLLLVWRQYRWPFVAVMALSLASAALGIGLIAFINVRLIEMVDTSLSVLPEFLGLLLLLMAVTLGSQLALTALGHHFV 80
Cdd:PRK10522 1 MELLRLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLLLMAVTLGSQLALTTLGHHFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 81 FRLRSEFIKRILDTQVERVEQLGSASLLAGLTSDVRAITIAFVRLPELVQGIILTFGSAAYLAWLSSKMLAVTALWIAIT 160
Cdd:PRK10522 81 YRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITIAFVRLPELVQGIILTLGSAAYLAWLSPKMLLVTAIWMAVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 161 IWGGFVLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKELTLNRERAEYIFNHLYIPDAREYRHHIIRADTFHLSAVNWSN 240
Cdd:PRK10522 161 IWGGFVLVARVYKHMATLRETEDKLYNDYQTVLEGRKELTLNRERAEYVFENEYEPDAQEYRHHIIRADTFHLSAVNWSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 241 IMMLGAIGLVFWMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKFDLAPFKAEFPRPQAFPDW 320
Cdd:PRK10522 241 IMMLGAIGLVFYMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKLALAPYKAEFPRPQAFPDW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 321 QTLELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFS 400
Cdd:PRK10522 321 QTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFTDVWLFEQLLGPEGQQANPALVEKWLTQLQMSHKLELQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:PRK10522 401 AVFTDFHLFDQLLGPEGKPANPALVEKWLERLKMAHKLELEDGRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 481 DPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRLSELTGEERDAASRDAVARTA 547
Cdd:PRK10522 481 DPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAVARTA 547
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-539 |
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: 744.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 1 MQLLLLVWRQYRWPFVAVMALSLASAALGIGLIAFINVRLIEMVDTSLSVLPEFLGLLLLLMAVTLGSQLALTALGHHFV 80
Cdd:COG4615 1 MNLLRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 81 FRLRSEFIKRILDTQVERVEQLGSASLLAGLTSDVRAITIAFVRLPELVQGIILTFGSAAYLAWLSSKMLAVTALWIAIT 160
Cdd:COG4615 81 ARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 161 IWGGFVLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKELTLNRERAEYIFNHLYIPDAREYRHHIIRADTFHLSAVNWSN 240
Cdd:COG4615 161 VAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLNRRRRRAFFDEDLQPTAERYRDLRIRADTIFALANNWGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 241 IMMLGAIGLVFWMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKFDLA-----PFKAEFPRPQ 315
Cdd:COG4615 241 LLFFALIGLILFLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELAlaaaePAAADAAAPP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 316 AFPDWQTLELRNVTFRYQ----DSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEK 391
Cdd:COG4615 321 APADFQTLELRGVTYRYPgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 392 PEDYRKLFSAVFTDVWLFEQLLGPEGqQANPALVEKWLTQLQMSHKLELQDGKILNLKLSKGQKKRVALLLALAEERDII 471
Cdd:COG4615 401 REAYRQLFSAVFSDFHLFDRLLGLDG-EADPARARELLERLELDHKVSVEDGRFSTTDLSQGQRKRLALLVALLEDRPIL 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 472 LLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRLSELTGEERDAAS 539
Cdd:COG4615 480 VFDEWAADQDPEFRRVFYTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
2-527 |
3.35e-106 |
|
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: 329.23 E-value: 3.35e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 2 QLLLLVWRQYRWPFVAVMALSLASAALGIGLIAFINVRLIEMVDTSLSVLPEFLGLLLLLMAVTLGSQLALTALGHHFVF 81
Cdd:TIGR01194 7 EILALLRSPFPAITAFSIALGLAGGLAIIALLASINNAIHEENFLGQGSLFSFGGLCLLALLFRIGADIFPAYAGMHIIA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 82 RLRSEFIKRILDTQVERVEQLGSASLLAGLTSDVRAITIAFVRLPELVQGIILTFGSAAYLAWLSSKMLAVTALWIAITI 161
Cdd:TIGR01194 87 NLRIALCEKILGAPIEEIDRRGAHNLIPLLTHDIDQINAFLFIFPPIAIALAIFFFCIAYLAYLSVPMFAITISAIIIGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 162 WGGFVLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKELTLNRERAEYiFNHLYIPDA--REYRHHIIRADTFHLsAVNWS 239
Cdd:TIGR01194 167 AAQLLAFMGGFKFFHAARDEEDAFNEHTHAIAFGAKELKIHGIRRLS-FAHGAIQESanNIADLHIIEILIFIA-AENFG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 240 NIMMLGAIGLVFWMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKFDlapFKAEFPRPQAF-- 317
Cdd:TIGR01194 245 QLLFFLLIGCALFAAAMFASIDAAAISAFVLALLYIKGPLEMLVSALPILAQAQIACQRLADFG---ERFNEPEPELEls 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 318 ---------PD--WQTLELRNVTFRYQD----SAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL 382
Cdd:TIGR01194 322 dadnvlllaHDksVDSIELKDVHMNPKApegsEGFALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 383 DGRALSAEKPEDYRKLFSAVFTDVWLFEQLLGP-EGQQANPALVEKWLTQLQMSHKLELQDGKI-LNLKLSKGQKKRVAL 460
Cdd:TIGR01194 402 DGAAVSADSRDDYRDLFSAIFADFHLFDDLIGPdEGEHASLDNAQQYLQRLEIADKVKIEDGGFsTTTALSTGQQKRLAL 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 461 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:TIGR01194 482 ICAWLEDRPILLFDEWAADQDPAFKRFFYEELLPDLKRQGKTIIIISHDDQYFELADQIIKLAAGCI 548
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-529 |
1.43e-54 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 193.46 E-value: 1.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 1 MQLLLLVWRQYRWPFVAVMALSLASAALGIgLIAFINVRLIEMV--DTSLSVLPEFLGLLLLLMAV----TLGSQLALTA 74
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLEL-LLPLLLGRIIDALlaGGDLSALLLLLLLLLGLALLrallSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 75 LGHHFVFRLRSEFIKRILDTQVERVEQLGSASLLAGLTSDVRAITIAFVR-LPELVQGIILTFGSAAYLAWLSSKMLAVT 153
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLFVIDWRLALIV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 154 ALWIAITIWGGFVLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKEL-TLNRERAEY-IFNHLyipdAREYRHHIIRAdtF 231
Cdd:COG1132 168 LLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVkAFGREERELeRFREA----NEELRRANLRA--A 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 232 HLSAVNWSNIMMLGAIGLVF------WMANSlGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKF-DL 304
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALvllvggLLVLS-GSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELlDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 305 APFKAEFPRPQAFPDWQ-TLELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD 383
Cdd:COG1132 321 PPEIPDPPGAVPLPPVRgEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 384 GRALSAEKPEDYRKLFSAVFTDVWLFEQ------LLGPEGqqANPALVEKWLTQLQMSHKLE-LQDGkiLN-------LK 449
Cdd:COG1132 401 GVDIRDLTLESLRRQIGVVPQDTFLFSGtireniRYGRPD--ATDEEVEEAAKAAQAHEFIEaLPDG--YDtvvgergVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 450 LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
323-526 |
1.26e-47 |
|
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: 163.32 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDS-AFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFeqllgpegqqanpalvekwltqlqmshklelqDGKIL-NLkLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:cd03228 81 VPQDPFLF--------------------------------SGTIReNI-LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1347499258 481 DPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLEMRDGR 526
Cdd:cd03228 128 DPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
323-527 |
1.00e-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: 152.10 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRK----- 397
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 -------LFSA-VFTDVwlfeqLLGPEGQQANPA----LVEKWLTQLQMSHKLElqdgKILNlKLSKGQKKRVALLLALA 465
Cdd:COG1122 81 fqnpddqLFAPtVEEDV-----AFGPENLGLPREeireRVEEALELVGLEHLAD----RPPH-ELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 466 EERDIILLDEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
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 ... |
324-526 |
4.83e-42 |
|
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: 149.92 E-value: 4.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYQDSAFSVG-PVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAV 402
Cdd:cd03225 1 ELKNLSFSYPDGARPALdDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 F--TDVWLF------EQLLGPEGQQANP----ALVEKWLTQLQMSHkleLQDGKILNlkLSKGQKKRVALLLALAEERDI 470
Cdd:cd03225 81 FqnPDDQFFgptveeEVAFGLENLGLPEeeieERVEEALELVGLEG---LRDRSPFT--LSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 471 ILLDEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISHDDHYFI-HADRLLEMRDGR 526
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-529 |
2.83e-39 |
|
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: 151.07 E-value: 2.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 4 LLLVWRQYRWPFVAVMALSLASAALGIGLIA----FInvrliemvdTSLSVLPEFLGLLLLLMAV-TLGsqLALTA---- 74
Cdd:COG4987 6 LLRLLRPHRGRLLLGVLLGLLTLLAGIGLLAlsgwLI---------AAAALAPPILNLFVPIVGVrAFA--IGRTVfryl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 75 ---LGHHFVFR----LRSEFIKRILDTQVERVEQLGSASLLAGLTSDVRAITIAFVRL--PELVqGIILTFGSAAYLAWL 145
Cdd:COG4987 75 erlVSHDATLRlladLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVllPLLV-ALLVILAAVAFLAFF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 146 SSKMLAVTALWIAITIWGGFVLVSRVYKHMAV-LRETEDKLYNDYQTVLEGRKELTLN------RERAEYIFNHLyipDA 218
Cdd:COG4987 154 SPALALVLALGLLLAGLLLPLLAARLGRRAGRrLAAARAALRARLTDLLQGAAELAAYgaldraLARLDAAEARL---AA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 219 REYRHHIIRADTfhlSAVNWsnIMMLGAIGLVFWMAnSLGWADTNVAATYSLTLLFLRTPLLSAVGALPT----LLSAQV 294
Cdd:COG4987 231 AQRRLARLSALA---QALLQ--LAAGLAVVAVLWLA-APLVAAGALSGPLLALLVLAALALFEALAPLPAaaqhLGRVRA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 295 AFNKLNKF-DLAPFKAEFPRPQAFPDWQTLELRNVTFRYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGL 372
Cdd:COG4987 305 AARRLNELlDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 373 YQPQSGEILLDGRALSAEKPEDYRKLFSAVFTDVWLFEQ------LLGpeGQQANPALVEKWLTQLQMSHKLE-LQDGki 445
Cdd:COG4987 385 LDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTtlrenlRLA--RPDATDEELWAALERVGLGDWLAaLPDG-- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 446 LNL-------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADR 518
Cdd:COG4987 461 LDTwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDR 538
|
570
....*....|.
gi 1347499258 519 LLEMRDGRLSE 529
Cdd:COG4987 539 ILVLEDGRIVE 549
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
323-527 |
1.49e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 137.64 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAV 402
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLF-----EQLLGP---EGQQANPALVEKWLTQLQMSHKLELQDGKilnlKLSKGQKKRVALLLALAEERDIILLD 474
Cdd:COG4619 80 PQEPALWggtvrDNLPFPfqlRERKFDRERALELLERLGLPPDILDKPVE----RLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 475 EWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYF-IHADRLLEMRDGRL 527
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-529 |
1.05e-36 |
|
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: 144.98 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 9 RQYRWPFVAVMALSLASAALGIGLIAFINVrlieMVDTslsVLP----EFLGLLLLLMAVTLGSQLALTALGHHFV---- 80
Cdd:COG2274 152 RRYRRLLLQVLLASLLINLLALATPLFTQV----VIDR---VLPnqdlSTLWVLAIGLLLALLFEGLLRLLRSYLLlrlg 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 81 ----FRLRSEFIKRILDTQVERVEQLGSASLLAGLtSDVRAITIAFV-RLPELVQGIILTFGSAAYLAWLSSKMLAVTAL 155
Cdd:COG2274 225 qridLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgSLLTALLDLLFVLIFLIVLFFYSPPLALVVLL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 156 WIAITIWGGFVLVSRVYKHMAVLRETEDKLYNDYQTVLEGRKEL-TLNRE-RAEYIFNHLYipdaREYRHHIIRADTFHL 233
Cdd:COG2274 304 LIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIkALGAEsRFRRRWENLL----AKYLNARFKLRRLSN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 234 SAVNWSN-IMMLGAIGLVFWMAN-------SLGwadTNVAAtYSLTLLFLrTPLLSAVGALPTLLSAQVAFNKLNK-FDL 304
Cdd:COG2274 380 LLSTLSGlLQQLATVALLWLGAYlvidgqlTLG---QLIAF-NILSGRFL-APVAQLIGLLQRFQDAKIALERLDDiLDL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 305 APFKAEFPRPQAFPDWQ-TLELRNVTFRY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL 382
Cdd:COG2274 455 PPEREEGRSKLSLPRLKgDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 383 DGRALSAEKPEDYRKLFSAVFTDVWLFEQ------LLGpeGQQANPALVEKWLTQ-------LQMSHKLELQ---DGKil 446
Cdd:COG2274 535 DGIDLRQIDPASLRRQIGVVLQDVFLFSGtireniTLG--DPDATDEEIIEAARLaglhdfiEALPMGYDTVvgeGGS-- 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 447 nlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLEMRDGR 526
Cdd:COG2274 611 --NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGR 686
|
...
gi 1347499258 527 LSE 529
Cdd:COG2274 687 IVE 689
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
323-527 |
6.22e-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: 6.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALsAEKPEDYRKLFSAV 402
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQLLGPEgqqanpalvekwltqlqmshklelqdgkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:cd03230 79 PEEPSLYENLTVRE------------------------------NLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1347499258 483 HFRREFYQVLLPLMQQmGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:cd03230 129 ESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
323-527 |
1.32e-35 |
|
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: 134.09 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSA-FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG-RALSAEKPEDYRKLFS 400
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFT-------------DVwLFeqllGPEGQQANPA----LVEKWLTQLQMSHKLELQDgkilnLKLSKGQKKRVALLLA 463
Cdd:TIGR04520 81 MVFQnpdnqfvgatvedDV-AF----GLENLGVPREemrkRVDEALKLVGMEDFRDREP-----HLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 464 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKI 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-529 |
8.55e-35 |
|
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: 137.97 E-value: 8.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 4 LLLVWRQYRWPFVAVMALSLASAALGIG---LIAFINVRLIEMVDTSLSVLPEFLGlllllMAVTLGSQLALTALGHHFV 80
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAqawLLASLLAGLIIGGAPLSALLPLLGL-----LLAVLLLRALLAWLRERAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 81 FR--------LRSEFIKRILDTQVERVEQLGSASLLAGLTSDVRAITIAFVR-LPELVQGII---LTFGSAAYLAWLSSK 148
Cdd:COG4988 83 FRaaarvkrrLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARyLPQLFLAALvplLILVAVFPLDWLSGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 149 MLAVTALWIAITIWG-GFVLVSRVYKHMAVLRetedKLYNDYQTVLEGRKELTL-NRERAEyifnhlyipdAREYRHhii 226
Cdd:COG4988 163 ILLVTAPLIPLFMILvGKGAAKASRRQWRALA----RLSGHFLDRLRGLTTLKLfGRAKAE----------AERIAE--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 227 RADTFHLS-------AVNWSNIMMLGAIGLVFWMANSLGWA--DTNVAATYSLTLLFLR----TPL--LSA---VGAlpt 288
Cdd:COG4988 226 ASEDFRKRtmkvlrvAFLSSAVLEFFASLSIALVAVYIGFRllGGSLTLFAALFVLLLApeffLPLrdLGSfyhARA--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 289 llSAQVAFNKLNKFDLAPFKAEFPRPQAFPDWQ--TLELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLA 366
Cdd:COG4988 303 --NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGppSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 367 MLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVFTDVWLFEQ------LLGpeGQQANPALVEKWLTQLQMSHKLE- 439
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGtirenlRLG--RPDASDEELEAALEAAGLDEFVAa 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 440 LQDGkiLN-------LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHY 512
Cdd:COG4988 459 LPDG--LDtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLAL 534
|
570
....*....|....*..
gi 1347499258 513 FIHADRLLEMRDGRLSE 529
Cdd:COG4988 535 LAQADRILVLDDGRIVE 551
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
324-526 |
4.50e-34 |
|
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: 126.21 E-value: 4.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYQDSaFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVF 403
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 404 tdvwlfeQllgpegqqanpalvekwltqlqmshklelqdgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:cd00267 80 -------Q--------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1347499258 484 FRREFYQVLLPLMQQmGKTIFAISHDDHYFIHA-DRLLEMRDGR 526
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 ... |
324-527 |
9.81e-34 |
|
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: 126.01 E-value: 9.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYQDSaFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFsavf 403
Cdd:cd03214 1 EVENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 404 tdvwlfeqllgpegqqanpALVEKWLTQLQMSHKLElqdgKILNlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:cd03214 76 -------------------AYVPQALELLGLAHLAD----RPFN-ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1347499258 484 FRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDlNLAARYADRVILLKDGRI 176
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
324-527 |
2.17e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.18 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAV 402
Cdd:PRK13632 9 KVENVSFSYpNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FT--DvwlfEQLLGP----------EGQQANP----ALVEKWLTQLQMSHKLELQDgkilnLKLSKGQKKRVALLLALAE 466
Cdd:PRK13632 89 FQnpD----NQFIGAtveddiafglENKKVPPkkmkDIIDDLAKKVGMEDYLDKEP-----QNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
323-527 |
7.32e-32 |
|
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: 123.18 E-value: 7.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAV 402
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQLLGPEgqqaNPALV---EKWLTQLQMSHKLELQdgKILNL-----------KLSKGQKKRVALLLALAEER 468
Cdd:cd03295 81 IQQIGLFPHMTVEE----NIALVpklLKWPKEKIRERADELL--ALVGLdpaefadryphELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 469 DIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDiDEAFRLADRIAIMKNGEI 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
323-527 |
1.24e-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: 121.44 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV----GpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPED---- 394
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqalkG-VSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 YRKLFSAVFTDVWLFEQL-----------LGPEGQQANPALVEKWLTQLQMSHKLELQDGKilnlkLSKGQKKRVALLLA 463
Cdd:cd03255 80 RRRHIGFVFQSFNLLPDLtalenvelpllLAGVPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 464 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
341-478 |
3.07e-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: 118.13 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 341 PVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVFTDVWLF------EQLLG 414
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFprltvrENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347499258 415 PEGQQANPAL-----VEKWLTQLQMSHKLELQDGKILNlKLSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:pfam00005 83 GLLLKGLSKRekdarAEEALEKLGLGDLADRPVGERPG-TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
323-527 |
1.95e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 118.63 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEkPEDYRKLFSAV 402
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD-PAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQLLGPE-----------GQQANPALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDII 471
Cdd:COG1131 79 PQEPALYPDLTVREnlrffarlyglPRKEARERIDELLELFGLTDAADRKVG-----TLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 472 LLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHD----DHYfihADRLLEMRDGRL 527
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYleeaERL---CDRVAIIDKGRI 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
323-527 |
4.24e-30 |
|
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: 117.99 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL---- 398
Cdd:cd03261 1 IELRGLTKSFGGRTVLKG-VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 -----FSAVFTD--------VWLFEQLLGPEGQQAnpALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALA 465
Cdd:cd03261 80 gmlfqSGALFDSltvfenvaFPLREHTRLSEEEIR--EIVLEKLEAVGLRGAEDLYPA-----ELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 466 EERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDH--YFIhADRLLEMRDGRL 527
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDtaFAI-ADRIAVLYDGKI 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
323-527 |
5.56e-30 |
|
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: 117.65 E-value: 5.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSaFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFsaV 402
Cdd:COG4555 2 IEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIG--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTD-------------VWLFEQLLGPEGQQaNPALVEKWLTQLQMShklELQDGKIlnLKLSKGQKKRVALLLALAEERD 469
Cdd:COG4555 79 LPDerglydrltvrenIRYFAELYGLFDEE-LKKRIEELIELLGLE---EFLDRRV--GELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 470 IILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHDdhyfIH-----ADRLLEMRDGRL 527
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHI----MQevealCDRVVILHKGKV 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
323-529 |
9.14e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 116.68 E-value: 9.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL- 398
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 -----FsaVFTDVWLFE-----------QLLGPEGQQANPALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLL 462
Cdd:COG1136 85 rrhigF--VFQFFNLLPeltalenvalpLLLAGVSRKERRERARELLERVGLGDRLDHRPS-----QLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
323-534 |
1.75e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 117.42 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFT-------------DVwlfeqLLGPEGQQ-ANPALVEK--W-LTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLAL 464
Cdd:PRK13635 86 VFQnpdnqfvgatvqdDV-----AFGLENIGvPREEMVERvdQaLRQVGMEDFLNREPH-----RLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRL-SELTGEE 534
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEIlEEGTPEE 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
323-527 |
4.15e-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: 115.53 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAV 402
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDV---------------------WLfeQLLGPEGQQAnpalVEKWLTQLQMSHkleLQDgKILNlKLSKGQKKRVALL 461
Cdd:COG1120 81 PQEPpapfgltvrelvalgryphlgLF--GRPSAEDREA----VEEALERTGLEH---LAD-RPVD-ELSGGERQRVLIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 462 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDlNLAARYADRLVLLKDGRI 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
324-529 |
2.43e-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: 112.70 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVF 403
Cdd:cd03254 4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 404 TDVWLFEQ------LLGpeGQQANPALVEKWLTQLQMSHKLE-LQDGKILNLK-----LSKGQKKRVALLLALAEERDII 471
Cdd:cd03254 84 QDTFLFSGtimeniRLG--RPNATDEEVIEAAKEAGAHDFIMkLPNGYDTVLGenggnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 472 LLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
323-526 |
3.45e-28 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 110.74 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDsAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAE--KPEDYRKLFS 400
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFTDVWLFeqllgpegqqanpalveKWLTQLQmshklelqdgkILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQ 480
Cdd:cd03229 80 MVFQDFALF-----------------PHLTVLE-----------NIALGLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1347499258 481 DPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGR 526
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
323-529 |
6.62e-28 |
|
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: 111.44 E-value: 6.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFS---VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR---ALSAEKPEDYR 396
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 397 KLFSAVFTD-------VW-LFEQLLGP-EGQQANPALVEKWLTQLQMSHKLELqDGKILNLK---LSKGQKKRVALLLAL 464
Cdd:cd03257 82 KEIQMVFQDpmsslnpRMtIGEQIAEPlRIHGKLSKKEARKEAVLLLLVGVGL-PEEVLNRYpheLSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDH--YFIhADRLLEMRDGRLSE 529
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGvvAKI-ADRVAVMYAGKIVE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-529 |
9.69e-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: 116.54 E-value: 9.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFS----VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR---ALSAEKPEDY 395
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKdltKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 RKLFSAVFTDVwlFEQL----------------LGPEGQQANPALVEKWLTQLQMSHKL------ElqdgkilnlkLSKG 453
Cdd:COG1123 341 RRRVQMVFQDP--YSSLnprmtvgdiiaeplrlHGLLSRAERRERVAELLERVGLPPDLadryphE----------LSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 454 QKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD----DHYfihADRLLEMRDGRLSE 529
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlavvRYI---ADRVAVMYDGRIVE 485
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
315-534 |
2.89e-27 |
|
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: 110.81 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 315 QAFPDWQTLELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPED 394
Cdd:cd03294 16 KAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 YRKL----FSAVFTDVWLFEQL-------LGPEGQQANPAL-VEKWLTQLQM------SHKLELQdgkilnlkLSKGQKK 456
Cdd:cd03294 96 LRELrrkkISMVFQSFALLPHRtvlenvaFGLEVQGVPRAErEERAAEALELvglegwEHKYPDE--------LSGGMQQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 457 RVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRLSEL-TGEE 534
Cdd:cd03294 168 RVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDlDEALRLGDRIAIMKDGRLVQVgTPEE 247
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-529 |
3.76e-27 |
|
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: 115.00 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSA-FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGRALSAEKPEDYRKL 398
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 FSAVFTD-------VWLFEQL-LGPEGQQANP----ALVEKWLTQLQMSHKLELQDGKilnlkLSKGQKKRVALLLALAE 466
Cdd:COG1123 85 IGMVFQDpmtqlnpVTVGDQIaEALENLGLSRaearARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRLSE 529
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIVE 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
323-527 |
6.64e-27 |
|
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: 106.92 E-value: 6.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFeqllgpegqqanpalvekwltqlqmshklelqDGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:cd03246 81 LPQDDELF--------------------------------SGSIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1347499258 482 PHFRREFYQVLLpLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:cd03246 129 VEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
323-540 |
1.47e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.05 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSA--FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFS 400
Cdd:PRK13650 5 IEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFTDvwlfeqllgPEGQQANpALVE---------KWLTQLQM----SHKLEL---QDGKILN-LKLSKGQKKRVALLLA 463
Cdd:PRK13650 85 MVFQN---------PDNQFVG-ATVEddvafglenKGIPHEEMkervNEALELvgmQDFKEREpARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 464 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRLsELTGEERDAASR 540
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV-ESTSTPRELFSR 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
324-525 |
3.43e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 105.80 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEK--------PED- 394
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErrksigyvMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 YRKLFSA-VFTDVWLFEQLLGPEGQQANPALVEKWLTQLQMSHKLELqdgkilnlklSKGQKKRVALLLALAEERDIILL 473
Cdd:cd03226 81 DYQLFTDsVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSL----------SGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 474 DEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISHDDHyFIH--ADRLLEMRDG 525
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYE-FLAkvCDRVLLLANG 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
323-546 |
4.12e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.71 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDS-AFSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKP--------E 393
Cdd:COG1121 7 IELENLTVSYGGRpVLE--DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRrigyvpqrA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 394 DYRKLFSA-VFtDV----------WLfeQLLGPEGQQAnpalVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLL 462
Cdd:COG1121 85 EVDWDFPItVR-DVvlmgrygrrgLF--RRPSRADREA----VDEALERVGLEDLADRPIG-----ELSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISHDDHyFI--HADRLLEMRDGRLSEltGEERDAASR 540
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLG-AVreYFDRVLLLNRGLVAH--GPPEEVLTP 228
|
....*.
gi 1347499258 541 DAVART 546
Cdd:COG1121 229 ENLSRA 234
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
323-527 |
6.40e-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: 105.29 E-value: 6.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEdyRKLFSAV 402
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLF-------------EQLLGPEGQQAnpalvEKWLTQLQMSHKLELQDGKIlnLKLSKGQKKRVALLLALAEERD 469
Cdd:cd03259 78 FQDYALFphltvaeniafglKLRGVPKAEIR-----ARVRELLELVGLEGLLNRYP--HELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 470 IILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD--DHYFIhADRLLEMRDGRL 527
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDqeEALAL-ADRIAVMNEGRI 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
323-527 |
6.91e-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: 105.63 E-value: 6.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEdyrklF 399
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 400 SAVFTDVWLFEQL-------LGPEGQQANPA----LVEKWLTQLQMS---HKLELQdgkilnlkLSKGQKKRVALLLALA 465
Cdd:cd03293 76 GYVFQQDALLPWLtvldnvaLGLELQGVPKAeareRAEELLELVGLSgfeNAYPHQ--------LSGGMRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 466 EERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEM--RDGRL 527
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFlADRVVVLsaRPGRI 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-546 |
9.59e-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: 9.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFS---VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLF 399
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 400 SAVFTDvwlfeqllgPEGqQANPAL-VEKWLTQLQMSHKLELQDGKILNL----------------KLSKGQKKRVALLL 462
Cdd:COG1124 82 QMVFQD---------PYA-SLHPRHtVDRILAEPLRIHGLPDREERIAELleqvglppsfldryphQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGRLSE-LTGEERDAASR 540
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEeLTVADLLAGPK 231
|
....*.
gi 1347499258 541 DAVART 546
Cdd:COG1124 232 HPYTRE 237
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
324-522 |
1.15e-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: 104.54 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRalsaeKPEDYRKLFSAV- 402
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 -FTDV-WLF----EQ--LLGPEGQ--------QANPALVEKWLTQLQMSHKLELQDGKilnlkLSKGQKKRVALLLALAE 466
Cdd:cd03235 75 qRRSIdRDFpisvRDvvLMGLYGHkglfrrlsKADKAKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 467 ERDIILLDEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISHD-DHYFIHADRLLEM 522
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDlGLVLEYFDRVLLL 205
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
323-526 |
1.63e-25 |
|
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: 104.10 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSA-FSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALsAEKPEDYRKLFSA 401
Cdd:COG4133 3 LEAENLSCRRGERLlFS--GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFEQLLGPE---------GQQANPALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIIL 472
Cdd:COG4133 80 LGHADGLKPELTVREnlrfwaalyGLRADREAIDEALEAVGLAGLADLPVR-----QLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 473 LDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHDDhYFIHADRLLEMRDGR 526
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQP-LELAAARVLDLGDFK 206
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
75-509 |
1.87e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 110.14 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 75 LGHHFVFR----LRSEFIKRILDTQVERVEQLGSASLLAGLTSDVRAITIAFVR--LPELVQG--IILTFGSAAYLAWLS 146
Cdd:TIGR02868 76 VGHDAALRslgaLRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRviVPAGVALvvGAAAVAAIAVLSVPA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 147 SKMLAVTALWIAITIWGGFVLVSRvyKHMAVLRETEDKLYNDYQTVLEGRKELTLNRERAEYIfnhlyiPDAREYRHHII 226
Cdd:TIGR02868 156 ALILAAGLLLAGFVAPLVSLRAAR--AAEQALARLRGELAAQLTDALDGAAELVASGALPAAL------AQVEEADRELT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 227 RADTFHLSAVNWSNIMMLGAIGLVFWMANSLG---WADTNVAATYSLTLLFLRTPLLSAVGALP----TLLSAQVAFNKL 299
Cdd:TIGR02868 228 RAERRAAAATALGAALTLLAAGLAVLGALWAGgpaVADGRLAPVTLAVLVLLPLAAFEAFAALPaaaqQLTRVRAAAERI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 300 NKFDLAPFK---AEFPRPQAF-PDWQTLELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQP 375
Cdd:TIGR02868 308 VEVLDAAGPvaeGSAPAAGAVgLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 376 QSGEILLDGRALSAEKPEDYRKLFSAVFTDVWLFEQLLG-------PE--GQQANPAL----VEKWLTQLQMSHKLELQD 442
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRenlrlarPDatDEELWAALervgLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 443 GKILnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHD 509
Cdd:TIGR02868 468 GGAR---LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
323-527 |
7.91e-25 |
|
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: 103.14 E-value: 7.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqdsafsvGP------VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR---ALSAEKPE 393
Cdd:COG1127 6 IEVRNLTKSF-------GDrvvldgVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 394 DYRK----LF--SAVFTD--VW------LFEQLLGPEGQQAnpALVekwLTQLQMshkLELQDgkILNLK---LSKGQKK 456
Cdd:COG1127 79 ELRRrigmLFqgGALFDSltVFenvafpLREHTDLSEAEIR--ELV---LEKLEL---VGLPG--AADKMpseLSGGMRK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 457 RVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDH--YFIhADRLLEMRDGRL 527
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDsaFAI-ADRVAVLADGKI 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
323-525 |
1.11e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQ-DSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:PRK13648 8 IVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDvwlfeqllgPEGQ----------------QANP-----ALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVAL 460
Cdd:PRK13648 88 VFQN---------PDNQfvgsivkydvafglenHAVPydemhRRVSEALKQVDMLERADYEPN-----ALSGGQKQRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 461 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDG 525
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
323-527 |
1.46e-24 |
|
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: 101.90 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAF-SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:cd03245 3 IEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLF-----------------EQLLgpegQQANPALVEKWLTQLQMSHKLELQDGkilNLKLSKGQKKRVALLLAL 464
Cdd:cd03245 83 VPQDVTLFygtlrdnitlgapladdERIL----RAAELAGVTDFVNKHPNGLDLQIGER---GRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 465 AEERDIILLDEWAADQDPHFRREFYQVLlplmQQM--GKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERL----RQLlgDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
332-509 |
1.66e-24 |
|
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: 100.96 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 332 YQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEK----------------PEDy 395
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkgllerrqrvglvfqdPDD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 rKLFSA-VFTDVWLFEQLLGPEGQQANpALVEKWLTQLQMSHkLELQdgkiLNLKLSKGQKKRVALLLALAEERDIILLD 474
Cdd:TIGR01166 80 -QLFAAdVDQDVAFGPLNLGLSEAEVE-RRVREALTAVGASG-LRER----PTHCLSGGEKKRVAIAGAVAMRPDVLLLD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 1347499258 475 EWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHD 509
Cdd:TIGR01166 153 EPTAGLDPAGREQMLAILRRLRAE-GMTVVISTHD 186
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
323-527 |
4.40e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.19 E-value: 4.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAF-SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE---ILLDGRALSAEKPEDYRKL 398
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 FSAVFT-------------DVwlfeqLLGPEGQQAN----PALVEKWLTQLQMshkLELQDGKILNLklSKGQKKRVALL 461
Cdd:PRK13640 86 VGIVFQnpdnqfvgatvgdDV-----AFGLENRAVPrpemIKIVRDVLADVGM---LDYIDSEPANL--SGGQKQRVAIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 462 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-527 |
5.19e-24 |
|
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: 98.27 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKlfsav 402
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 ftdvwlfeqlLGpegqqanpalvekwltqLQMSHklelQdgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:cd03216 75 ----------AG-----------------IAMVY----Q--------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1347499258 483 HFRREFYQVLLPLmQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:cd03216 116 AEVERLFKVIRRL-RAQGVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
323-526 |
5.31e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.85 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGralsaeKPEDY-RK---- 397
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG------KPIDYsRKglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 ---------------LFSA-VFTDVwlfeqLLGPegqqANPALVEKWLtQLQMSHKLELQDGKILNLK----LSKGQKKR 457
Cdd:PRK13636 80 lresvgmvfqdpdnqLFSAsVYQDV-----SFGA----VNLKLPEDEV-RKRVDNALKRTGIEHLKDKpthcLSFGQKKR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 458 VALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGR 526
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGR 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
323-529 |
6.15e-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: 100.38 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGP-VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRdISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFEQLL------GPEGqqANPALVEKWLtQLQMSHKL--ELQDGKILNL-----KLSKGQKKRVALLLALAEER 468
Cdd:cd03251 81 VSQDVFLFNDTVaeniayGRPG--ATREEVEEAA-RAANAHEFimELPEGYDTVIgergvKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 469 DIILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
323-527 |
6.92e-24 |
|
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: 99.89 E-value: 6.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAF-SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL--- 398
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 --FSAVFTD------VWLFEQLLGPEGQQANpALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDI 470
Cdd:cd03263 81 pqFDALFDEltvrehLRFYARLKGLPKSEIK-EEVELLLRVLGLTDKANKRAR-----TLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 471 ILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSmDEAEALCDRIAIMSDGKL 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
323-527 |
2.56e-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: 97.95 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVgpvNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDyrKLFSAV 402
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQL---------------LGPEGQQAnpalVEKWLTQLQMSHKLelqdgKILNLKLSKGQKKRVALLLALAEE 467
Cdd:cd03298 76 FQENNLFAHLtveqnvglglspglkLTAEDRQA----IEVALARVGLAGLE-----KRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 468 RDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISH--DDHYFIhADRLLEMRDGRL 527
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHqpEDAKRL-AQRVVFLDNGRI 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
323-529 |
2.80e-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: 98.46 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAV 402
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQLLGPEGQQANPALVEKwltQLQMSHKLELQDGKILN-------------LKLSKGQKKRVALLLALAEERD 469
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDE---EVIEAAKAAQIHDKIMRfpdgydtivgergLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 470 IILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVE 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
323-529 |
6.78e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 97.05 E-value: 6.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPED---YRKLF 399
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 400 SAVFTDVWL------FE------QLLGPEGQQANpALVEKWLTQLQMSHKLELqdgkiLNLKLSKGQKKRVALLLALAEE 467
Cdd:COG2884 82 GVVFQDFRLlpdrtvYEnvalplRVTGKSRKEIR-RRVREVLDLVGLSDKAKA-----LPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 468 RDIILLDEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISHDDHyFIHA--DRLLEMRDGRLSE 529
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
323-530 |
8.08e-23 |
|
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: 97.27 E-value: 8.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFS---VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRK-- 397
Cdd:cd03258 2 IELKNVSKVFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 -----------LFSA--VFTDVWLFEQLLGPEGQQAnPALVEKWLTQLQMSHKlelqdGKILNLKLSKGQKKRVALLLAL 464
Cdd:cd03258 82 rrigmifqhfnLLSSrtVFENVALPLEIAGVPKAEI-EERVLELLELVGLEDK-----ADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDdhyfIH-----ADRLLEMRDGRLSEL 530
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHE----MEvvkriCDRVAVMEKGEVVEE 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
323-527 |
8.78e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 99.79 E-value: 8.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDyRKlFSAV 402
Cdd:COG3842 6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-RN-VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLF-------------EQLLGPEGQQAnpALVEKWLTQLQMSHkleLQDGKIlnLKLSKGQKKRVALLLALAEERD 469
Cdd:COG3842 83 FQDYALFphltvaenvafglRMRGVPKAEIR--ARVAELLELVGLEG---LADRYP--HQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1347499258 470 IILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqEEALALADRIAVMNDGRI 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
323-529 |
1.77e-22 |
|
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: 96.40 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQ-DSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFEQLLGPEGQQANPAL-VEKWLTQLQM--SHK--LELQDG--KILNLK---LSKGQKKRVALLLALAEERDII 471
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMsMERVIEAAKLagAHDfiSELPEGydTIVGEQgagLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 472 LLDEWAADQDphfrrefYQVLLPLMQQM-----GKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:cd03252 161 IFDEATSALD-------YESEHAIMRNMhdicaGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
323-526 |
1.96e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.11 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAV 402
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTD---------VWLfEQLLGPEGQQANPALVEKwltqlQMSHKLELQDGKILNLK----LSKGQKKRVALLLALAEERD 469
Cdd:PRK13647 85 FQDpddqvfsstVWD-DVAFGPVNMGLDKDEVER-----RVEEALKAVRMWDFRDKppyhLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 470 IILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHD-DHYFIHADRLLEMRDGR 526
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDvDLAAEWADQVIVLKEGR 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
323-541 |
2.76e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.59 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVgpvNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPedYRKLFSAV 402
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF---DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQL---------------LGPEGQQAnpalVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEE 467
Cdd:COG3840 77 FQENNLFPHLtvaqniglglrpglkLTAEQRAQ----VEQALERVGLAGLLDRLPG-----QLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 468 RDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGR------LSELTGEERDAASR 540
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRiaadgpTAALLDGEPPPALA 227
|
.
gi 1347499258 541 D 541
Cdd:COG3840 228 A 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
323-529 |
3.81e-22 |
|
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: 93.53 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKpEDYRKLFSA 401
Cdd:cd03247 1 LSINNVSFSYPEQEQQVlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFeqllgpegqqanpalvekwltqlqmshklelqDGKILN---LKLSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:cd03247 80 LNQRPYLF--------------------------------DTTLRNnlgRRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 479 DQDPhfrREFYQVLLPLMQQM-GKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:cd03247 128 GLDP---ITERQLLSLIFEVLkDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
312-533 |
4.42e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.98 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 312 PRPQAFPDWQT---LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALS 388
Cdd:PRK11607 6 PRPQAKTRKALtplLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 389 AEKPedYRKLFSAVFTDVWLF-----EQLLG--------PEGQQAnpALVEKWLTqlqMSHKLELQDGKilNLKLSKGQK 455
Cdd:PRK11607 85 HVPP--YQRPINMMFQSYALFphmtvEQNIAfglkqdklPKAEIA--SRVNEMLG---LVHMQEFAKRK--PHQLSGGQR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347499258 456 KRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRLSELtGE 533
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGKFVQI-GE 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
303-522 |
5.11e-22 |
|
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: 99.67 E-value: 5.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 303 DLAPFKAEFPRPQA------FPDWQTLELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ 376
Cdd:TIGR02857 296 ALFAVLDAAPRPLAgkapvtAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 377 SGEILLDGRALSAEKPEDYRKLFSAVFTDVWLFEQ------LLGPEGqqANPALVEKWLTQ---------LQMSHKLELQ 441
Cdd:TIGR02857 376 EGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGtiaeniRLARPD--ASDAEIREALERagldefvaaLPQGLDTPIG 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 442 DGkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLE 521
Cdd:TIGR02857 454 EG---GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVV 528
|
.
gi 1347499258 522 M 522
Cdd:TIGR02857 529 L 529
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
323-527 |
7.27e-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: 94.61 E-value: 7.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPedYRKLFSAV 402
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQL-------LGPEGQQANPAL----VEKWLTQLQMShklELQDGKIlnLKLSKGQKKRVALLLALAEERDII 471
Cdd:cd03300 78 FQNYALFPHLtvfeniaFGLRLKKLPKAEikerVAEALDLVQLE---GYANRKP--SQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 472 LLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDqEEALTMSDRIAVMNKGKI 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
323-529 |
8.15e-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: 95.16 E-value: 8.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPE------ 393
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtalDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDrgvvfq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 394 DYRklfsavftdvwLFEQL-------LGPEGQQANPA----LVEKWLTQLQMSHKLEL---QdgkilnlkLSKGQKKRVA 459
Cdd:COG1116 88 EPA-----------LLPWLtvldnvaLGLELRGVPKAerreRARELLELVGLAGFEDAyphQ--------LSGGMRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 460 LLLALAEERDIILLDEwaadqdPhF-------RREFYQVLLPLMQQMGKTIFAISHDdhyfIH-----ADRLLEM--RDG 525
Cdd:COG1116 149 IARALANDPEVLLMDE------P-FgaldaltRERLQDELLRLWQETGKTVLFVTHD----VDeavflADRVVVLsaRPG 217
|
....
gi 1347499258 526 RLSE 529
Cdd:COG1116 218 RIVE 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
267-536 |
9.04e-22 |
|
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: 99.43 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 267 TYSLTLLFLRTPLLSAVGALPTLLSAQVAFNKLNKFDLAPfkAEFPRPQAFPDWQTL----ELRNVTFRYQDSAFSVGPV 342
Cdd:TIGR01193 416 TFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVD--SEFINKKKRTELNNLngdiVINDVSYSYGYGSNILSDI 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 343 NLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVFTDVWLF-----EQLLgpeg 417
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFsgsilENLL---- 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 418 QQANP-------------ALVEKWLTQLQMSHKLELQDGkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF 484
Cdd:TIGR01193 570 LGAKEnvsqdeiwaaceiAEIKDDIENMPLGYQTELSEE---GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 485 RREFYQVLLPLMQqmgKTIFAISHDDHYFIHADRLLEMRDGRLSElTGEERD 536
Cdd:TIGR01193 647 EKKIVNNLLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKIIE-QGSHDE 694
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
323-539 |
1.18e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.05 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG-RALSAEKPEDYRKLFSA 401
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDV-------WLFEQL-LGPEGQQANPALVEKWLTQLQMSHKLELQDGKILNlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK13644 82 VFQNPetqfvgrTVEEDLaFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPK-TLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 474 DEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHDDHYFIHADRLLEMRDGRLSeLTGEERDAAS 539
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVMDRGKIV-LEGEPENVLS 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
323-509 |
2.37e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 93.56 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRY------QDsafsvgpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYR 396
Cdd:COG0411 5 LEVRGLTKRFgglvavDD-------VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 397 KL-----F--SAVFTD----------------VWLFEQLLGP----EGQQANPALVEKWLTQLQMSHKLELQDGkilnlK 449
Cdd:COG0411 78 RLgiartFqnPRLFPEltvlenvlvaaharlgRGLLAALLRLprarREEREARERAEELLERVGLADRADEPAG-----N 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 450 LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD 509
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
323-527 |
2.44e-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: 92.89 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL-FSA 401
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFEQL-------LGPEGQQANPAL--------------VEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVAL 460
Cdd:cd03219 80 TFQIPRLFPELtvlenvmVAAQARTGSGLLlararreerearerAEELLERVGLADLADRPAG-----ELSYGQQRRLEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 461 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
323-526 |
2.48e-21 |
|
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: 92.34 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEK-------PED- 394
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEEr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 --YRKLfsAVFTDVWLFEQLLGPEGQQANPAlVEKWLTQLQMSHKLElqdgKILNlKLSKGQKKRVALLLALAEERDIIL 472
Cdd:cd03269 80 glYPKM--KVIDQLVYLAQLKGLKKEEARRR-IDEWLERLELSEYAN----KRVE-ELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 473 LDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHD-DHYFIHADRLLEMRDGR 526
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQmELVEELCDRVLLLNKGR 205
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
324-527 |
3.18e-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: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDY-RKL---- 398
Cdd:COG4604 3 EIKNVSKRYGGKV-VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELaKRLailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 ----FSAVFTdVwlfEQLLG----PEGQ----QANPALVEKWLTQLQMShklELQDgKILNlKLSKGQKKRVALLLALAE 466
Cdd:COG4604 82 qenhINSRLT-V---RELVAfgrfPYSKgrltAEDREIIDEAIAYLDLE---DLAD-RYLD-ELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDdhyfI-----HADRLLEMRDGRL 527
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD----InfascYADHIVAMKDGRV 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
323-526 |
4.49e-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: 92.25 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFS-- 400
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 -------------AVFTDV-----------WLFEQLLGPEGQQANPALvekwLTQLQMSHKLELQDGkilnlKLSKGQKK 456
Cdd:cd03256 81 gmifqqfnlierlSVLENVlsgrlgrrstwRSLFGLFPKEEKQRALAA----LERVGLLDKAYQRAD-----QLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 457 RVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFI-HADRLLEMRDGR 526
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAReYADRIVGLKDGR 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
323-527 |
6.49e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.83 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPE--DYRKLFS 400
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFT--DVWLF----EQ--LLGPEGQQANPALVEKWLTQLQMSHKLELQDGKILNlKLSKGQKKRVALLLALAEERDIIL 472
Cdd:PRK13639 82 IVFQnpDDQLFaptvEEdvAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPH-HLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 473 LDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDvDLVPVYADKVYVMSDGKI 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
323-527 |
2.95e-20 |
|
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: 89.13 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPE--DYRKLFS 400
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKG-IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFTDVWLFEQL-------LGP-----EGQQANPALVEKWLTQLQMSHKlelQDGKIlnLKLSKGQKKRVALLLALAEER 468
Cdd:cd03262 80 MVFQQFNLFPHLtvlenitLAPikvkgMSKAEAEERALELLEKVGLADK---ADAYP--AQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 469 DIILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHdDHYFIH--ADRLLEMRDGRL 527
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTH-EMGFARevADRVIFMDDGRI 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
321-543 |
3.43e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.92 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 321 QTLELRNVTFRYQDSA--FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL 398
Cdd:PRK13642 3 KILEVENLVFKYEKESdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 FSAVFTDVwlFEQLLGPEGQQANPALVE-KWLTQLQMSHKLE--LQDGKILNLK------LSKGQKKRVALLLALAEERD 469
Cdd:PRK13642 83 IGMVFQNP--DNQFVGATVEDDVAFGMEnQGIPREEMIKRVDeaLLAVNMLDFKtreparLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 470 IILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGR-LSELTGEERDAASRDAV 543
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEiIKEAAPSELFATSEDMV 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
342-527 |
6.01e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKP----EDYRKLFSAVF--TDVWLFEQ---- 411
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFqfPEAQLFENtvlk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 412 --LLGP------EGQQANPALveKWLTQLQMSHKLELQDgkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:PRK13641 106 dvEFGPknfgfsEDEAKEKAL--KWLKKVGLSEDLISKS----PFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1347499258 484 FRREFYQVLLPlMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:PRK13641 180 GRKEMMQLFKD-YQKAGHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
322-536 |
6.37e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.11 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRY-QDSAF---SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAE--KPEDY 395
Cdd:PRK13637 2 SIKIENLTHIYmEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 RKLFSAVFT--DVWLFEQLL------GPEGQQANPALVEKWLTQLQMSHKLELQDGKILN-LKLSKGQKKRVALLLALAE 466
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIekdiafGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSpFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISH--DDHYFIhADRLLEMRDGRLsELTGEERD 536
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHsmEDVAKL-ADRIIVMNKGKC-ELQGTPRE 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
323-533 |
6.78e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 88.62 E-value: 6.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRyQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFS-- 400
Cdd:PRK10247 8 LQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSyc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 ----AVFTDVwLFEQLLGP---EGQQANPALVEKWLTQLQMSHKLeLQdgKILNlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK10247 87 aqtpTLFGDT-VYDNLIFPwqiRNQQPDPAIFLDDLERFALPDTI-LT--KNIA-ELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 474 DEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRL--LEMRDGRLSELTGE 533
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVitLQPHAGEMQEARYE 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
323-527 |
7.97e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.76 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQD-----SAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPE-DYR 396
Cdd:PRK13633 5 IKCKNVSYKYESneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 397 KLFSAVFT-------------DVwlfeqLLGPEGQQANP----ALVEKWLTQLQMS----HKLELqdgkilnlkLSKGQK 455
Cdd:PRK13633 85 NKAGMVFQnpdnqivativeeDV-----AFGPENLGIPPeeirERVDESLKKVGMYeyrrHAPHL---------LSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 456 KRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
323-527 |
9.18e-20 |
|
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: 87.85 E-value: 9.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPED---YRKLF 399
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 400 SAVFTDVWL------FEQLLGP-EGQQANPALVEK----WLTQLQMSHKlelqdGKILNLKLSKGQKKRVALLLALAEER 468
Cdd:cd03292 81 GVVFQDFRLlpdrnvYENVAFAlEVTGVPPREIRKrvpaALELVGLSHK-----HRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 469 DIILLDEWAADQDPHFRREFYQvLLPLMQQMGKTIFAISHDDHYF-IHADRLLEMRDGRL 527
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-529 |
1.09e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.58 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVlKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFEQLLGPEGQQANPALVEKWLTQLQMSHKLE--LQDGKILNL-------KLSKGQKKRVALLLALAEERDIIL 472
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEklLEDDKGLNAwlgeggrQLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 473 LDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
323-529 |
1.68e-19 |
|
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: 87.16 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFE----QLLGPEGQQANPALVE--------KWLTQLQMSHKLELQDGkilNLKLSKGQKKRVALLLALAEERD 469
Cdd:cd03244 83 IPQDPVLFSgtirSNLDPFGEYSDEELWQalervglkEFVESLPGGLDTVVEEG---GENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 470 IILLDEWAADQDPHFRRefyqvllpLMQQM------GKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:cd03244 160 ILVLDEATASVDPETDA--------LIQKTireafkDCTVLTIAHRLDTIIDSDRILVLDKGRVVE 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
322-527 |
2.39e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSa 401
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 vftdvWLFEQLLGPEG---------------------QQANPALVEKWLTQLQMSHkleLQDGKILNlkLSKGQKKRVAL 460
Cdd:PRK11231 80 -----LLPQHHLTPEGitvrelvaygrspwlslwgrlSAEDNARVNQAMEQTRINH---LADRRLTD--LSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 461 LLALAEERDIILLDEWAADQDPHfrrefYQV-LLPLMQQM---GKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDIN-----HQVeLMRLMRELntqGKTVVTVLHDlNQASRYCDHLVVLANGHV 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
323-527 |
3.61e-19 |
|
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: 86.37 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFS--VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFS 400
Cdd:cd03248 12 VKFQNVTFAYPTRPDTlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFTDVWLFEQLLGPE---GQQANPALVEKWLTQLQMSHKL--ELQDGKILNL-----KLSKGQKKRVALLLALAEERDI 470
Cdd:cd03248 92 LVGQEPVLFARSLQDNiayGLQSCSFECVKEAAQKAHAHSFisELASGYDTEVgekgsQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 471 ILLDEWAADQDPHFRREFYQVLLPLMQQmgKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
323-547 |
3.70e-19 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 87.55 E-value: 3.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFS--------VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPED 394
Cdd:TIGR02769 3 LEVRDVTHTYRTGGLFgakqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 ---YRKLFSAVFTDVWlfeqllgpegQQANPALVEKWLTQLQMSHKLEL----QDGKILNL----------------KLS 451
Cdd:TIGR02769 83 rraFRRDVQLVFQDSP----------SAVNPRMTVRQIIGEPLRHLTSLdeseQKARIAELldmvglrsedadklprQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 452 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD---DHYFihADRLLEMRDGRLS 528
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDlrlVQSF--CQRVAVMDKGQIV 230
|
250
....*....|....*....
gi 1347499258 529 eltgEERDAASRDAVARTA 547
Cdd:TIGR02769 231 ----EECDVAQLLSFKHPA 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
323-527 |
4.66e-19 |
|
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: 86.24 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDsaFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEdyRKLFSAV 402
Cdd:cd03299 1 LKVENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQL-------LGPEGQQANPALVEKWLtqLQMSHKLELqdGKILNLK---LSKGQKKRVALLLALAEERDIIL 472
Cdd:cd03299 77 PQNYALFPHMtvykniaYGLKKRKVDKKEIERKV--LEIAEMLGI--DHLLNRKpetLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 473 LDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDfEEAWALADKVAIMLNGKL 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
323-527 |
6.94e-19 |
|
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: 85.38 E-value: 6.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDyRKLfSAV 402
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDI-AMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQL-------LGPEGQQANPALVEKWLTQ----LQMSHklelqdgkILNLK---LSKGQKKRVALLLALAEER 468
Cdd:cd03301 78 FQNYALYPHMtvydniaFGLKLRKVPKDEIDERVREvaelLQIEH--------LLDRKpkqLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 469 DIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDqVEAMTMADRIAVMNDGQI 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
322-527 |
9.98e-19 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 85.47 E-value: 9.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFsa 401
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFEQL-----------LGPEGQQANPALVEKWLTQLQMSHKLE-LQDGkiLNLKLSKGQKKRVALLLALAEERD 469
Cdd:cd03296 79 VFQHYALFRHMtvfdnvafglrVKPRSERPPEAEIRAKVHELLKLVQLDwLADR--YPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1347499258 470 IILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGRL 527
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEvADRVVVMNKGRI 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
342-527 |
1.52e-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: 84.51 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRalsaekpedyrklfsavftDVWLFEQLLG--PE--G 417
Cdd:cd03220 41 VSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-------------------VSSLLGLGGGfnPEltG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 418 QQaNPALVEKWL--TQLQMSHKL-------ELqdGKILNLKL---SKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 485
Cdd:cd03220 102 RE-NIYLNGRLLglSRKEIDEKIdeiiefsEL--GDFIDLPVktySSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1347499258 486 REFYQVLLPLMQQmGKTIFAISHDDHYFI-HADRLLEMRDGRL 527
Cdd:cd03220 179 EKCQRRLRELLKQ-GKTVILVSHDPSSIKrLCDRALVLEKGKI 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
323-535 |
2.54e-18 |
|
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: 84.02 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVG---PVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAeKPEDYRKLF 399
Cdd:COG4181 9 IELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA-LDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 400 SA-----VFTDvwlfEQLLG------------PEGQQANP-ALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALL 461
Cdd:COG4181 88 RArhvgfVFQS----FQLLPtltalenvmlplELAGRRDArARARALLERVGLGHRLDHYPA-----QLSGGEQQRVALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 462 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRLSELTGEER 535
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
323-536 |
2.84e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 85.46 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQ-DSAF---SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEK-PEDYRK 397
Cdd:PRK13634 3 ITFQKVEHRYQyKTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 LFSAV-----FTDVWLFEQLL------GPEG----QQANPALVEKWLTQLQMSHKLELQDgkilNLKLSKGQKKRVALLL 462
Cdd:PRK13634 83 LRKKVgivfqFPEHQLFEETVekdicfGPMNfgvsEEDAKQKAREMIELVGLPEELLARS----PFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISH--DD--HYfihADRLLEMRDGRLsELTGEERD 536
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHsmEDaaRY---ADQIVVMHKGTV-FLQGTPRE 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
342-525 |
3.33e-18 |
|
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: 83.67 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYrklfsAVFTDVWLFEQLLGPEgqqaN 421
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRE----N 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 422 PAL-VEKWLTQLQMSHKLELQDGKI--LNL---------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFY 489
Cdd:TIGR01184 75 IALaVDRVLPDLSKSERRAIVEEHIalVGLteaadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1347499258 490 QVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDG 525
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
322-529 |
4.61e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.58 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYqdSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL-F 399
Cdd:COG1118 2 SIEVRNISKRF--GSFTLlDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVgF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 400 saVFTDVWLF-------------EQLLGPEGQQAnpALVEKWLTQLQMSHklelqdgkilnLK------LSKGQKKRVAL 460
Cdd:COG1118 80 --VFQHYALFphmtvaeniafglRVRPPSKAEIR--ARVEELLELVQLEG-----------LAdrypsqLSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 461 LLALAEERDIILLDE-WAAdQDPHFRREFYQVLLPLMQQMG-KTIFaISHD--DHYFIhADRLLEMRDGRLSE 529
Cdd:COG1118 145 ARALAVEPEVLLLDEpFGA-LDAKVRKELRRWLRRLHDELGgTTVF-VTHDqeEALEL-ADRVVVMNQGRIEQ 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
323-526 |
5.90e-18 |
|
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: 82.52 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGP----VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR-ALSAEKPEdyrk 397
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSiAYVSQEPW---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 LFSAVFTDVWLFeqllgpeGQQANPALVEKWLT--QLQmshklelQDGKILNLK-----------LSKGQKKRVALLLAL 464
Cdd:cd03250 77 IQNGTIRENILF-------GKPFDEERYEKVIKacALE-------PDLEILPDGdlteigekginLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 465 AEERDIILLDEWAADQDPHFRRE-FYQVLLPLMQQmGKTIFAISHDDHYFIHADRLLEMRDGR 526
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHiFENCILGLLLN-NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
323-536 |
6.91e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.03 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGP----VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAE-KPEDYRK 397
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRalfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 LFSAV-----FTDVWLFEQLL------GPE----GQQANPALVEKWLTQLQMSHKLELQDgkilNLKLSKGQKKRVALLL 462
Cdd:PRK13649 83 IRKKVglvfqFPESQLFEETVlkdvafGPQnfgvSQEEAEALAREKLALVGISESLFEKN----PFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISH--DD--HYfihADRLLEMRDGRLSeLTGEERD 536
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHlmDDvaNY---ADFVYVLEKGKLV-LSGKPKD 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
323-531 |
6.93e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.94 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFS---VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLF 399
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 400 SAVFTDVWLFEQLLgPE----GQQANPALVEKWLTQLQMSHKLEL-------QDGKILNLKLSKGQKKRVALLLALAEER 468
Cdd:PRK11629 86 NQKLGFIYQFHHLL-PDftalENVAMPLLIGKKKPAEINSRALEMlaavgleHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 469 DIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRLS-ELT 531
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTaELS 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
323-526 |
1.05e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.00 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEdyRKLFSAV 402
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQL-------LGPEGQQ-ANPALVEKWLTQLQMSHKLELQDGKILNlkLSKGQKKRVALLLALAEERDIILLD 474
Cdd:PRK09452 92 FQSYALFPHMtvfenvaFGLRMQKtPAAEITPRVMEALRMVQLEEFAQRKPHQ--LSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 475 EWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGR 526
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDqEEALTMSDRIVVMRDGR 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
323-529 |
1.88e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.68 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGraLSAEKPE----DYRKL 398
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHN-IDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKvderLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 FSAVFTDVWLFEQL-------LGP-----EGQQANPALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAE 466
Cdd:PRK09493 79 AGMVFQQFYLFPHLtalenvmFGPlrvrgASKEEAEKQARELLAKVGLAERAHHYPS-----ELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHDDHyFIH--ADRLLEMRDGRLSE 529
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIG-FAEkvASRLIFIDKGRIAE 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
322-529 |
2.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDSA----FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDY-- 395
Cdd:PRK13646 2 TIRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 --RKLFSAVFT--DVWLFEQ------LLGPEGQQANPALVEKWLTQLQMSHKLELQDGKILNLKLSKGQKKRVALLLALA 465
Cdd:PRK13646 82 pvRKRIGMVFQfpESQLFEDtvereiIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 466 EERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRLSE 529
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVS 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
323-518 |
4.85e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.35 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQD-SAFSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR---ALSAEKPEDYRKL 398
Cdd:PRK11831 8 VDMRGVSFTRGNrCIFD--NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 FS------AVFTDVWLFEQLLGP--EGQQANPALVEkwlTQLQMshKLELQD----GKILNLKLSKGQKKRVALLLALAE 466
Cdd:PRK11831 86 MSmlfqsgALFTDMNVFDNVAYPlrEHTQLPAPLLH---STVMM--KLEAVGlrgaAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD--------DHYFIHADR 518
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDvpevlsiaDHAYIVADK 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
322-527 |
7.06e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 82.04 E-value: 7.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDyRKLfSA 401
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI-AM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFtdvwlfeQllgpegqqaNPAL---------------------------VEKWLTQLQMSHklelqdgkILNLK---LS 451
Cdd:COG3839 80 VF-------Q---------SYALyphmtvyeniafplklrkvpkaeidrrVREAAELLGLED--------LLDRKpkqLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 452 KGQKKRVALLLALAEERDIILLDEWAADQDPH----FRREFYQvllpLMQQMGKTIFAISHDdhy-fihADRLLEMRDGR 526
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKlrveMRAEIKR----LHRRLGTTTIYVTHDqveamtlADRIAVMNDGR 211
|
.
gi 1347499258 527 L 527
Cdd:COG3839 212 I 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
330-527 |
8.80e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.44 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 330 FRYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPE--DYRKLFSAVFTDvw 407
Cdd:PRK13638 9 FRYQDEPVLKG-LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 408 lfeqllgPEGQ-------------QANPALVEKWLTQlQMSHKLELQDGKILNLK----LSKGQKKRVALLLALAEERDI 470
Cdd:PRK13638 86 -------PEQQifytdidsdiafsLRNLGVPEAEITR-RVDEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 471 ILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDiDLIYEISDAVYVLRQGQI 214
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
342-527 |
9.01e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.74 E-value: 9.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAlsaekpedyrklfsavftdVWLFE----------- 410
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV-------------------SALLElgagfhpeltg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 411 --------QLLGpegqqanpalvekwLTQLQMSHKL-------ELqdGKILNLKL---SKGQKKRVALLLALAEERDIIL 472
Cdd:COG1134 106 reniylngRLLG--------------LSRKEIDEKFdeivefaEL--GDFIDQPVktySSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 473 LDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHdDHYFI--HADRLLEMRDGRL 527
Cdd:COG1134 170 VDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSH-SMGAVrrLCDRAIWLEKGRL 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
323-529 |
1.04e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.12 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGP--------VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSA---EK 391
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGKHqhqtvlnnVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnrAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 392 PEDYRKLFSAVFTDVwlfeqlLGpegqQANPALVEKWLTQLQMSHKLELQD-------GKILNL-------------KLS 451
Cdd:PRK10419 84 RKAFRRDIQMVFQDS------IS----AVNPRKTVREIIREPLRHLLSLDKaerlaraSEMLRAvdlddsvldkrppQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 452 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD---DHYFIHadRLLEMRDGRLS 528
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDlrlVERFCQ--RVMVMDNGQIV 231
|
.
gi 1347499258 529 E 529
Cdd:PRK10419 232 E 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
323-508 |
1.13e-16 |
|
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: 78.95 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAF---SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL- 398
Cdd:cd03266 2 ITADALTKRFRDVKKtvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 -FSA---------VFTDVWLFEQLLGPEGQQANpALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEER 468
Cdd:cd03266 82 fVSDstglydrltARENLEYFAGLYGLKGDELT-ARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1347499258 469 DIILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISH 508
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTH 194
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
339-527 |
1.28e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.50 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 339 VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYqPQSGEILLDGRALSAEKPED---YRKLFS-----AVFTDVWLFE 410
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElarHRAYLSqqqspPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 411 QLLGPEGqqANPALVEKWLTQLqmSHKLELQD--GKILNlKLSKGQKKRV---ALLL----ALAEERDIILLDEWAADQD 481
Cdd:COG4138 91 ALHQPAG--ASSEAVEQLLAQL--AEALGLEDklSRPLT-QLSGGEWQRVrlaAVLLqvwpTINPEGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1347499258 482 PHFRREFYQVLLPLMQQmGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:COG4138 166 VAQQAALDRLLRELCQQ-GITVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
322-475 |
1.38e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.54 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEK-------PED 394
Cdd:COG4152 1 MLELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 ---YRKLfsavftDVWlfEQLL------GPEGQQANPALvEKWLTQLQMSH----KLElqdgkilnlKLSKGQKKRVALL 461
Cdd:COG4152 80 rglYPKM------KVG--EQLVylarlkGLSKAEAKRRA-DEWLERLGLGDrankKVE---------ELSKGNQQKVQLI 141
|
170
....*....|....
gi 1347499258 462 LALAEERDIILLDE 475
Cdd:COG4152 142 AALLHDPELLILDE 155
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-545 |
1.49e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqdsafsvGP------VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYR 396
Cdd:COG3845 6 LELRGITKRF-------GGvvanddVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 397 KL--------FSavftdvwLFEQL-------LGPEGQQA---NPALVEKWLTQLqmSHKLELQ---DGKILNlkLSKGQK 455
Cdd:COG3845 79 ALgigmvhqhFM-------LVPNLtvaenivLGLEPTKGgrlDRKAARARIREL--SERYGLDvdpDAKVED--LSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 456 KRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLpLMQQMGKTIFAISHDdhyfIH-----ADRLLEMRDGRlseL 530
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILR-RLAAEGKSIIFITHK----LRevmaiADRVTVLRRGK---V 219
|
250
....*....|....*.
gi 1347499258 531 TGE-ERDAASRDAVAR 545
Cdd:COG3845 220 VGTvDTAETSEEELAE 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
342-540 |
1.98e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.90 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFsaVFTDVWLFEQL-------LG 414
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGF--VFQHYALFRHMtvfdniaFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 415 ----PEGQQANPALVEKWLTQL----QMSHKLELQDGKilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRR 486
Cdd:PRK10851 99 ltvlPRRERPNAAAIKAKVTQLlemvQLAHLADRYPAQ-----LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 487 EFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGRLSEL-TGEE--RDAASR 540
Cdd:PRK10851 174 ELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAgTPDQvwREPATR 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
278-527 |
2.66e-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: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 278 PLLSAVGALPTLLSAQVAFNKLNKFdLAPFKAEF-----PRPQAfpdwqTLELRNVTFRYQDS-AFSVGPVNLTIRRGEL 351
Cdd:COG4618 287 PIEQAIGGWKQFVSARQAYRRLNEL-LAAVPAEPermplPRPKG-----RLSVENLTVVPPGSkRPILRGVSFSLEPGEV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 352 LFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVFTDVWLFeqllgpEG---------QQANP 422
Cdd:COG4618 361 LGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELF------DGtiaeniarfGDADP 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 423 ALVEKWLTQLQMsHKLelqdgkILNL-------------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFY 489
Cdd:COG4618 435 EKVVAAAKLAGV-HEM------ILRLpdgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALA 507
|
250 260 270
....*....|....*....|....*....|....*...
gi 1347499258 490 QVLLpLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:COG4618 508 AAIR-ALKARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
323-527 |
5.16e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL- 398
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVevlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 ---FSAVFTDVWLFEQLLGPE-----------GQQANPALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLAL 464
Cdd:PRK10535 85 rehFGFIFQRYHLLSHLTAAQnvevpavyaglERKQRLLRAQELLQRLGLEDRVEYQPS-----QLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
323-527 |
5.70e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.31 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVgpvNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEdyRKLFSAV 402
Cdd:PRK10771 2 LKLTDITWLYHHLPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQL-------LGpegqqANPAL---VEKWLTQLQMSHKLELQDG-KILNLKLSKGQKKRVALLLALAEERDII 471
Cdd:PRK10771 77 FQENNLFSHLtvaqnigLG-----LNPGLklnAAQREKLHAIARQMGIEDLlARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 472 LLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISH--DDHYFIhADRLLEMRDGRL 527
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHslEDAARI-APRSLVVADGRI 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
342-509 |
7.22e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 7.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDyrklfSAVFTDvwlfEQLLGPEGQQAN 421
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQN----EGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 422 PAL---------VEKWLTQLQMSHKLELQD-GKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQV 491
Cdd:PRK11248 91 VAFglqlagvekMQRLEIAHQMLKKVGLEGaEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
|
170
....*....|....*...
gi 1347499258 492 LLPLMQQMGKTIFAISHD 509
Cdd:PRK11248 171 LLKLWQETGKQVLLITHD 188
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
323-529 |
7.49e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.45 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDS-AFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFEQLLG-----PEGQQANPALVEKwltQLQMSHKLE----LQDGkiLN-------LKLSKGQKKRVALLLALA 465
Cdd:PRK11176 422 VSQNVHLFNDTIAnniayARTEQYSREQIEE---AARMAYAMDfinkMDNG--LDtvigengVLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 466 EERDIILLDEWAADQDPHFRREFYQVLLPLmqQMGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
349-527 |
8.02e-16 |
|
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: 76.56 E-value: 8.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAL-SAEK----PEDYRKLfSAVFTDVWLFEQL---------LG 414
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKkinlPPQQRKI-GLVFQQYALFPHLnvrenlafgLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 415 PEGQQANPALVEKWLTQLQMSHkleLQDGKIlnLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREfyqvLLP 494
Cdd:cd03297 102 RKRNREDRISVDELLDLLGLDH---LLNRYP--AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ----LLP 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1347499258 495 LMQQMGK-----TIFaISHD-DHYFIHADRLLEMRDGRL 527
Cdd:cd03297 173 ELKQIKKnlnipVIF-VTHDlSEAEYLADRIVVMEDGRL 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-530 |
8.91e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.54 E-value: 8.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 2 QLLLLVWRQyrWPFVAVMALSLASAALGIGLIAFINVRLIEMVDTSLSVlPEFLGLLLLLMAVTLGSQLALTALGHHFVF 81
Cdd:TIGR00958 151 RLLGLSGRD--WPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGP-PALASAIFFMCLLSIASSVSAGLRGGSFNY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 82 -------RLRSEFIKRILDTQVERVEQLGSASLLAGLTSDVRAI--TIAFvRLPELVQGIILTFGSAAYLAWLSSKMLAV 152
Cdd:TIGR00958 228 tmarinlRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsrSLSL-NVNVLLRNLVMLLGLLGFMLWLSPRLTMV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 153 TALWIAITIwggfvLVSRVY--KHMAVLRETEDKLYNDYQTVLEG-------------RKELTLNRERAEYIFNhlyipd 217
Cdd:TIGR00958 307 TLINLPLVF-----LAEKVFgkRYQLLSEELQEAVAKANQVAEEAlsgmrtvrsfaaeEGEASRFKEALEETLQ------ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 218 areyrhhIIRADTFHLSAVNWSN-IMMLGAIGLVFW------MANSLGWADTNVAATYSL-------TLLFLRTPLLSAV 283
Cdd:TIGR00958 376 -------LNKRKALAYAGYLWTTsVLGMLIQVLVLYyggqlvLTGKVSSGNLVSFLLYQEqlgeavrVLSYVYSGMMQAV 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 284 GAlptllSAQVafnklnkFDLAPFKAEFPRPQAF-PDWQT--LELRNVTFRYQDSafSVGPV----NLTIRRGELLFLIG 356
Cdd:TIGR00958 449 GA-----SEKV-------FEYLDRKPNIPLTGTLaPLNLEglIEFQDVSFSYPNR--PDVPVlkglTFTLHPGEVVALVG 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 357 GNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRK----------LFSAVFTDVWLFEQLLGPEGQQANPAlve 426
Cdd:TIGR00958 515 PSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRqvalvgqepvLFSGSVRENIAYGLTDTPDEEIMAAA--- 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 427 kwltQLQMSHKL--ELQDGKILNL-----KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQvllpLMQQM 499
Cdd:TIGR00958 592 ----KAANAHDFimEFPNGYDTEVgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE----SRSRA 663
|
570 580 590
....*....|....*....|....*....|.
gi 1347499258 500 GKTIFAISHDDHYFIHADRLLEMRDGRLSEL 530
Cdd:TIGR00958 664 SRTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
323-527 |
9.68e-16 |
|
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: 75.55 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQdsafsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL-FSA 401
Cdd:cd03215 5 LEVRGLSVKGA-----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VftdvwlfeqllgPEGQQANpALVekwltqLQMShkleLQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:cd03215 80 V------------PEDRKRE-GLV------LDLS----VAENIALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1347499258 482 PHFRREFYQVLLPLMQQmGKTIFAISHDDHYFIH-ADRLLEMRDGRL 527
Cdd:cd03215 137 VGAKAEIYRLIRELADA-GKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
322-488 |
1.79e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 75.21 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGRALSAEKPEDyRKL 398
Cdd:COG4136 1 MLSLENLTITLGGRPL-LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQ-RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 fSAVFTDVWLFEQL-----LG---PE--GQQANPALVEKWLTQLQMSHkLELQDGKilnlKLSKGQKKRVALLLALAEER 468
Cdd:COG4136 79 -GILFQDDLLFPHLsvgenLAfalPPtiGRAQRRARVEQALEEAGLAG-FADRDPA----TLSGGQRARVALLRALLAEP 152
|
170 180
....*....|....*....|
gi 1347499258 469 DIILLDEWAADQDPHFRREF 488
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQF 172
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
323-529 |
2.06e-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: 75.68 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLY-----QPQSGEILLDGRALSA--EKPEDY 395
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 RKLFSAVFTDVWLFE-----------QLLGPEGQQANPALVEKWLTQLQMSHklELQDgKILNLKLSKGQKKRVALLLAL 464
Cdd:cd03260 80 RRRVGMVFQKPNPFPgsiydnvayglRLHGIKLKEELDERVEEALRKAALWD--EVKD-RLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMgkTIFAISHDdhyfIH-----ADRLLEMRDGRLSE 529
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHN----MQqaarvADRTAFLLNGRLVE 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
323-527 |
3.05e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.99 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAV 402
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 F--TDVWLF----EQ--LLGPEGQQANPALVEKWLTQ-LQMSHKLELQDGkiLNLKLSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK13652 84 FqnPDDQIFsptvEQdiAFGPINLGLDEETVAHRVSSaLHMLGLEELRDR--VPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 474 DEWAADQDPHFRREFYQVLLPLMQQMGKT-IFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTvIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
342-527 |
3.39e-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: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEdYRKLFSAVF---TDVW----------L 408
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK-FLRRIGVVFgqkTQLWwdlpvidsfyL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 409 FEQLLGPEGQQANPALVEkwLTQLqmshkleLQDGKILNL---KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 485
Cdd:cd03267 119 LAAIYDLPPARFKKRLDE--LSEL-------LDLEELLDTpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1347499258 486 REFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGRL 527
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
323-526 |
4.19e-15 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 75.12 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG-EILLDGRALSAEKPEDYRK---L 398
Cdd:COG1119 4 LELRNVTVRRGGKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKrigL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 FSAV------------------FTDVW-LFEQllgPEGQQAnpALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVA 459
Cdd:COG1119 83 VSPAlqlrfprdetvldvvlsgFFDSIgLYRE---PTDEQR--ERARELLELLGLAHLADRPFG-----TLSQGEQRRVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 460 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHA-DRLLEMRDGR 526
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
323-529 |
5.00e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNV--TFRYQDSAF------SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALS----AE 390
Cdd:PRK15112 5 LEVRNLskTFRYRTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 391 KPEDYRKLFSAVFTDvwlfeqlLGPE---GQ----------QANPALVEKWLTQLQMSHKLELQDGKILNLKLSKGQKKR 457
Cdd:PRK15112 85 RSQRIRMIFQDPSTS-------LNPRqriSQildfplrlntDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 458 VALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGRLSE 529
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVE 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
340-527 |
9.55e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.20 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 340 GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYqPQSGEILLDGRALSAEKPED---YRKLFS----AVFT-DVWLFEQ 411
Cdd:PRK03695 13 GPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAElarHRAYLSqqqtPPFAmPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 412 LLGPEGqqANPALVEKWLTQLqmSHKLELQD--GKILNlKLSKGQKKRV---ALLL----ALAEERDIILLDEWAADQDP 482
Cdd:PRK03695 92 LHQPDK--TRTEAVASALNEV--AEALGLDDklGRSVN-QLSGGEWQRVrlaAVVLqvwpDINPAGQLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1347499258 483 HFRREFYQvLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:PRK03695 167 AQQAALDR-LLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
342-527 |
1.25e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.04 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLfSAV----------FT--DVWLF 409
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAVlpqhsslsfpFTveEVVAM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 410 EQLLGPEGQQANPALVEKWLTQLQMSHkleLQDGKIlnLKLSKGQKKRVALLLALA------EERDIILLDEWAADQDPH 483
Cdd:PRK13548 100 GRAPHGLSRAEDDALVAAALAQVDLAH---LAGRDY--PQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1347499258 484 FRREFYQVLLPLMQQMGKTIFAISHD----DHYfihADRLLEMRDGRL 527
Cdd:PRK13548 175 HQHHVLRLARQLAHERGLAVIVVLHDlnlaARY---ADRIVLLHQGRL 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
325-527 |
1.38e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 325 LRNVTFRY-QDSAFSVGPVN---LTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSA-----EKPEDY 395
Cdd:PRK13645 9 LDNVSYTYaKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 RKLFSAVFT--DVWLFEQLL------GPEGQQANPALVEKWLTQLQMSHKLELQDGKILNLKLSKGQKKRVALLLALAEE 467
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQETIekdiafGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 468 RDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
323-534 |
1.62e-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: 72.79 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEkPEDYRKLFSAV 402
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRE-PREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQLLGPEGQQ--------ANPALVEKWLTQLQMSHKLELQDgKILNlKLSKGQKKRVALLLALAEERDIILLD 474
Cdd:cd03265 79 FQDLSVDDELTGWENLYiharlygvPGAERRERIDELLDFVGLLEAAD-RLVK-TYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 475 EWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL-SELTGEE 534
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRIiAEGTPEE 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
342-529 |
1.63e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA----VFTDVWLFEQLLGPEG 417
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhvgfVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 418 QQAnPALVE------------KWLTQLQMSHKLelqdgKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 485
Cdd:PRK10584 109 VEL-PALLRgessrqsrngakALLEQLGLGKRL-----DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1347499258 486 REFYQVLLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
336-530 |
1.97e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.07 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 336 AFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALS----AEKPEDYRKLFSAVFTDVWLFEQ 411
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRRKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 412 LLGPEG-----QQANPALVEKWLTQLQMSHKLELQD-GKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 485
Cdd:PRK10070 121 MTVLDNtafgmELAGINAEERREKALDALRQVGLENyAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1347499258 486 REFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRLSEL 530
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQV 246
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
323-509 |
2.03e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALsAEKP--EDYRKLFS 400
Cdd:PRK11300 6 LSVSGLMMRF-GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-EGLPghQIARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFTDVWLF------EQLLGPEGQQAN----------PAL-------VEKWLTQLQMSHKLELQDGKILNlkLSKGQKKR 457
Cdd:PRK11300 84 RTFQHVRLFremtviENLLVAQHQQLKtglfsgllktPAFrraeseaLDRAATWLERVGLLEHANRQAGN--LAYGQQRR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 458 VALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD 509
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-534 |
2.39e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.44 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqdsafsvGP------VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYR 396
Cdd:COG1129 5 LEMRGISKSF-------GGvkaldgVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 397 KL-FSAVFTDVWLFEQL-------LGPEgqQANPALV---------EKWLTQLQMShklelqdgkiLNLK-----LSKGQ 454
Cdd:COG1129 78 AAgIAIIHQELNLVPNLsvaenifLGRE--PRRGGLIdwramrrraRELLARLGLD----------IDPDtpvgdLSVAQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 455 KKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL------ 527
Cdd:COG1129 146 QQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRlDEVFEIADRVTVLRDGRLvgtgpv 224
|
....*..
gi 1347499258 528 SELTGEE 534
Cdd:COG1129 225 AELTEDE 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
323-527 |
2.51e-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: 71.86 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRalSAEKPEDYRKLFSAV 402
Cdd:cd03268 1 LKTNDLTKTYGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 403 FTDVWLFEQLLGPE-------GQQANPALVEKWLTQLQMSHklelqDGKILNLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03268 78 IEAPGFYPNLTAREnlrllarLLGIRKKRIDEVLDVVGLKD-----SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 476 WAADQDPHFRREFYQVLLPLMQQmGKTIFAISHddhyFIH-----ADRLLEMRDGRL 527
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQ-GITVLISSH----LLSeiqkvADRIGIINKGKL 204
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
312-529 |
3.25e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 75.52 E-value: 3.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 312 PRPQAFPDWQTL-----ELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRA 386
Cdd:PRK10790 325 PRQQYGNDDRPLqsgriDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 387 LSAEKPEDYRKLFSAVFTD-VWLFEQLLG--PEGQQANPALVEKWLTQLQ-------MSHKLELQDGKILNlKLSKGQKK 456
Cdd:PRK10790 405 LSSLSHSVLRQGVAMVQQDpVVLADTFLAnvTLGRDISEEQVWQALETVQlaelarsLPDGLYTPLGEQGN-NLSVGQKQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 457 RVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQmgKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
317-529 |
3.84e-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: 71.29 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 317 FPDWQTLELRNVTFRYQ-DSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDY 395
Cdd:cd03369 1 WPEHGEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 RKLFSAVFTDVWLF----EQLLGPEGQQanpalvekwlTQLQMSHKLELQDGkilNLKLSKGQKKRVALLLALAEERDII 471
Cdd:cd03369 81 RSSLTIIPQDPTLFsgtiRSNLDPFDEY----------SDEEIYGALRVSEG---GLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 472 LLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
323-475 |
4.01e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.02 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFryqdsafSVGP------VNLTIRRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGRALSAEKPED 394
Cdd:COG0396 1 LEIKNLHV-------SVEGkeilkgVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 --------------------YRKLFSAVFTdvwlfEQLLGPEGQQANPALVEKWLTQLQMSHKLeLQDGkiLNLKLSKGQ 454
Cdd:COG0396 74 raragiflafqypveipgvsVSNFLRTALN-----ARRGEELSAREFLKLLKEKMKELGLDEDF-LDRY--VNEGFSGGE 145
|
170 180
....*....|....*....|.
gi 1347499258 455 KKRVALLLALAEERDIILLDE 475
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDE 166
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
345-520 |
4.70e-14 |
|
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: 72.06 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 345 TIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAeKPE----DY----RKLFSAVFTDVWLFEQLlgpE 416
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-KPQyikaDYegtvRDLLSSITKDFYTHPYF---K 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 417 GQQANPALVEKWLTQlqmshklELQDgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLM 496
Cdd:cd03237 97 TEIAKPLQIEQILDR-------EVPE-------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*.
gi 1347499258 497 QQMGKTIFAISHdDHYFIH--ADRLL 520
Cdd:cd03237 163 ENNEKTAFVVEH-DIIMIDylADRLI 187
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
324-529 |
5.24e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.61 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVF 403
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 404 TDVWLFEQ------LLGPEGqqANPALVEKWLTQLQMSHKLELQDGKILNL------KLSKGQKKRVALLLALAEERDII 471
Cdd:PRK13657 416 QDAGLFNRsiedniRVGRPD--ATDEEMRAAAERAQAHDFIERKPDGYDTVvgergrQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 472 LLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:PRK13657 494 ILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
324-529 |
5.73e-14 |
|
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: 71.42 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYqDSAFSVG---PVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFS 400
Cdd:cd03249 2 EFKNVSFRY-PSRPDVPilkGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFTDVWLFEQ------LLGpegqqANPALVEkwlTQLQMSHKLELQDgKILNL-------------KLSKGQKKRVALL 461
Cdd:cd03249 81 LVSQEPVLFDGtiaeniRYG-----KPDATDE---EVEEAAKKANIHD-FIMSLpdgydtlvgergsQLSGGQKQRIAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 462 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMqqMGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
323-527 |
5.81e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.22 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAL--SAEKPEDYRKLFS 400
Cdd:PRK11432 7 VVLKNITKRFGSNTV-IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 --AVFTDVWLFE------QLLGpegqqanpalVEKWLTQLQMSHKLELQDgkilnL---------KLSKGQKKRVALLLA 463
Cdd:PRK11432 86 syALFPHMSLGEnvgyglKMLG----------VPKEERKQRVKEALELVD-----LagfedryvdQISGGQQQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 464 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDD-HYFIHADRLLEMRDGRL 527
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQsEAFAVSDTVIVMNKGKI 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
323-492 |
8.05e-14 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 70.68 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGeLLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL---- 398
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIgylp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 ----FSAVFTdVWLFEQLLG-----PEGQQanPALVEKWLTQLQMshkLELQDGKIlnLKLSKGQKKRVALLLALAEERD 469
Cdd:cd03264 79 qefgVYPNFT-VREFLDYIAwlkgiPSKEV--KARVDEVLELVNL---GDRAKKKI--GSLSGGMRRRVGIAQALVGDPS 150
|
170 180
....*....|....*....|...
gi 1347499258 470 IILLDEWAADQDPHFRREFYQVL 492
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLL 173
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
323-547 |
9.24e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 9.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqdSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLfsa 401
Cdd:PRK15439 12 LCARSISKQY--SGVEVlKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 vftDVWLFEQ--------------LLGPEGQQANPALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEE 467
Cdd:PRK15439 87 ---GIYLVPQepllfpnlsvkeniLFGLPKRQASMQKMKQLLAALGCQLDLDSSAG-----SLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 468 RDIILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHDDHYFIH-ADRLLEMRDGR--LSELTGEERDAASRDAVA 544
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQlADRISVMRDGTiaLSGKTADLSTDDIIQAIT 237
|
...
gi 1347499258 545 RTA 547
Cdd:PRK15439 238 PAA 240
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
342-522 |
1.04e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.57 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR---ALSAEKPEDYRKL----FSAVFTDVWLFEQLLG 414
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGarvAYVPQRSEVPDSLpltvRDLVAMGRWARRGLWR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 415 PEGQQANpALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLP 494
Cdd:NF040873 91 RLTRDDR-AAVDDALERVGLADLAGRQLG-----ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAE 164
|
170 180
....*....|....*....|....*...
gi 1347499258 495 LMQQmGKTIFAISHDDHYFIHADRLLEM 522
Cdd:NF040873 165 EHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
323-526 |
1.17e-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: 68.24 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSA-FSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRalsaekpedyrklfsa 401
Cdd:cd03221 1 IELENLSKTYGGKLlLK--DISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST---------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 vfTDVWLFEQllgpegqqanpalvekwltqlqmshklelqdgkilnlkLSKGQKKRVALLLALAEERDIILLDEwaadqd 481
Cdd:cd03221 63 --VKIGYFEQ--------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE------ 96
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1347499258 482 P--HFRREFYQVLLPLMQQMGKTIFAISHdDHYFIH--ADRLLEMRDGR 526
Cdd:cd03221 97 PtnHLDLESIEALEEALKEYPGTVILVSH-DRYFLDqvATKIIELEDGK 144
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
345-527 |
1.69e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 345 TIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI----LLDGRALSAEKPEDY------------RKLFSAVFT--DV 406
Cdd:PRK13631 48 TFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNpyskkiknfkelRRRVSMVFQfpEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 407 WLFEQ------LLGPE--GQQANPA--LVEKWLTQLQMSHK-LELQDgkilnLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK13631 128 QLFKDtiekdiMFGPValGVKKSEAkkLAKFYLNKMGLDDSyLERSP-----FGLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 476 WAADQDPHFRREFYQVLLPLMQQmGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:PRK13631 203 PTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
323-527 |
2.32e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.09 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEiLLDGRALSAEKPEDYRKLFS-- 400
Cdd:PRK11247 13 LLLNAVSKRYGERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEAREDTRLMFQda 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 ------AVFTDVWLfeQLLGPEGQQANPALVEKWLTqlqmSHKLELQDGkilnlkLSKGQKKRVALLLALAEERDIILLD 474
Cdd:PRK11247 91 rllpwkKVIDNVGL--GLKGQWRDAALQALAAVGLA----DRANEWPAA------LSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 475 EWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGRL 527
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
342-527 |
2.46e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL-------LDGRALSAE-----------------KPEDYRK 397
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdekNKKKTKEKEkvleklviqktrfkkikKIKEIRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 LFSAVF--TDVWLFEQ------LLGPEGQQANPALVEKwltqlQMSHKLELQDGKILNLK-----LSKGQKKRVALLLAL 464
Cdd:PRK13651 106 RVGVVFqfAEYQLFEQtiekdiIFGPVSMGVSKEEAKK-----RAAKYIELVGLDESYLQrspfeLSGGQKRRVALAGIL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDlDNVLEWTKRTIFFKDGKI 243
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
341-543 |
3.38e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 341 PVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDyrklfsAVFTDVwlfeqLLGPEGQQA 420
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD------AIRAGI-----MLCPEDRKA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 421 ---------------------NPA---LVEKWLTQL------QMSHKLELQDGKILNlkLSKGQKKRVALLLALAEERDI 470
Cdd:PRK11288 340 egiipvhsvadninisarrhhLRAgclINNRWEAENadrfirSLNIKTPSREQLIMN--LSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 471 ILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHDDHYFIH-ADRLLEMRDGRLS-ELTgeeRDAASRDAV 543
Cdd:PRK11288 418 ILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGvADRIVVMREGRIAgELA---REQATERQA 488
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
323-508 |
3.61e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.15 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQ-DSAFS---VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGRALSAEKPEDYRK 397
Cdd:PRK13643 2 IKFEKVNYTYQpNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 LFSAV-----FTDVWLFEQLL------GPEG-----QQANPALVEKwLTQLQMSHKLELQDgkilNLKLSKGQKKRVALL 461
Cdd:PRK13643 82 VRKKVgvvfqFPESQLFEETVlkdvafGPQNfgipkEKAEKIAAEK-LEMVGLADEFWEKS----PFELSGGQMRRVAIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1347499258 462 LALAEERDIILLDEWAADQDPHFRREFYQvLLPLMQQMGKTIFAISH 508
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTH 202
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
323-509 |
6.15e-13 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 69.70 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV----GpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGRALSAEKPEDY 395
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkavdG-VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 RKL----FSAVFTD-------VW-LFEQL-------LGPEGQQANpALVEKWLTQLQMShklelQDGKILNL---KLSKG 453
Cdd:COG0444 81 RKIrgreIQMIFQDpmtslnpVMtVGDQIaeplrihGGLSKAEAR-ERAIELLERVGLP-----DPERRLDRyphELSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 454 QKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD 509
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
323-532 |
7.56e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSA-FSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-----------DGRALSAE 390
Cdd:COG0488 316 LELEGLSKSYGDKTlLD--DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgetvkigyfdqHQEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 391 KPedyrklfsavftdvwLFEQL--LGPEGQQANP-ALVEKWLTQLQMSHKlelqdgKIlnLKLSKGQKKRVALLLALAEE 467
Cdd:COG0488 394 KT---------------VLDELrdGAPGGTEQEVrGYLGRFLFSGDDAFK------PV--GVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 468 RDIILLDEWAADQDPHFRrefyQVLLPLMQQMGKTIFAISHdDHYFI--HADRLLEMRDGRLSELTG 532
Cdd:COG0488 451 PNVLLLDEPTNHLDIETL----EALEEALDDFPGTVLLVSH-DRYFLdrVATRILEFEDGGVREYPG 512
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
325-545 |
1.02e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 325 LRNVTFRYQDSA-FSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRA----LSAEKPED-YRKL 398
Cdd:COG0488 1 LENLSKSFGGRPlLD--DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigyLPQEPPLDdDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 FSAV---FTDVW-LFEQLLGPEGQQANPALVEKWLTQLQmsHKLELQDG--------KILN-LK------------LSKG 453
Cdd:COG0488 79 LDTVldgDAELRaLEAELEELEAKLAEPDEDLERLAELQ--EEFEALGGweaearaeEILSgLGfpeedldrpvseLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 454 QKKRVALLLALAEERDIILLDE-----------WAADqdphfrrefyqvllpLMQQMGKTIFAISHdDHYFIH--ADRLL 520
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEptnhldlesieWLEE---------------FLKNYPGTVLVVSH-DRYFLDrvATRIL 220
|
250 260 270
....*....|....*....|....*....|....
gi 1347499258 521 EMRDGRLSELTG---------EERDAASRDAVAR 545
Cdd:COG0488 221 ELDRGKLTLYPGnysayleqrAERLEQEAAAYAK 254
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
323-527 |
2.13e-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: 66.01 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGRALSAEKPEDYRKLfs 400
Cdd:cd03217 1 LEIKDLHVSVGGKEILKG-VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFTdvwlfeqllgpeGQQANPAlvekwLTQLQMSHKLelqdgKILNLKLSKGQKKRVALLLALAEERDIILLDE----- 475
Cdd:cd03217 78 GIFL------------AFQYPPE-----IPGVKNADFL-----RYVNEGFSGGEKKRNEILQLLLLEPDLAILDEpdsgl 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 476 ------WAADQDPHFRREfyqvllplmqqmGKTIFAISHDDHY--FIHADRLLEMRDGRL 527
Cdd:cd03217 136 didalrLVAEVINKLREE------------GKSVLIITHYQRLldYIKPDRVHVLYDGRI 183
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
303-519 |
2.26e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.32 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 303 DLAPFKAEFPRPQAFPDwQTLELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL 382
Cdd:PRK13536 23 HQGISEAKASIPGSMST-VAIDLAGVSKSYGDKAV-VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 383 DG-----RALSAEK-----PE-DYRKLFSAVFTDVWLFEQLLGPEGQQAN---PALVEkwLTQLQMSHKLELQDgkilnl 448
Cdd:PRK13536 101 LGvpvpaRARLARArigvvPQfDNLDLEFTVRENLLVFGRYFGMSTREIEaviPSLLE--FARLESKADARVSD------ 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 449 kLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAIShddHYFIHADRL 519
Cdd:PRK13536 173 -LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTT---HFMEEAERL 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
323-519 |
2.45e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL---- 398
Cdd:PRK13537 8 IDFRNVEKRYGDKLV-VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 --------FSaVFTDVWLFEQLLGPEGQQANpALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDI 470
Cdd:PRK13537 87 qfdnldpdFT-VRENLLVFGRYFGLSAAAAR-ALVPPLLEFAKLENKADAKVG-----ELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1347499258 471 ILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAIShddHYFIHADRL 519
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTT---HFMEEAERL 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
342-527 |
3.44e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.93 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG----RALSAEKPEDYRKLFSAVFTDVWLFEQLLGPEG 417
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqHYASKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 418 QQANPALVEKWLTQLQMSHKLELQDGKILNL------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQV 491
Cdd:PRK10253 106 RYPHQPLFTRWRKEDEEAVTKAMQATGITHLadqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 1347499258 492 LLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:PRK10253 186 LSELNREKGYTLAAVLHDlNQACRYASHLIALREGKI 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
342-525 |
3.45e-12 |
|
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: 65.82 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDY--RKLFSAVFT--DVWLFEQLL---- 413
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsRNRYSVAYAaqKPWLLNATVeeni 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 414 ---GPEGQQANPALVEKWLTQ-----LQMSHKLELQDGKIlnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 485
Cdd:cd03290 100 tfgSPFNKQRYKAVTDACSLQpdidlLPFGDQTEIGERGI---NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1347499258 486 REFYQV-LLPLMQQMGKTIFAISHDDHYFIHADRLLEMRDG 525
Cdd:cd03290 177 DHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
282-529 |
4.86e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.33 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 282 AVGA---LPTLLSAQVAFNKLNKFDLAPFKAEfprpqafpdwqTLELRN-VTFRYQDSAFsVGPVNLTIRRGELLFLIGG 357
Cdd:PRK11174 317 AVGAaesLVTFLETPLAHPQQGEKELASNDPV-----------TIEAEDlEILSPDGKTL-AGPLNFTLPAGQRIALVGP 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 358 NGSGKSTLAMLLTGlYQPQSGEILLDGRALSAEKPEDYRKLFSAVFTDVWLFEQ------LLGpeGQQANPALVEKWLTQ 431
Cdd:PRK11174 385 SGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGtlrdnvLLG--NPDASDEQLQQALEN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 432 LQMSHKLELQ----DGKI--LNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFA 505
Cdd:PRK11174 462 AWVSEFLPLLpqglDTPIgdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLM 539
|
250 260
....*....|....*....|....
gi 1347499258 506 ISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:PRK11174 540 VTHQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-535 |
4.98e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.26 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAeKPEDYR-KLFSAVFTDVWL--------FEQL 412
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-LPEYKRaKYIGRVFQDPMMgtapsmtiEENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 413 -----------LGPEGQQANPALVEKWLTQLQMShkLELQdgkiLNLK---LSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:COG1101 104 alayrrgkrrgLRRGLTKKRRELFRELLATLGLG--LENR----LDTKvglLSGGQRQALSLLMATLTKPKLLLLDEHTA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 479 DQDPHfRREFyqvLLPLMQQMGK----TIFAISHDDHYFI-HADRLLEMRDGR-LSELTGEER 535
Cdd:COG1101 178 ALDPK-TAAL---VLELTEKIVEennlTTLMVTHNMEQALdYGNRLIMMHEGRiILDVSGEEK 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
342-509 |
5.18e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.56 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVFTDVWL-FE---------- 410
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEfdvrqvvemg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 411 -----QLLGPEGqQANPALVEKWLTQLQMShklELQDGKILNlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHfr 485
Cdd:PRK09536 102 rtphrSRFDTWT-ETDRAAVERAMERTGVA---QFADRPVTS--LSGGERQRVLLARALAQATPVLLLDEPTASLDIN-- 173
|
170 180
....*....|....*....|....*...
gi 1347499258 486 refYQV-LLPLMQQM---GKTIFAISHD 509
Cdd:PRK09536 174 ---HQVrTLELVRRLvddGKTAVAAIHD 198
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
325-509 |
5.49e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.36 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 325 LRNVTFRYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDyrKLFSAVFT 404
Cdd:PRK11000 6 LRNVTKAYGDVVISKD-INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 405 DVWLFEQL-------LGPEGQQANPALVEKWLTQ----LQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:PRK11000 83 SYALYPHLsvaenmsFGLKLAGAKKEEINQRVNQvaevLQLAHLLDRKPK-----ALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1347499258 474 DEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD 509
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
345-530 |
6.02e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.27 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 345 TIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAlsAEKP-----------EDY-RKLFSAVFTDVWLFEQL 412
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKI--SYKPqyispdydgtvEEFlRSANTDDFGSSYYKTEI 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 413 LGPegqqanpalvekwltqlqmshkleLQDGKIL--NLK-LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFY 489
Cdd:COG1245 440 IKP------------------------LGLEKLLdkNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 490 QVLLPLMQQMGKTIFAISHdDHYFIH--ADRLL----------------EMRDGR---LSEL 530
Cdd:COG1245 496 KAIRRFAENRGKTAMVVDH-DIYLIDyiSDRLMvfegepgvhghasgpmDMREGMnrfLKEL 556
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
323-527 |
7.79e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.52 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRY----QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI----------------LL 382
Cdd:TIGR03269 280 IKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 383 DGRAlsaeKP------EDYrklfsAVFTDVWLFEQLLGPEGQQANPAL-VEKWLTQLQMSHKLELQDGKILNL---KLSK 452
Cdd:TIGR03269 360 RGRA----KRyigilhQEY-----DLYPHRTVLDNLTEAIGLELPDELaRMKAVITLKMVGFDEEKAEEILDKypdELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 453 GQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKI 506
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
338-527 |
8.47e-12 |
|
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: 68.50 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 338 SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAL---------SAEKPEDYRKLFS--AVFTDV 406
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnldavrqSLGMCPQHNILFHhlTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 407 WLFEQLLGPEGQQANPALvEKWLTQLQMSHKL--ELQDgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHF 484
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEM-EAMLEDTGLHHKRneEAQD-------LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1347499258 485 RREFYQVLLPLmqQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:TIGR01257 1097 RRSIWDLLLKY--RSGRTIIMSTHHmDEADLLGDRIAIISQGRL 1138
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
342-482 |
1.21e-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: 64.49 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAeKPEDYRKLF--------SAVFTDVWLFEQLL 413
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-LPMHKRARLgigylpqeASIFRKLTVEENIL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 414 GpegqqanpALVEKWLTQLQMSHKLE--LQDGKILNLK------LSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:cd03218 98 A--------VLEIRGLSKKEREEKLEelLEEFHITHLRkskassLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
15-173 |
1.23e-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: 65.53 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 15 FVAVMALSLASAALGIGLIAFINvRLIEMVDTSLSVLPeflglLLLLMAVTLGSQLALTAL--------GHHFVFRLRSE 86
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVK-NLIDALSAGGSSGG-----LLALLVALFLLQAVLSALssyllgrtGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 87 FIKRILDTQVERVEQLGSASLLAGLTSDV----RAITIAfvrLPELVQGIILTFGSAAYLAWLSSKMLAVTALWIAITIW 162
Cdd:cd18551 75 LWRRLLRLPVSFFDRRRSGDLVSRVTNDTtllrELITSG---LPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170
....*....|.
gi 1347499258 163 GGFVLVSRVYK 173
Cdd:cd18551 152 IILPLGRRIRK 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
345-525 |
1.32e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 345 TIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAlsAEKPEdYRKLFSAVFTDVWLFeqllgpegqQANPAL 424
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKI--SYKPQ-YIKPDYDGTVEDLLR---------SITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 425 VEKWLtQLQMSHKLELQdgKIL--NLK-LSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGK 501
Cdd:PRK13409 429 GSSYY-KSEIIKPLQLE--RLLdkNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREA 505
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1347499258 502 TIFAISHdDHYFIH--ADRLL----------------EMRDG 525
Cdd:PRK13409 506 TALVVDH-DIYMIDyiSDRLMvfegepgkhghasgpmDMREG 546
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
342-527 |
1.45e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTL----AMLLTGLYQPQSgEILLDGRALSAEK--PEDYRKlfSAVFTDvWLFEQ---- 411
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITGDKSAGS-HIELLGRTVQREGrlARDIRK--SRANTG-YIFQQfnlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 412 ---------LLGPEGQQANPALVEKWLTQLQMSHKLE-LQDGKILNL------KLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK09984 99 nrlsvlenvLIGALGSTPFWRTCFSWFTREQKQRALQaLTRVGMVHFahqrvsTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 476 WAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD-DHYFIHADRLLEMRDGRL 527
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHV 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
322-529 |
4.41e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.23 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-----GEILLDG-RALSAEKP--E 393
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHG-IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvGDITIDTaRSLSQQKGliR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 394 DYRKLFSAVFTDVWLFEQLLGPEGQQANPALVEKWLTQLQMSHKLELQDGKILNLK-------LSKGQKKRVALLLALAE 466
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKetsyprrLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQQMgKTIFAISHDDHYFIH-ADRLLEMRDGRLSE 529
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
322-527 |
4.48e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDY-RKLfs 400
Cdd:PRK10575 11 TFALRNVSFRVPGRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 avftdVWLFEQLLGPEGQQANpALVE----KW---LTQLQMSHKLELQDG-KILNLK---------LSKGQKKRVALLLA 463
Cdd:PRK10575 88 -----AYLPQQLPAAEGMTVR-ELVAigryPWhgaLGRFGAADREKVEEAiSLVGLKplahrlvdsLSGGERQRAWIAML 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 464 LAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFI-HADRLLEMRDGRL 527
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEM 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
323-514 |
4.51e-11 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 62.84 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPED-------Y 395
Cdd:cd03224 1 LEVENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragigY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 ----RKLFSA--VFTDVWLFEQLLGPEGQQAN--------PALVEKWLTQLQmshklelqdgkilnlKLSKGQKKRVALL 461
Cdd:cd03224 80 vpegRRIFPEltVEENLLLGAYARRRAKRKARlervyelfPRLKERRKQLAG---------------TLSGGEQQMLAIA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 462 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQQMGKTI--------FAISHDDHYFI 514
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTIllveqnarFALEIADRAYV 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
342-543 |
4.61e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL-FSAVFTDVWLFEQLLGPEGQQA 420
Cdd:PRK09700 24 VNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLENLYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 421 NPALVEK--------WLTQLQ----MSHKLELQ---DGKILNLKLSKGQKKRVALLLALaeERDIILLDEWAADqdphFR 485
Cdd:PRK09700 104 GRHLTKKvcgvniidWREMRVraamMLLRVGLKvdlDEKVANLSISHKQMLEIAKTLML--DAKVIIMDEPTSS----LT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 486 REFYQVLLPLMQQM---GKTIFAISHDDHYFIH-ADRLLEMRDGRlSELTGEERDAASRDAV 543
Cdd:PRK09700 178 NKEVDYLFLIMNQLrkeGTAIVYISHKLAEIRRiCDRYTVMKDGS-SVCSGMVSDVSNDDIV 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-547 |
4.84e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDyrKLFSAVftdVWLfeqllgPEGQQAN 421
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ--RLARGL---VYL------PEDRQSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 422 PALVE---KW----LTQLQMShkLELQDGK----------ILNLK----------LSKGQKKRVALLLALAEERDIILLD 474
Cdd:PRK15439 351 GLYLDaplAWnvcaLTHNRRG--FWIKPARenavleryrrALNIKfnhaeqaartLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1347499258 475 EWAADQDPHFRREFYQVLLPLMQQMGKTIFaISHDDHYFIH-ADRLLEMRDGRLS-ELTGEerdAASRDAVARTA 547
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQNVAVLF-ISSDLEEIEQmADRVLVMHQGEISgALTGA---AINVDTIMRLA 499
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
324-508 |
5.49e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 64.05 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRK--- 397
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 ----------LFSA--VFTDVWLFEQLLGpegqqANPALVEKWLTQLqmshkLELQDgkiLNLK-------LSKGQKKRV 458
Cdd:PRK11153 83 qigmifqhfnLLSSrtVFDNVALPLELAG-----TPKAEIKARVTEL-----LELVG---LSDKadrypaqLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1347499258 459 ALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISH 508
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
323-547 |
5.62e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqdsafSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKP---------- 392
Cdd:COG1129 257 LEVEGLSVGG-----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdairagiay 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 393 --EDyRK---LF----------SAVFTDVWLFeQLLGPEGQQanpALVEKWLTQLQMshKLELQDGKILNlkLSKG--QK 455
Cdd:COG1129 332 vpED-RKgegLVldlsirenitLASLDRLSRG-GLLDRRRER---ALAEEYIKRLRI--KTPSPEQPVGN--LSGGnqQK 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 456 krVALLLALAEERDIILLDEwaadqdPhFR-------REFYQvllpLMQQM---GKTIFAISHDDHYFIH-ADRLLEMRD 524
Cdd:COG1129 403 --VVLAKWLATDPKVLILDE------P-TRgidvgakAEIYR----LIRELaaeGKAVIVISSELPELLGlSDRILVMRE 469
|
250 260
....*....|....*....|....
gi 1347499258 525 GRLS-ELTGEErdaASRDAVARTA 547
Cdd:COG1129 470 GRIVgELDREE---ATEEAIMAAA 490
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
323-475 |
1.02e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.12 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLF--- 399
Cdd:PRK13540 2 LDVIELDFDYHDQPL-LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCfvg 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 400 --SAVFTDVWLFEQLLGPEGQQANPALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK13540 81 hrSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCG-----LLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
323-529 |
1.36e-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: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL- 398
Cdd:COG1135 2 IELENLSKTFPTKGGPVtalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 --FSAVFtdvwlfeqllgpegQQANpalvekwltqLQMS--------HKLELQD----------GKILNL---------- 448
Cdd:COG1135 82 rkIGMIF--------------QHFN----------LLSSrtvaenvaLPLEIAGvpkaeirkrvAELLELvglsdkaday 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 449 --KLSKGQKKRVALLLALAEERDIILLDEwaADQ--DPHFRREFYQVLLPLMQQMGKTIFAISHDdhyfIH-----ADRL 519
Cdd:COG1135 138 psQLSGGQKQRVGIARALANNPKVLLCDE--ATSalDPETTRSILDLLKDINRELGLTIVLITHE----MDvvrriCDRV 211
|
250
....*....|
gi 1347499258 520 LEMRDGRLSE 529
Cdd:COG1135 212 AVLENGRIVE 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
342-529 |
1.46e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.91 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPED-------------YRKLFSAVFT--DV 406
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTMVFQhfNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 407 WLFE-----------QLLGPEGQQANPALVeKWLTQLQMShklELQDGKiLNLKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK10619 104 WSHMtvlenvmeapiQVLGLSKQEARERAV-KYLAKVGID---ERAQGK-YPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 476 WAADQDPHFRREfyqvLLPLMQQM---GKTIFAISHDDHYFIH-ADRLLEMRDGRLSE 529
Cdd:PRK10619 179 PTSALDPELVGE----VLRIMQQLaeeGKTMVVVTHEMGFARHvSSHVIFLHQGKIEE 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
322-529 |
1.69e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.57 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRA--LSAE-KPEDYRKL 398
Cdd:PRK11124 2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTpSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 ---FSAVFT--DVW--------LFE---QLLGPEGQQANpALVEKWLTQLQMSHKLELqdgkiLNLKLSKGQKKRVALLL 462
Cdd:PRK11124 81 rrnVGMVFQqyNLWphltvqqnLIEapcRVLGLSKDQAL-ARAEKLLERLRLKPYADR-----FPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 463 ALAEERDIILLDEWAADQDPHFRREFYQVLLPLmQQMGKTIFAISHD-DHYFIHADRLLEMRDGRLSE 529
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEvEVARKTASRVVYMENGHIVE 221
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
321-546 |
1.76e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.64 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 321 QTLELRNVTFryQDSAFSVGPVNLTIRRGELLFLIGGNGSGKS-----TLAMLLTGLYQpQSGEILLDGRALSAEK---- 391
Cdd:PRK10418 3 QQIELRNIAL--QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVAPCAlrgr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 392 -----PEDYRKLFSAVFTDVWLFEQLLGPEGQQANPAlvekwltqlQMSHKLE---LQD-GKILNL---KLSKGQKKRVA 459
Cdd:PRK10418 80 kiatiMQNPRSAFNPLHTMHTHARETCLALGKPADDA---------TLTAALEavgLENaARVLKLypfEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 460 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGRLSElTGEERD-- 536
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVE-QGDVETlf 229
|
250
....*....|
gi 1347499258 537 AASRDAVART 546
Cdd:PRK10418 230 NAPKHAVTRS 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
257-529 |
2.09e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 257 LGWADTNVAATYSLTLL-FLRTPLlsavGALPTLLS----AQVAFNKLNKFDLAPFKAEFPRPQAFPDWQTLELRNVTFR 331
Cdd:PLN03232 548 LGGDLTPARAFTSLSLFaVLRSPL----NMLPNLLSqvvnANVSLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFS 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 332 Y--QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSgEILLDGRALSAEKPEdYRKLFSAVFTDVWLF 409
Cdd:PLN03232 624 WdsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVVIRGSVAYVPQ-VSWIFNATVRENILF 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 410 eqllgpeGQQANPALVEKWLTQLQMSHKLELQDGKILN------LKLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:PLN03232 702 -------GSDFESERYWRAIDVTALQHDLDLLPGRDLTeigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1347499258 484 FRREFYQVLLPLMQQmGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:PLN03232 775 VAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
322-529 |
3.19e-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: 62.53 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:COG5265 357 EVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFEQLLG-------PEgqqANPALVEKWLTQLQMSHKLE-LQDGkiLN-------LKLSKGQKKRVALLLALAE 466
Cdd:COG5265 437 VPQDTVLFNDTIAyniaygrPD---ASEEEVEAAARAAQIHDFIEsLPDG--YDtrvgergLKLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 467 ERDIILLDEWAADQDPHFRREFYQVLLPLMQqmGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
139-530 |
4.41e-10 |
|
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: 62.66 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 139 AAYLAWLS---SKMLAVTALWIAITIWGGFVLVSRVY--KHMAvLRETEDKLYNDyqtVLEGRKELTLNRERAEYIFNHL 213
Cdd:TIGR00957 448 ALYFLWLNlgpSVLAGVAVMVLMVPLNAVMAMKTKTYqvAHMK-SKDNRIKLMNE---ILNGIKVLKLYAWELAFLDKVE 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 214 YIpdaREYRHHIIRADTFhLSAV---NWSNIMMLGAIgLVFWMANSLGwaDTNV----AATYSLTLL-FLRTPLlsavGA 285
Cdd:TIGR00957 524 GI---RQEELKVLKKSAY-LHAVgtfTWVCTPFLVAL-ITFAVYVTVD--ENNIldaeKAFVSLALFnILRFPL----NI 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 286 LPTLLS----AQVAFNKLNKF----DLAPFKAEfPRPQAFPDWQTLELRNVTFRY-QDSAFSVGPVNLTIRRGELLFLIG 356
Cdd:TIGR00957 593 LPMVISsivqASVSLKRLRIFlsheELEPDSIE-RRTIKPGEGNSITVHNATFTWaRDLPPTLNGITFSIPEGALVAVVG 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 357 GNGSGKSTLAMLLTGLYQPQSGEILLDGRAlsAEKPEdyrklfSAVFTDVWLFEQLLGpeGQQANPALVEKWLTQLQMSH 436
Cdd:TIGR00957 672 QVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AYVPQ------QAWIQNDSLRENILF--GKALNEKYYQQVLEACALLP 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 437 KLELQDG--------KILNlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE-FYQVLLPLMQQMGKTIFAIS 507
Cdd:TIGR00957 742 DLEILPSgdrteigeKGVN--LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHiFEHVIGPEGVLKNKTRILVT 819
|
410 420
....*....|....*....|...
gi 1347499258 508 HDDHYFIHADRLLEMRDGRLSEL 530
Cdd:TIGR00957 820 HGISYLPQVDVIIVMSGGKISEM 842
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
321-527 |
4.42e-10 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 59.10 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 321 QTLELRNVTFRYQDSAFSVGP-----VNLTIRRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGRALSaekPE 393
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKSGKqllknVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLD---KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 394 DYRKLFSAVFTDVWLFEQLLGPEgqqanpalvekwltQLQMSHKLElqdgkilnlKLSKGQKKRVALLLALAEERDIILL 473
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTLTVRE--------------TLMFAAKLR---------GLSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 474 DEWAADQDPhFRREFYQVLLPLMQQMGKTIFAISHDDHYFIHA--DRLLEMRDGRL 527
Cdd:cd03213 136 DEPTSGLDS-SSALQVMSLLRRLADTGRTIICSIHQPSSEIFElfDKLLLLSQGRV 190
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
343-475 |
5.02e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 343 NLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLF-----SAVFTDVWLFEQL--LGP 415
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqPGIKTELTALENLrfYQR 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 416 EGQQANPALVEKWLTQLQMSHKLELQDGkilnlKLSKGQKKRVALL-LALAeERDIILLDE 475
Cdd:PRK13538 101 LHGPGDDEALWEALAQVGLAGFEDVPVR-----QLSAGQQRRVALArLWLT-RAPLWILDE 155
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
342-536 |
8.34e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 8.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDgRALsAEKPEDYRKLFSAVFTDVWLFEqllgpEGQQAN 421
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSI-AYVPQQAWIMNATVRGNILFFD-----EEDAAR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 422 PALVEKwLTQL-----QMSHKLELQDG-KILNLklSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLpL 495
Cdd:PTZ00243 752 LADAVR-VSQLeadlaQLGGGLETEIGeKGVNL--SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF-L 827
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1347499258 496 MQQMGKTIFAISHDDHYFIHADRLLEMRDGRLsELTGEERD 536
Cdd:PTZ00243 828 GALAGKTRVLATHQVHVVPRADYVVALGDGRV-EFSGSSAD 867
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
339-405 |
1.70e-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: 60.08 E-value: 1.70e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 339 VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLyQPQSGEILLDGRALSAEKPEDYRKLFSA---VFTD 405
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRPLRRRmqvVFQD 370
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
339-482 |
1.86e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.37 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 339 VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALS-------AEKPEDYRKLFSAVFTDVWLFEQ 411
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplharARRGIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347499258 412 LLG--------PEGQQANPAlvEKWLTQLQMSHkleLQDGkiLNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:PRK10895 99 LMAvlqirddlSAEQREDRA--NELMEEFHIEH---LRDS--MGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
323-398 |
1.87e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.04 E-value: 1.87e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL 398
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
342-510 |
2.13e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLY--QPQSGEILLDGRALSAEKPedyrkLFSAVF--TDVWLFEQLLGPEG 417
Cdd:COG2401 49 LNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS-----LIDAIGrkGDFKDAVELLNAVG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 418 QQANPALVEKWltqlqmSHklelqdgkilnlkLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQ 497
Cdd:COG2401 124 LSDAVLWLRRF------KE-------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLAR 184
|
170
....*....|...
gi 1347499258 498 QMGKTIFAISHDD 510
Cdd:COG2401 185 RAGITLVVATHHY 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
305-481 |
3.41e-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: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 305 APFKAEFPRP-QAFPDWQTLELRNVTFRYQ-DSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL 382
Cdd:TIGR00957 1266 APWQIQETAPpSGWPPRGRVEFRNYCLRYReDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 383 DGRALSAEKPEDYRKLFSAVFTDVWLFEQL----LGPEGQQANPalvEKWlTQLQMSH----------KLELQ--DGkil 446
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSlrmnLDPFSQYSDE---EVW-WALELAHlktfvsalpdKLDHEcaEG--- 1418
|
170 180 190
....*....|....*....|....*....|....*
gi 1347499258 447 NLKLSKGQKKRVALLLALAEERDIILLDEWAADQD 481
Cdd:TIGR00957 1419 GENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-508 |
3.85e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 57.62 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQ--PQ---SGEILLDGRALSAEKPEDYRK 397
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDG-VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 LFSAVFT------DVWLFEQL-LGP----------EGQQANPALVEKWLTQLQMSHKLELQDGKilnlkLSKGQKKRVAL 460
Cdd:PRK14247 83 RVQMVFQipnpipNLSIFENVaLGLklnrlvkskkELQERVRWALEKAQLWDEVKDRLDAPAGK-----LSGGQQQRLCI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1347499258 461 LLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMgkTIFAISH 508
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTH 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
323-526 |
4.13e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYqPQ---SGEILLDGRALSAEKPEDY-RKL 398
Cdd:PRK13549 6 LEMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 FSAVFTDVWLFEQL-------LGPE----GQQANPALV---EKWLTQLQMSHKLELqdgKILNLKLskGQKKRVALLLAL 464
Cdd:PRK13549 84 IAIIHQELALVKELsvlenifLGNEitpgGIMDYDAMYlraQKLLAQLKLDINPAT---PVGNLGL--GQQQLVEIAKAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 465 AEERDIILLDEWAAdqdPHFRREFyQVLLPLMQQM---GKTIFAISHD-DHYFIHADRLLEMRDGR 526
Cdd:PRK13549 159 NKQARLLILDEPTA---SLTESET-AVLLDIIRDLkahGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
233-529 |
4.26e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 233 LSAVNwsnIMMLGAIGLV-----FWMANSLGWADTNVAATYSLTLL-FLRTPLLsavgALPTLLS----AQVAFNKLNKF 302
Cdd:PLN03130 522 LSAFN---SFILNSIPVLvtvvsFGVFTLLGGDLTPARAFTSLSLFaVLRFPLF----MLPNLITqavnANVSLKRLEEL 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 303 DLAPFKAEFPRPQAFPDWQTLELRNVTFRYQDSA--FSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-GE 379
Cdd:PLN03130 595 LLAEERVLLPNPPLEPGLPAISIKNGYFSWDSKAerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdAS 674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 380 ILLDGRAlsAEKPEdYRKLFSAVFTDVWLFeqllgpeGQQANPALVEKWLTQLQMSHKLELQDGKILN------LKLSKG 453
Cdd:PLN03130 675 VVIRGTV--AYVPQ-VSWIFNATVRDNILF-------GSPFDPERYERAIDVTALQHDLDLLPGGDLTeigergVNISGG 744
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 454 QKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:PLN03130 745 QKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELR-GKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
339-535 |
4.54e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.05 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 339 VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVftdvwlfeQL------ 412
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKI--------QIvfqnpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 413 --LGPE---GQQ-ANPALVEkwlTQLQMSHKLE--LQDGKILNLK----------LSKGQKKRVALLLALAEERDIILLD 474
Cdd:PRK11308 103 gsLNPRkkvGQIlEEPLLIN---TSLSAAERREkaLAMMAKVGLRpehydryphmFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 475 EWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGRLSELTGEER 535
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQ 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-475 |
4.65e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEdYRKLFSAVF---TDVWL-------FEq 411
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKE-FARRIGVVFgqrSQLWWdlpaidsFR- 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 412 LLG-----PEgqqanpALVEKWLTQLqmSHKLELQDgkILNL---KLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:COG4586 119 LLKaiyriPD------AEYKKRLDEL--VELLDLGE--LLDTpvrQLSLGQRMRCELAAALLHRPKILFLDE 180
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
329-529 |
8.04e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.19 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 329 TFRY-QDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVFTDVW 407
Cdd:PRK10789 320 QFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 408 LFEQLLGpegqqANPALVEKWLTQLQMSHKLELQD--GKILNLK-------------LSKGQKKRVALLLALAEERDIIL 472
Cdd:PRK10789 400 LFSDTVA-----NNIALGRPDATQQEIEHVARLASvhDDILRLPqgydtevgergvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 473 LDEWAADQDPhfrREFYQVLLPLMQ-QMGKTIFAISHDDHYFIHADRLLEMRDGRLSE 529
Cdd:PRK10789 475 LDDALSAVDG---RTEHQILHNLRQwGEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
322-537 |
1.06e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.89 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdgralsaekPEDYRKLF-- 399
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGARVLFlp 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 400 -SAVFTDVWLFEQLLGPEG-QQANPALVEKWLTQLQMSHKLE-LQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEW 476
Cdd:COG4178 433 qRPYLPLGTLREALLYPATaEAFSDAELREALEAVGLGHLAErLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 477 AADQDPHFRREFYQVLLPLMQQMgkTIFAISHDDHYFIHADRLLEMRDGRLSELTGEERDA 537
Cdd:COG4178 513 TSALDEENEAALYQLLREELPGT--TVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
322-394 |
1.09e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.16 E-value: 1.09e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 322 TLELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPED 394
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD 75
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
323-526 |
1.18e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYqDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYqPQ---SGEILLDGRALSAEKPEDY-RKL 398
Cdd:TIGR02633 2 LEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 FS------------AVFTDVWLFEQLLGPEGQQANPALV---EKWLTQLQMShklELQDGKILNlKLSKGQKKRVALLLA 463
Cdd:TIGR02633 80 IViihqeltlvpelSVAENIFLGNEITLPGGRMAYNAMYlraKNLLRELQLD---ADNVTRPVG-DYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 464 LAEERDIILLDEWAADqdphFRREFYQVLLPL---MQQMGKTIFAISHD-DHYFIHADRLLEMRDGR 526
Cdd:TIGR02633 156 LNKQARLLILDEPSSS----LTEKETEILLDIirdLKAHGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
342-475 |
1.34e-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: 55.19 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLfsavftdVWLfeqllgpeGQQAN 421
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL-------LYL--------GHAPG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 422 PALVEKWLTQLQMSHKLELQDGKILNL--------------KLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03231 84 IKTTLSVLENLRFWHADHSDEQVEEALarvglngfedrpvaQLSAGQQRRVALARLLLSGRPLWILDE 151
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
323-387 |
1.55e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 1.55e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 323 LELRNVTFRY------QDSAFSVgpvnltiRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAL 387
Cdd:PRK11288 5 LSFDGIGKTFpgvkalDDISFDC-------RAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM 68
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
342-475 |
3.00e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.11 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKP---------EDYRKLFSAVFTDVWLFEQL 412
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeachylghRNAMKPALTVAENLEFWAAF 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 413 LGPEGQQANPALvekwltqlqmsHKLELQDgkILNLK---LSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK13539 101 LGGEELDIAAAL-----------EAVGLAP--LAHLPfgyLSAGQKRRVALARLLVSNRPIWILDE 153
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
342-511 |
3.27e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRkLFSAVFTDVWLFEQLL-GPEGQQA 420
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY-LDTTLPLTVNRFLRLRpGTKKEDI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 421 NPAlvekwLTQLQMSHKLE--LQdgkilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQ 498
Cdd:PRK09544 102 LPA-----LKRVQAGHLIDapMQ-------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRE 169
|
170
....*....|...
gi 1347499258 499 MGKTIFAISHDDH 511
Cdd:PRK09544 170 LDCAVLMVSHDLH 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
323-522 |
4.69e-08 |
|
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: 52.54 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgralsaEKPEDYRKLF--- 399
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEGEDLLFlpq 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 400 SAVFTDVWLFEQLLGPegqqanpalvekWLTqlqmshklelqdgkilnlKLSKGQKKRVALLLALAEERDIILLDEWAAD 479
Cdd:cd03223 72 RPYLPLGTLREQLIYP------------WDD------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1347499258 480 QDPHFRREFYQVLlplmQQMGKTIFAISHDDHYFIHADRLLEM 522
Cdd:cd03223 122 LDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDL 160
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
342-540 |
5.23e-08 |
|
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: 56.07 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR-----ALSAEKPEDYRK--LFSAVFtDVWLFEQLLg 414
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRisfspQTSWIMPGTIKDniIFGLSY-DEYRYTSVI- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 415 pegqqaNPALVEKWLTQLQMSHKLELQDGKIlnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE-FYQVLL 493
Cdd:TIGR01271 523 ------KACQLEEDIALFPEKDKTVLGEGGI---TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEiFESCLC 593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 494 PLMqqMGKTIFAISHDDHYFIHADRLLEMRD------GRLSELTGEERDAASR 540
Cdd:TIGR01271 594 KLM--SNKTRILVTSKLEHLKKADKILLLHEgvcyfyGTFSELQAKRPDFSSL 644
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
324-547 |
7.76e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFR----YQDSAFSVgpvnltiRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLF 399
Cdd:PRK09700 267 EVRNVTSRdrkkVRDISFSV-------CRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 400 SAVFT----DVWLFEQLLGPEGQQANPAL-VEKW-----LTQLQMSHKLELQDGKILNLK----------LSKGQKKRVA 459
Cdd:PRK09700 340 MAYITesrrDNGFFPNFSIAQNMAISRSLkDGGYkgamgLFHEVDEQRTAENQRELLALKchsvnqniteLSGGNQQKVL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 460 LLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHDDHYFIHA-DRLLEMRDGRLSELTgEERDAA 538
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVcDRIAVFCEGRLTQIL-TNRDDM 497
|
....*....
gi 1347499258 539 SRDAVARTA 547
Cdd:PRK09700 498 SEEEIMAWA 506
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
342-526 |
8.79e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALS-AEK----PEDYRKLfSAVFTDVWLFeqllgpe 416
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKgiclPPEKRRI-GYVFQDARLF------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 417 gqqanPAL-VEKWLtQLQMSHKLELQDGKILNL------------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPH 483
Cdd:PRK11144 89 -----PHYkVRGNL-RYGMAKSMVAQFDKIVALlgieplldrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1347499258 484 FRREfyqvLLPLMQQMGKT----IFAISHDDHYFIH-ADRLLEMRDGR 526
Cdd:PRK11144 163 RKRE----LLPYLERLAREinipILYVSHSLDEILRlADRVVVLEQGK 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
322-526 |
9.60e-08 |
|
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: 54.34 E-value: 9.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRnVTFRYQDSAFSVgpvNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAL-SAEKPED---YRK 397
Cdd:COG4148 2 MLEVD-FRLRRGGFTLDV---DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFlppHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 398 LFSAVFTDVWLFEQL---------LGPEGQQANPALVEKWLTQLQMSHKLELQDGKilnlkLSKGQKKRVALLLALAEER 468
Cdd:COG4148 78 RIGYVFQEARLFPHLsvrgnllygRKRAPRAERRISFDEVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 469 DIILLDEWAADQDPHFRREfyqvLLPLMQQMGKT----IFAISHDdhyfIH-----ADRLLEMRDGR 526
Cdd:COG4148 153 RLLLMDEPLAALDLARKAE----ILPYLERLRDEldipILYVSHS----LDevarlADHVVLLEQGR 211
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
342-540 |
1.09e-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: 53.32 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAlsaekpeDYRKLFSAVFTDVWLFEQLLGPEGQQAN 421
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI-------SFSSQFSWIMPGTIKENIIFGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 422 PALVEKwLTQLQMS-HKLELQDGKIL---NLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRRE-FYQVLLPLM 496
Cdd:cd03291 129 YKSVVK-ACQLEEDiTKFPEKDNTVLgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEiFESCVCKLM 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1347499258 497 QQmgKTIFAISHDDHYFIHADRLLEMRDGR------LSELTGEERDAASR 540
Cdd:cd03291 208 AN--KTRILVTSKMEHLKKADKILILHEGSsyfygtFSELQSLRPDFSSK 255
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
349-509 |
1.16e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 349 GELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR---ALSAEKPEDYRKLFSAVFTDVW-----------------L 408
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYasldprqtvgdsimeplR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 409 FEQLLGPEGQQANPAlvekWLTQ---LQMSHKLELQDgkilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR 485
Cdd:PRK10261 430 VHGLLPGKAAAARVA----WLLErvgLLPEHAWRYPH------EFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180
....*....|....*....|....
gi 1347499258 486 REFYQVLLPLMQQMGKTIFAISHD 509
Cdd:PRK10261 500 GQIINLLLDLQRDFGIAYLFISHD 523
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
342-398 |
1.23e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.11 E-value: 1.23e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTG--LYQPQSGEILLDGRALSAEKPEDYRKL 398
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL 84
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
323-527 |
1.43e-07 |
|
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: 52.93 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLF----EQLLGPEGQQANPAL------------VEKWLTQLQmshkLELQDGKILnlkLSKGQKKRVALLLALA 465
Cdd:cd03289 82 IPQKVFIFsgtfRKNLDPYGKWSDEEIwkvaeevglksvIEQFPGQLD----FVLVDGGCV---LSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 466 EERDIILLDEWAADQDPhfrrEFYQVLLPLMQQ--MGKTIFAISHDDHYFIHADRLLEMRDGRL 527
Cdd:cd03289 155 SKAKILLLDEPSAHLDP----ITYQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
324-508 |
1.54e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 324 ELRNVTFRYQDSAF--SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAlsaekpedyrklfSA 401
Cdd:PRK13545 23 KLKDLFFRSKDGEYhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-------------AL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFEQLLGPEGQQANPALVEKWLTQLQ--MSHKLELQD-GKILNLKL---SKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK13545 90 IAISSGLNGQLTGIENIELKGLMMGLTKEKIKeiIPEIIEFADiGKFIYQPVktySSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190
....*....|....*....|....*....|...
gi 1347499258 476 WAADQDPHFRREFYQVLLPLMQQmGKTIFAISH 508
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISH 201
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
15-253 |
1.83e-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: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 15 FVAVMALSLASAALGIgLIAFINVRLIEMV--DTSLSVLPE----FLGLLLLLMAVTLGSQLALTALGHHFVFRLRSEFI 88
Cdd:cd07346 1 LLLALLLLLLATALGL-ALPLLTKLLIDDVipAGDLSLLLWiallLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 89 KRILDTQVERVEQLGSASLLAGLTSDVRAITIAFVR-LPELVQGIILTFGSAAYLAWLSSKMLAVTALWIAITIWGGFVL 167
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 168 VSRVYKHMAVLRETEDKLYNDYQTVLEGRKEL-TLNRERAEY-IFNHLyipdAREYRHHIIRADTfhLSAVNWSNIMMLG 245
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVkAFAAEEREIeRFREA----NRDLRDANLRAAR--LSALFSPLIGLLT 233
|
250
....*....|
gi 1347499258 246 AIG--LVFWM 253
Cdd:cd07346 234 ALGtaLVLLY 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
342-527 |
2.27e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.80 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPED---YRKLFSAVFTDvwlfEQLLGPEGQ 418
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQD----HHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 419 QANPAL------VEKWLTQLQMSHKLE----LQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREF 488
Cdd:PRK10908 97 YDNVAIpliiagASGDDIRRRVSAALDkvglLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1347499258 489 YQvLLPLMQQMGKTIFAISHDDHYFIHAD-RLLEMRDGRL 527
Cdd:PRK10908 177 LR-LFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
323-529 |
3.12e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.15 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRN--VTFRYQDSAFS-VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ----SGEILLDGRALSAEKPEDY 395
Cdd:COG4172 7 LSVEDlsVAFGQGGGTVEaVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 RKL----FSAVFtdvwlfeqllgpegQQA----NPAL-VEKwltqlQMSHKLELQDG--------KILNL---------- 448
Cdd:COG4172 87 RRIrgnrIAMIF--------------QEPmtslNPLHtIGK-----QIAEVLRLHRGlsgaaaraRALELlervgipdpe 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 449 --------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHD----DHYfihA 516
Cdd:COG4172 148 rrldayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvvRRF---A 224
|
250
....*....|...
gi 1347499258 517 DRLLEMRDGRLSE 529
Cdd:COG4172 225 DRVAVMRQGEIVE 237
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
342-475 |
3.51e-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: 51.12 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGRALsaeKPEDYRKLFSAVF-TDVWLFE------- 410
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPR---KPDQFQKCVAYVRqDDILLPGltvretl 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 411 ----QLLGPEgQQANPALVEKWLTQLqMSHkleLQDGKILNLK---LSKGQKKRVALLLALAEERDIILLDE 475
Cdd:cd03234 103 tytaILRLPR-KSSDAIRKKRVEDVL-LRD---LALTRIGGNLvkgISGGERRRVSIAVQLLWDPKVLILDE 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
312-507 |
3.90e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 312 PRPQAFPDWQTLELRNVTFRYQDsaF-SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAE 390
Cdd:NF033858 256 PRPADDDDEPAIEARGLTMRFGD--FtAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 391 KPEDYRKL------FS-----AVFTDVWLFEQLLGPEGQQANPALVEkwltqlqMSHKLELQD-GKILNLKLSKGQKKRV 458
Cdd:NF033858 334 DIATRRRVgymsqaFSlygelTVRQNLELHARLFHLPAAEIAARVAE-------MLERFDLADvADALPDSLPLGIRQRL 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1347499258 459 ALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFaIS 507
Cdd:NF033858 407 SLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIF-IS 454
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
323-475 |
5.07e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.19 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDS-AFSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLY--QPQ---SGEILLDGRALSAEK--PED 394
Cdd:COG1117 12 IEVRNLNVYYGDKqALK--DINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDGEDIYDPDvdVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 YRKLFSAVFtdvwlfeqllgpegQQANP-------------------------ALVEKWLTQLQmshkL--ELQDgkILN 447
Cdd:COG1117 90 LRRRVGMVF--------------QKPNPfpksiydnvayglrlhgikskseldEIVEESLRKAA----LwdEVKD--RLK 149
|
170 180 190
....*....|....*....|....*....|.
gi 1347499258 448 ---LKLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:COG1117 150 ksaLGLSGGQQQRLCIARALAVEPEVLLMDE 180
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
323-475 |
8.62e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLDGRALSAEKPED------ 394
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRG-LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 -----YRKLFSAVFTDVWLFEQLLGPEGQQANPAL--------VEKWLTQLQMSHKLELQDgkiLNLKLSKGQKKRVALL 461
Cdd:PRK09580 81 fmafqYPVEIPGVSNQFFLQTALNAVRSYRGQEPLdrfdfqdlMEEKIALLKMPEDLLTRS---VNVGFSGGEKKRNDIL 157
|
170
....*....|....
gi 1347499258 462 LALAEERDIILLDE 475
Cdd:PRK09580 158 QMAVLEPELCILDE 171
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
323-508 |
8.85e-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: 51.73 E-value: 8.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAfSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGL--YQPQSGEILLD----------------- 383
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 384 ------GRALSAEK------PEDYRKLFS-----------AVFTDVWLFEQLL------GPEGQQANPALVEkWLTQLQM 434
Cdd:TIGR03269 80 epcpvcGGTLEPEEvdfwnlSDKLRRRIRkriaimlqrtfALYGDDTVLDNVLealeeiGYEGKEAVGRAVD-LIEMVQL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1347499258 435 SHKLELqdgkiLNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISH 508
Cdd:TIGR03269 159 SHRITH-----IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
323-385 |
9.82e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 9.82e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 323 LELRNVTFRY------QDsafsvgpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYqPQ---SGEILLDGR 385
Cdd:NF040905 2 LEMRGITKTFpgvkalDD-------VNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGE 65
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
338-530 |
1.30e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.48 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 338 SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRklfsAVFTDV-WLFEQLLGpe 416
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWR----AVRSDIqMIFQDPLA-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 417 gqQANPAL------VEKWLTQLQMSHKLELQD---------GKILNL------KLSKGQKKRVALLLALAEERDIILLDE 475
Cdd:PRK15079 110 --SLNPRMtigeiiAEPLRTYHPKLSRQEVKDrvkammlkvGLLPNLinryphEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 476 WAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGRLSEL 530
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVEL 243
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
307-536 |
1.99e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 307 FKAEFPRPQAFPDWQTLELRNVTFRYQDSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL----- 381
Cdd:PLN03073 493 YKFEFPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakv 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 382 ---------LDGRALSAEKPEDYRKLFSAVftdvwlfeqllgPEGQqanpalVEKWLTQLQMSHKLELQDgkilNLKLSK 452
Cdd:PLN03073 573 rmavfsqhhVDGLDLSSNPLLYMMRCFPGV------------PEQK------LRAHLGSFGVTGNLALQP----MYTLSG 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 453 GQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLlpLMQQMGktIFAISHDDHYFIHA-DRLLEMRDGRLSELT 531
Cdd:PLN03073 631 GQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPFH 706
|
....*
gi 1347499258 532 GEERD 536
Cdd:PLN03073 707 GTFHD 711
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
348-526 |
2.03e-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: 47.75 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 348 RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdgraLSAEKpedyrklfsavftdvwlfeqllgpegqqanpalvek 427
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----IDGED------------------------------------ 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 428 wlTQLQMSHKLELQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRR-----EFYQVLLPLMQQMGKT 502
Cdd:smart00382 41 --ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAlllllEELRLLLLLKSEKNLT 118
|
170 180 190
....*....|....*....|....*....|
gi 1347499258 503 IFAISHDDHYFIHA------DRLLEMRDGR 526
Cdd:smart00382 119 VILTTNDEKDLGPAllrrrfDRRIVLLLIL 148
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
316-511 |
3.45e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.70 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 316 AFPDWQTLELRNVTFRYqdsafSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILLDGRALSAEKPED- 394
Cdd:PRK15134 284 AFPIRKGILKRTVDHNV-----VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQl 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 --YRKLFSAVFTD-----------VWLFEQLLGPEGQQANPALVEKWLTQLQMSHKLELQDGKILNLKLSKGQKKRVALL 461
Cdd:PRK15134 358 lpVRHRIQVVFQDpnsslnprlnvLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIA 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1347499258 462 LALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDH 511
Cdd:PRK15134 438 RALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
342-385 |
3.55e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 3.55e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR 385
Cdd:PRK10982 17 VNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK 60
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
340-482 |
3.97e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 340 GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR-ALSAEKPE--DYRKLFSAVFTDVWLFEQL---L 413
Cdd:PRK13543 28 GPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtATRGDRSRfmAYLGHLPGLKADLSTLENLhflC 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 414 GPEGQQA----NPALVEKWLTQLQMShklelqdgkiLNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDP 482
Cdd:PRK13543 108 GLHGRRAkqmpGSALAIVGLAGYEDT----------LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
226-544 |
4.72e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 226 IRADTFHLSAVNWSNIMMLGAIGLVFWMANS---LGWADTNVAATYSLTLLFLrtplLSAVGALPTLLS-----AQVAFN 297
Cdd:PLN03232 1123 IRFTLANTSSNRWLTIRLETLGGVMIWLTATfavLRNGNAENQAGFASTMGLL----LSYTLNITTLLSgvlrqASKAEN 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 298 KLNK-------FDL---APFKAEFPRP-QAFPDWQTLELRNVTFRYQDS--------AFSVGPvnltirrGELLFLIGGN 358
Cdd:PLN03232 1199 SLNSvervgnyIDLpseATAIIENNRPvSGWPSRGSIKFEDVHLRYRPGlppvlhglSFFVSP-------SEKVGVVGRT 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 359 GSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVFTDVWLFEQL----LGPEGQQANPALVEKwltqLQM 434
Cdd:PLN03232 1272 GAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTvrfnIDPFSEHNDADLWEA----LER 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 435 SHKLELQDGKILNL---------KLSKGQKKRVALLLALAEERDIILLDEWAADQDPH--------FRREFYQVllplmq 497
Cdd:PLN03232 1348 AHIKDVIDRNPFGLdaevseggeNFSVGQRQLLSLARALLRRSKILVLDEATASVDVRtdsliqrtIREEFKSC------ 1421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1347499258 498 qmgkTIFAISHDDHYFIHADRLLEMRDGRLSELTGEErDAASRDAVA 544
Cdd:PLN03232 1422 ----TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQ-ELLSRDTSA 1463
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
322-540 |
5.30e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDS-AFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFS 400
Cdd:PTZ00243 1308 SLVFEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 401 AVFTDVWLFE----QLLGPeGQQANPALVEKWLTQLQMSHKL----ELQDGKILN--LKLSKGQKKRVALLLALAEE-RD 469
Cdd:PTZ00243 1388 MIPQDPVLFDgtvrQNVDP-FLEASSAEVWAALELVGLRERVasesEGIDSRVLEggSNYSVGQRQLMCMARALLKKgSG 1466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 470 IILLDEWAADQDPHFRRefyQVLLPLMQQMGK-TIFAISHDDHYFIHADRLLEMRDGRLSELtGEERDAASR 540
Cdd:PTZ00243 1467 FILMDEATANIDPALDR---QIQATVMSAFSAyTVITIAHRLHTVAQYDKIIVMDHGAVAEM-GSPRELVMN 1534
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
323-508 |
5.53e-06 |
|
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: 49.63 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQ-DSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKL--- 398
Cdd:TIGR01257 1938 LRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgyc 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 399 --FSAV------FTDVWLFEQLLGPEGQQANPalVEKWLTQlqmSHKLELQDGKILNlKLSKGQKKRVALLLALAEERDI 470
Cdd:TIGR01257 2018 pqFDAIddlltgREHLYLYARLRGVPAEEIEK--VANWSIQ---SLGLSLYADRLAG-TYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190
....*....|....*....|....*....|....*...
gi 1347499258 471 ILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISH 508
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSH 2128
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
377-508 |
5.62e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 377 SGEILLDGRALSAEKPEDYRKLFSAVFTDVWLFEQLL------GPEG-------QQANPALVEKWLTQLQMSHKLELQD- 442
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIyenikfGKEDatredvkRACKFAAIDEFIESLPNKYDTNVGPy 1355
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1347499258 443 GKilnlKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISH 508
Cdd:PTZ00265 1356 GK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
322-498 |
8.37e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 322 TLELRNVTFRYQDSAFSVGPvNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VF----TDvwlfeqLLGPE----GQQA---------NPALVEKWLTQLQMSHKLELQdgkilNLKLSKGQKKRVALLLAL 464
Cdd:PRK10938 82 EWqrnnTD------MLSPGeddtGRTTaeiiqdevkDPARCEQLAQQFGITALLDRR-----FKYLSTGETRKTLLCQAL 150
|
170 180 190
....*....|....*....|....*....|....
gi 1347499258 465 AEERDIILLDEWAADQDPHFRREFYQVLLPLMQQ 498
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
317-482 |
9.78e-06 |
|
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: 48.75 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 317 FPDWQTLELRNVTFRYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILLDGRALSAEKPEDY 395
Cdd:TIGR01271 1212 WPSGGQMDVQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 RKLFSAVFTDVWL----FEQLLGPEGQQANPAL--------VEKWLTQLQMSHKLELQDGKILnlkLSKGQKKRVALLLA 463
Cdd:TIGR01271 1291 RKAFGVIPQKVFIfsgtFRKNLDPYEQWSDEEIwkvaeevgLKSVIEQFPDKLDFVLVDGGYV---LSNGHKQLMCLARS 1367
|
170
....*....|....*....
gi 1347499258 464 LAEERDIILLDEWAADQDP 482
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDP 1386
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
226-529 |
1.42e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 226 IRADTFHLSAVNWSNIMMLGAIGLVFWMANSL-----GWADTNVAATYSLTLLFLR----TPLLSAVGALPTLlsAQVAF 296
Cdd:PLN03130 1126 IRFTLVNMSSNRWLAIRLETLGGLMIWLTASFavmqnGRAENQAAFASTMGLLLSYalniTSLLTAVLRLASL--AENSL 1203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 297 NKL----NKFDL---APFKAEFPRPQ-AFPDWQTLELRNVTFRYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAM 367
Cdd:PLN03130 1204 NAVervgTYIDLpseAPLVIENNRPPpGWPSSGSIKFEDVVLRYRPELPPVlHGLSFEISPSEKVGIVGRTGAGKSSMLN 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 368 LLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSAVFTDVWLFEQL----LGPEGQQANPALVEkwltQLQMSHKLELQDG 443
Cdd:PLN03130 1284 ALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTvrfnLDPFNEHNDADLWE----SLERAHLKDVIRR 1359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 444 KILNL---------KLSKGQKKRVALLLALAEERDIILLDEWAADQD--------PHFRREFYQVllplmqqmgkTIFAI 506
Cdd:PLN03130 1360 NSLGLdaevseageNFSVGQRQLLSLARALLRRSKILVLDEATAAVDvrtdaliqKTIREEFKSC----------TMLII 1429
|
330 340
....*....|....*....|...
gi 1347499258 507 SHDDHYFIHADRLLEMRDGRLSE 529
Cdd:PLN03130 1430 AHRLNTIIDCDRILVLDAGRVVE 1452
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
323-543 |
1.43e-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: 46.83 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPEDYRKLFSA 401
Cdd:cd03288 20 IKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 402 VFTDVWLFEQL----LGPEGQQANPALVEKwLTQLQMSHKLELQDGKILNL------KLSKGQKKRVALLLALAEERDII 471
Cdd:cd03288 100 ILQDPILFSGSirfnLDPECKCTDDRLWEA-LEIAQLKNMVKSLPGGLDAVvteggeNFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 472 LLDEWAADQDPHFRREFYQVLLPLMQQmgKTIFAISHDDHYFIHADRLLEMRDGRLSELTGEERDAASRDAV 543
Cdd:cd03288 179 IMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGV 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
310-536 |
2.16e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 310 EFPRPQAFPDWQTLELRNVtfryqdSAFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSA 389
Cdd:PRK10762 245 QYPRLDKAPGEVRLKVDNL------SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 390 EKPED-------Y----RK-----LFSAV-----FTDVWLFEQLLGPEGQQANPALVEKWLTQLQMshKLELQDGKILNl 448
Cdd:PRK10762 319 RSPQDglangivYisedRKrdglvLGMSVkenmsLTALRYFSRAGGSLKHADEQQAVSDFIRLFNI--KTPSMEQAIGL- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 449 kLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQvLLPLMQQMGKTIFAISHDDHYFI-HADRLLEMRDGRL 527
Cdd:PRK10762 396 -LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEGLSIILVSSEMPEVLgMSDRILVMHEGRI 473
|
250
....*....|
gi 1347499258 528 S-ELTGEERD 536
Cdd:PRK10762 474 SgEFTREQAT 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
324-380 |
2.31e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 324 ELRNVTFRYQD----SAFSVgpvnlTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
Cdd:PRK11147 321 EMENVNYQIDGkqlvKDFSA-----QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
323-539 |
2.51e-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: 46.74 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAF--SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ-SGEILLDGRALS----------- 388
Cdd:TIGR02633 258 LEARNLTCWDVINPHrkRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDirnpaqairag 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 389 -AEKPEDyRKLFSAVftdvwlfeQLLGPeGQQANPALVEKWLTQLQMSHKLELQ--DGKILNLK------------LSKG 453
Cdd:TIGR02633 338 iAMVPED-RKRHGIV--------PILGV-GKNITLSVLKSFCFKMRIDAAAELQiiGSAIQRLKvktaspflpigrLSGG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 454 QKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQmGKTIFAISHDDHYFIH-ADRLLEMRDGRL----- 527
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGlSDRVLVIGEGKLkgdfv 486
|
250
....*....|...
gi 1347499258 528 -SELTGEERDAAS 539
Cdd:TIGR02633 487 nHALTQEQVLAAA 499
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
346-519 |
2.58e-05 |
|
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: 44.87 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 346 IRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAeKPEdyrklfsavftdvwlfeqllgpegqqanpalv 425
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVY-KPQ-------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 426 ekwltqlqmshklelqdgkilNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFA 505
Cdd:cd03222 69 ---------------------YIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALV 127
|
170
....*....|....
gi 1347499258 506 ISHDdhyFIHADRL 519
Cdd:cd03222 128 VEHD---LAVLDYL 138
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
290-493 |
2.82e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 290 LSAQVAFN-KLNKFDLaPFKAEFPRPQAFPDWQTL-ELRNVTFRYQDSafsvgPV----NLTIRRGELLFLIGGNGSGKS 363
Cdd:PRK10938 227 LVAQLAHSeQLEGVQL-PEPDEPSARHALPANEPRiVLNNGVVSYNDR-----PIlhnlSWQVNPGEHWQIVGPNGAGKS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 364 TLAMLLTGLYqPQ--------------SGEILLDGRA----LSAEKPEDYR-------KLFSAVFTDVWLFEQLlgPEGQ 418
Cdd:PRK10938 301 TLLSLITGDH-PQgysndltlfgrrrgSGETIWDIKKhigyVSSSLHLDYRvstsvrnVILSGFFDSIGIYQAV--SDRQ 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 419 QanpALVEKWLTQLQMSHKLelqdGKILNLKLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFR---REFYQVLL 493
Cdd:PRK10938 378 Q---KLAQQWLDILGIDKRT----ADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLI 448
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
312-529 |
3.56e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.39 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 312 PRPQAFPDWQTLELRNVTFRYQDSAFSVGPV---NLTIRRGELLFLIGGNGSGKSTLAMLLTGLY-----QPQSGEILLD 383
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVrnlSFSLQRGETLAIVGESGSGKSVTALALMRLLeqaggLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 384 GR-----ALSAEKPEDYRKLFSA---------------VFT-DVWLFEQLLGPEGQQANPALVE--KWLTQLQMShklel 440
Cdd:PRK10261 82 RRsrqviELSEQSAAQMRHVRGAdmamifqepmtslnpVFTvGEQIAESIRLHQGASREEAMVEakRMLDQVRIP----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 441 QDGKILNL---KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-A 516
Cdd:PRK10261 157 EAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiA 236
|
250
....*....|...
gi 1347499258 517 DRLLEMRDGRLSE 529
Cdd:PRK10261 237 DRVLVMYQGEAVE 249
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
306-382 |
4.04e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 4.04e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1347499258 306 PFKAEFPRPQAFPDwQTLELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL 382
Cdd:PRK10636 297 PFHFSFRAPESLPN-PLLKMEKVSAGYGDRII-LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
342-527 |
4.57e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 44.87 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 342 VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALS------------AEKPEDyRKLFSAVftdvwLF 409
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqtakimreavAIVPEG-RRVFSRM-----TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 410 EQLLGPEGQQANPalvEKWLTQLQMSHKL--ELQDGKILNL-KLSKGQKKRVALLLALAEERDIILLDEWAADQDPHFRR 486
Cdd:PRK11614 98 EENLAMGGFFAER---DQFQERIKWVYELfpRLHERRIQRAgTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1347499258 487 EFYQVLLPLMQQmGKTIFAISHDDHYFIH-ADRLLEMRDGRL 527
Cdd:PRK11614 175 QIFDTIEQLREQ-GMTIFLVEQNANQALKlADRGYVLENGHV 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
344-394 |
5.56e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 5.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 344 LTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRALSAEKPED 394
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS 75
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
323-385 |
7.17e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.53 E-value: 7.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347499258 323 LELRNVTFRYqdsafsvGP------VNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGR 385
Cdd:PRK11701 7 LSVRGLTKLY-------GPrkgcrdVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR 68
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
326-509 |
8.88e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 326 RNVTFryqdsaFSVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGRAlsaekpedyrklfSAVFTD 405
Cdd:PRK13546 33 KNKTF------FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV-------------SVIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 406 VWLFEQLLGPEGQQANPALV---EKWLTQLqMSHKLELQD-GKILNL---KLSKGQKKRVALLLALAEERDIILLDEWAA 478
Cdd:PRK13546 94 AGLSGQLTGIENIEFKMLCMgfkRKEIKAM-TPKIIEFSElGEFIYQpvkKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190
....*....|....*....|....*....|.
gi 1347499258 479 DQDPHFRREFYQVLLPLMQQmGKTIFAISHD 509
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHN 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
321-380 |
1.18e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.88 E-value: 1.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 321 QTLELRNVTFRYQDSA-FSvgPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
Cdd:PRK15064 318 NALEVENLTKGFDNGPlFK--NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
311-394 |
1.61e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 311 FPRPQAFPDWQTLELRNVTFRYQDSAF--SVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQS-GEILLDGRAL 387
Cdd:PRK13549 248 YPREPHTIGEVILEVRNLTAWDPVNPHikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPV 327
|
....*..
gi 1347499258 388 SAEKPED 394
Cdd:PRK13549 328 KIRNPQQ 334
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
315-383 |
2.14e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 2.14e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1347499258 315 QAFPDWQTLELRNVTFRYqDSAFSV---GPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD 383
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHY-DTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN 445
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
354-526 |
2.85e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 43.77 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 354 LIGGNGSGKSTLAMLLTGLYQPQSGEIL-------------------LDGRALSAEKPEDYRKLF------SAVFTDVWL 408
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARpqpgikvgylpqepqldptKTVRENVEEGVAEIKDALdrfneiSAKYAEPDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 409 -FEQLLGPEGQ-QANPALVEKWL--TQLQMS-HKLELQDGKILNLKLSKGQKKRVALLLALAEERDIILLDEwaadqdP- 482
Cdd:TIGR03719 116 dFDKLAAEQAElQEIIDAADAWDldSQLEIAmDALRCPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDE------Pt 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1347499258 483 -HFRREFYQVLLPLMQQMGKTIFAISHdDHYFIH--ADRLLEMRDGR 526
Cdd:TIGR03719 190 nHLDAESVAWLERHLQEYPGTVVAVTH-DRYFLDnvAGWILELDRGR 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
323-380 |
2.95e-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: 43.39 E-value: 2.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1347499258 323 LELRNVTFRYQDSAFsVGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
Cdd:TIGR03719 323 IEAENLTKAFGDKLL-IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-508 |
8.52e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.37 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRNVTFRYQDSAFSVGpVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ-----SGEILLDGRALSAEK--PEDY 395
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKG-VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDvdPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 396 RKLFSAVFTDVWLFEQLLGPEgqqaNPALVEKwLTQLQMSHKlELQDGKILNLK------------------LSKGQKKR 457
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYD----NVAIGVK-LNGLVKSKK-ELDERVEWALKkaalwdevkdrlndypsnLSGGQRQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1347499258 458 VALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMgkTIFAISH 508
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTH 206
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
355-380 |
1.14e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 1.14e-03
10 20
....*....|....*....|....*.
gi 1347499258 355 IGGNGSGKSTLAMLLTGLYQPQSGEI 380
Cdd:PRK11819 356 IGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
327-385 |
1.57e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.86 E-value: 1.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1347499258 327 NVTFRYQDSAFS-VGPVNLTIRRGELLFLIGGNGSGKSTLAMLLTGLYQPQ---SGEILLDGR 385
Cdd:PRK09473 19 RVTFSTPDGDVTaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGR 81
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
323-529 |
3.92e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.07 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 323 LELRN--VTFRYQDSAFSV-GPVNLTIRRGELLFLIGGNGSGKSTLAM-LLTGLYQPQ----SGEILLDGRALSAEKPED 394
Cdd:PRK15134 6 LAIENlsVAFRQQQTVRTVvNDVSLQIEAGETLALVGESGSGKSVTALsILRLLPSPPvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 395 YRKL----FSAVFTDVW------------LFEQLLGPEGQQANPALVEkwltqlqMSHKLEL----QDGKILN---LKLS 451
Cdd:PRK15134 86 LRGVrgnkIAMIFQEPMvslnplhtlekqLYEVLSLHRGMRREAARGE-------ILNCLDRvgirQAAKRLTdypHQLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1347499258 452 KGQKKRVALLLALAEERDIILLDEWAADQDPHFRREFYQVLLPLMQQMGKTIFAISHDDHYFIH-ADRLLEMRDGRLSE 529
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVE 237
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
72-252 |
7.95e-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: 38.31 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 72 LTALGHHFVFRLRSEFIKRILDTQVERVEQLGSASLLAGLTSDVRAI-TIAFVRLPELVQGIILTFGSAAYLAWLSSKML 150
Cdd:cd18557 60 FNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLqSAVTDNLSQLLRNILQVIGGLIILFILSWKLT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1347499258 151 AVTALWIAITIWGGFVLVSRVykhMAVLRETEDKLYNDYQTVLEG----RKELTLNRERAE-YIFNHLyIPDAREYRHHI 225
Cdd:cd18557 140 LVLLLVIPLLLIASKIYGRYI---RKLSKEVQDALAKAGQVAEESlsniRTVRSFSAEEKEiRRYSEA-LDRSYRLARKK 215
|
170 180
....*....|....*....|....*..
gi 1347499258 226 IRADTFHLSavnWSNIMMLGAIGLVFW 252
Cdd:cd18557 216 ALANALFQG---ITSLLIYLSLLLVLW 239
|
|
| |
