|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-592 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 605.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 15 KEQLTVIRRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGhaTVPVMWYFAGLYFFGMVVRALMQFV 94
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG--DLSALLLLLLLLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 95 QNFSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWA-LFNTLFTAFFAVISSFVAMYLTD 173
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAhGLPQLVRSVVTLIGALVVLFVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 174 AQIALWLLVFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAM 253
Cdd:COG1132 161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 254 IRTNSLLlSPLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRVLRVMD 333
Cdd:COG1132 241 ARLSALF-FPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 334 DPTIAPAQHVDPTAKITRGKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLI 413
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 414 DDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSS 493
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 494 GQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSND 573
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|....*....
gi 1027832812 574 ELLQQHGYYYDMIQLQNSA 592
Cdd:COG1132 560 ELLARGGLYARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-590 |
6.53e-145 |
|
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: 435.80 E-value: 6.53e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 13 PVKEQLTVIRRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYLktGHATVPVMWYFAGLYFFGMVVRALMQ 92
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVL--PNQDLSTLWVLAIGLLLALLFEGLLR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 93 FVQNfsstmgaeYMLENVRRQMFAKLH--------RMGMRYFDQVPGGSILSRLtNDTMSFSNFWA--LFNTLFTAFFAV 162
Cdd:COG2274 214 LLRS--------YLLLRLGQRIDLRLSsrffrhllRLPLSFFESRSVGDLASRF-RDVESIREFLTgsLLTALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 163 ISsFVAMYLTDAQIALWLLVFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHT 242
Cdd:COG2274 285 IF-LIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 243 NDAYFKTRQAMIRTNSLLLSpLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGV 322
Cdd:COG2274 364 LAKYLNARFKLRRLSNLLST-LSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAK 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 323 VAGSRVLRVMDDPTIAPAQHVDPTAKITRGKIEFRHVTFAYDGQ-HPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLM 401
Cdd:COG2274 443 IALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 402 RFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQ 481
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 482 SRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVL 561
Cdd:COG2274 603 TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVL 682
|
570 580
....*....|....*....|....*....
gi 1027832812 562 NQGKIVERGSNDELLQQHGYYYDMIQLQN 590
Cdd:COG2274 683 DKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-589 |
1.80e-128 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 389.46 E-value: 1.80e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 21 IRRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSST 100
Cdd:PRK10790 11 LKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAAYVGLQLLAAGLHYAQSLLFN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 101 MGAEYMLENVRRQ-MFAKLhRMGMRYFDQVPGGSILSRLTNDTMSFSNFWA-LFNTLFTAFFAVISSFVAMYLTDAQIAL 178
Cdd:PRK10790 91 RAAVGVVQQLRTDvMDAAL-RQPLSAFDTQPVGQLISRVTNDTEVIRDLYVtVVATVLRSAALIGAMLVAMFSLDWRMAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 179 WLLVFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNS 258
Cdd:PRK10790 170 VAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 259 LLLSPLIDLFYAL---GTVMVLGIFGVrglnGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRVLRVMDdp 335
Cdd:PRK10790 250 FLLRPLLSLFSALilcGLLMLFGFSAS----GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMD-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 336 tiAPAQHV-DPTAKITRGKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLID 414
Cdd:PRK10790 324 --GPRQQYgNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 415 DRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDqISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSG 494
Cdd:PRK10790 402 GRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 495 QRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDE 574
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQ 560
|
570
....*....|....*
gi 1027832812 575 LLQQHGYYYDMIQLQ 589
Cdd:PRK10790 561 LLAAQGRYWQMYQLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
22-590 |
1.48e-126 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 383.68 E-value: 1.48e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 22 RRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYLktGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTM 101
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGF--GGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 102 GAEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDT-MSFSNFWALFNTLFTAFFAVISSFVAMYLTDAQIALWL 180
Cdd:TIGR02203 81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSeQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 181 LVFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAyfKTRQAM-IRTNSL 259
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNR--NRRLAMkMTSAGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 260 LLSPLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRVLRVMDDPtiap 339
Cdd:TIGR02203 239 ISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSP---- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 340 aQHVDPTAKI---TRGKIEFRHVTFAYDGQH-PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDD 415
Cdd:TIGR02203 315 -PEKDTGTRAierARGDVEFRNVTFRYPGRDrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 416 RDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFN-DQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSG 494
Cdd:TIGR02203 394 HDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 495 QRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDE 574
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNE 553
|
570
....*....|....*.
gi 1027832812 575 LLQQHGYYYDMIQLQN 590
Cdd:TIGR02203 554 LLARNGLYAQLHNMQF 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
352-580 |
4.25e-114 |
|
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: 339.20 E-value: 4.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 352 GKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMG 431
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKI 511
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 512 LILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHG 580
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-580 |
2.65e-112 |
|
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: 346.75 E-value: 2.65e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 17 QLTVIRRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYLkTGHATVPVMWYFAGLYFFGMVVRALMQFVQN 96
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLI-IGGAPLSALLPLLGLLLAVLLLRALLAWLRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 97 FSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALF-NTLFTAFFAVISSFVAMYLTDAQ 175
Cdd:COG4988 80 RAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYlPQLFLAALVPLLILVAVFPLDWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 176 IALWLLVFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYfktRQamiR 255
Cdd:COG4988 160 SGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDF---RK---R 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 256 TNSLL----LSPLI-DLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMtsmmDNLSDF----QDGVVAGS 326
Cdd:COG4988 234 TMKVLrvafLSSAVlEFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPL----RDLGSFyharANGIAAAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 327 RVLRVMDDPTIAPAQHVDPTAKITRGKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEF 406
Cdd:COG4988 310 KIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 407 QSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIE 486
Cdd:COG4988 390 YSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 487 RGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKI 566
Cdd:COG4988 470 GGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRI 549
|
570
....*....|....
gi 1027832812 567 VERGSNDELLQQHG 580
Cdd:COG4988 550 VEQGTHEELLAKNG 563
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
354-585 |
6.14e-102 |
|
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: 308.39 E-value: 6.14e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQH-PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGL 432
Cdd:cd03251 1 VEFKNVTFRYPGDGpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKIL 512
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 513 ILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYYYDM 585
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
354-589 |
8.05e-101 |
|
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: 305.62 E-value: 8.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDG--QHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMG 431
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKI 511
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 512 LILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYYYDMIQLQ 589
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-589 |
1.88e-100 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 316.58 E-value: 1.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 22 RRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYLktGHATVPVMWYFAGLYFFGMVVRALMQFVQNF--SS 99
Cdd:PRK11176 14 RRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGF--GKADRSVLKWMPLVVIGLMILRGITSFISSYciSW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 100 TMGAEYMleNVRRQMFAklHRMGM--RYFDQVPGGSILSRLTNDT--MSFSNFWALFnTLFTAFFAVISSFVAMYLTDAQ 175
Cdd:PRK11176 92 VSGKVVM--TMRRRLFG--HMMGMpvSFFDKQSTGTLLSRITYDSeqVASSSSGALI-TVVREGASIIGLFIMMFYYSWQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 176 IALWLLVFMPFLAVTIwyyqRYSSRVYRR----MRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDayFKTRQ 251
Cdd:PRK11176 167 LSLILIVIAPIVSIAI----RVVSKRFRNisknMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSN--RMRQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 252 AM-IRTNSLLLSPLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRVLR 330
Cdd:PRK11176 241 GMkMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 331 VMDDPTiapaQHVDPTAKITR--GKIEFRHVTFAYDG-QHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ 407
Cdd:PRK11176 321 ILDLEQ----EKDEGKRVIERakGDIEFRNVTFTYPGkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 408 SGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIR-MFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIE 486
Cdd:PRK11176 397 EGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 487 RGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKI 566
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
570 580
....*....|....*....|...
gi 1027832812 567 VERGSNDELLQQHGYYYDMIQLQ 589
Cdd:PRK11176 557 VERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-595 |
3.93e-99 |
|
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: 314.07 E-value: 3.93e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 1 MAARQSVWARSMPVKEQLTVIRRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYFAGL 80
Cdd:COG5265 1 APSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 81 YFFGMVVRALMQFVQNFSSTMGAEYMLENVRR---QMFAKLHRMGMRY-FDQVPGG--SILSRLTNDTMSFSNFwALFNT 154
Cdd:COG5265 81 LLAYGLLRLLSVLFGELRDALFARVTQRAVRRlalEVFRHLHALSLRFhLERQTGGlsRDIERGTKGIEFLLRF-LLFNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 155 LFTA--FFAVISSFVAMYltDAQIALWLLV-FMPFLAVTIWYyQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQ 231
Cdd:COG5265 160 LPTLleIALVAGILLVKY--DWWFALITLVtVVLYIAFTVVV-TEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 232 EHRINGEFDHTNDAYfktRQAMIRT-NSLLL-----SPLIDLfyALGTVMVLGIFGVrgLNGYVAAGVVYAFITYLNNFY 305
Cdd:COG5265 237 EAREARRYDEALARY---ERAAVKSqTSLALlnfgqALIIAL--GLTAMMLMAAQGV--VAGTMTVGDFVLVNAYLIQLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 306 NPMTS-------MMDNLSDFQdgvvagsRVLRVMD-DPTIAPAqhvdPTAK---ITRGKIEFRHVTFAYDGQHPVLKDVS 374
Cdd:COG5265 310 IPLNFlgfvyreIRQALADME-------RMFDLLDqPPEVADA----PDAPplvVGGGEVRFENVSFGYDPERPILKGVS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 375 FVAEPGQTVALVGQTGSGKtSTI-NVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFND 453
Cdd:COG5265 379 FEVPAGKTVAIVGPSGAGK-STLaRLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 454 QISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGL 533
Cdd:COG5265 458 DASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL 537
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 534 DRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYYYDMIQLQNSAHVD 595
Cdd:COG5265 538 REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEA 599
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
35-328 |
5.77e-99 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 302.77 E-value: 5.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQM 114
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWA-LFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIWY 193
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTsGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 194 YQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYALGT 273
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFA-LFRPLVELLSSLAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 274 VMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18544 240 ALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
106-588 |
5.25e-97 |
|
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: 307.08 E-value: 5.25e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 106 MLENVRRQMFAKL------HRMGMRyfdqvpGGSILSRLTNDTMSFSNFWA-LFNTLFTAFFAVISSFVAMYLTDAQIAL 178
Cdd:COG4987 86 LLADLRVRLYRRLeplapaGLARLR------SGDLLNRLVADVDALDNLYLrVLLPLLVALLVILAAVAFLAFFSPALAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 179 WLLVFMPFLAVTI-WYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFK--TRQAMIR 255
Cdd:COG4987 160 VLALGLLLAGLLLpLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAaqRRLARLS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 256 TNSLLLSPLIDLFyALGTVMVLGIFGVR--GLNGYVAAGVVYAFITyLNNFYNPMTSMMDNLSDFQDgvvAGSRVLRVMD 333
Cdd:COG4987 240 ALAQALLQLAAGL-AVVAVLWLAAPLVAagALSGPLLALLVLAALA-LFEALAPLPAAAQHLGRVRA---AARRLNELLD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 334 DPTiAPAQHVDPTAKITRGKIEFRHVTFAYDGQ-HPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVL 412
Cdd:COG4987 315 APP-AVTEPAEPAPAPGGPSLELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 413 IDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYS 492
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLS 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 493 SGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSN 572
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTH 553
|
490
....*....|....*.
gi 1027832812 573 DELLQQHGYYYDMIQL 588
Cdd:COG4987 554 EELLAQNGRYRQLYQR 569
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
354-589 |
1.40e-95 |
|
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: 292.21 E-value: 1.40e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLV 433
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILI 513
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027832812 514 LDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYYYDMIQLQ 589
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-586 |
8.11e-90 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 292.40 E-value: 8.11e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 5 QSVWARSMPVKEQLT-----------VIRRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYL--KTGHATV 71
Cdd:TIGR00958 122 AALWAVLSSAGASEKeaeqgqsetadLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGgdKGPPALA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 72 PVMWyFAGLYFFGmvvRALMQFVQNFSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWAL 151
Cdd:TIGR00958 202 SAIF-FMCLLSIA---SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 152 -FNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFR 230
Cdd:TIGR00958 278 nVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 231 QEhriNGEFDHTNDAYFKTRQ-----AMIRTNSLLLSPLIDLFYalgTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFY 305
Cdd:TIGR00958 358 AE---EGEASRFKEALEETLQlnkrkALAYAGYLWTTSVLGMLI---QVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLG 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 306 NPMTSMMDNLSDFQDGVVAGSRVLRVMD-DPTIAPAQHVDPtaKITRGKIEFRHVTFAYDGQ--HPVLKDVSFVAEPGQT 382
Cdd:TIGR00958 432 EAVRVLSYVYSGMMQAVGASEKVFEYLDrKPNIPLTGTLAP--LNLEGLIEFQDVSFSYPNRpdVPVLKGLTFTLHPGEV 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 383 VALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQA 462
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMA 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 463 AARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTglDRIQENRTT 542
Cdd:TIGR00958 590 AAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTV 667
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1027832812 543 IAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYYYDMI 586
Cdd:TIGR00958 668 LLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
115-589 |
2.63e-85 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 277.23 E-value: 2.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFW-ALFNTLFTAFFAVISSF-VAMYLtDAQIALWLLVfmpfLAVTIW 192
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWlEFMREHLATLVALVVLLpLALFM-NWRLSLVLVV----LGIVYT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 193 YYQRYSSRVYRRMRERLSELNTKL----SEAITGISVIQQF-RQEHRINGEFDHTNDayfktrqamirtnslLLS---PL 264
Cdd:PRK13657 171 LITTLVMRKTKDGQAAVEEHYHDLfahvSDAIGNVSVVQSYnRIEAETQALRDIADN---------------LLAaqmPV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 265 IDlFYALGTVM-------------VLGIFGVrgLNGYVAAGVVYAFItylnNFYNPMTSMMDNLSDFQDGVVAGSRVLR- 330
Cdd:PRK13657 236 LS-WWALASVLnraastitmlailVLGAALV--QKGQLRVGEVVAFV----GFATLLIGRLDQVVAFINQVFMAAPKLEe 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 331 ---VMDD-PTIAPAQHVDPTAKItRGKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEF 406
Cdd:PRK13657 309 ffeVEDAvPDVRDPPGAIDLGRV-KGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 407 QSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIE 486
Cdd:PRK13657 388 QSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 487 RGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKI 566
Cdd:PRK13657 468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
490 500
....*....|....*....|...
gi 1027832812 567 VERGSNDELLQQHGYYYDMIQLQ 589
Cdd:PRK13657 548 VESGSFDELVARGGRFAALLRAQ 570
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
10-589 |
3.76e-81 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 268.92 E-value: 3.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 10 RSMPVKEQLTVIRRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYL-KTGHATVPVMwyfaglyFFGMVVR 88
Cdd:TIGR01846 116 RSVAGKALKFGFSWFIPAIIRYRKQFREVLLISLALQLFALVTPLLFQVVIDKVLvHRGLSTLSVL-------ALAMLAV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 89 ALMQFVQNFSSTMGAEYMLENVRRQMFAKLHR----MGMRYFDQVPGGSILSR----------LTNDTMSfsnfwALFNT 154
Cdd:TIGR01846 189 AIFEPALGGLRTYLFAHLTSRIDVELGARLYRhllgLPLGYFESRRVGDTVARvreleqirnfLTGSALT-----VVLDL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 155 LFTAFFavissFVAMYLTDAQIALWLLVFMPFLAVtIWYYqrYSSRVYRRMR---ERLSELNTKLSEAITGISVIQQFRQ 231
Cdd:TIGR01846 264 LFVVVF-----LAVMFFYSPTLTGVVIGSLVCYAL-LSVF--VGPILRKRVEdkfERSAAATSFLVESVTGIETIKATAT 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 232 EHRINGEFDHTNDAYFKTRQAMIRTnSLLLSPLIDLFYALGTVMVLgIFGVRG-LNGYVAAGVVYAFITYLNNFYNPMTS 310
Cdd:TIGR01846 336 EPQFQNRWDRQLAAYVAASFRVTNL-GNIAGQAIELIQKLTFAILL-WFGAHLvIGGALSPGQLVAFNMLAGRVTQPVLR 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 311 MMDNLSDFQDGVVAGSRVLRVMDDPTIAPAQHVDPTAKItRGKIEFRHVTFAYDGQHP-VLKDVSFVAEPGQTVALVGQT 389
Cdd:TIGR01846 414 LAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAALPEL-RGAITFENIRFRYAPDSPeVLSNLNLDIKPGEFIGIVGPS 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 390 GSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKA 469
Cdd:TIGR01846 493 GSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGA 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 470 DDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRL 549
Cdd:TIGR01846 573 HDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRL 652
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1027832812 550 STIQNADLILVLNQGKIVERGSNDELLQQHGYYYDMIQLQ 589
Cdd:TIGR01846 653 STVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
352-571 |
1.78e-78 |
|
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: 247.41 E-value: 1.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 352 GKIEFRHVTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKM 430
Cdd:cd03244 1 GDIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEPFMFYGDINSNIRMFNdQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPK 510
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 511 ILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGS 571
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
354-589 |
1.54e-76 |
|
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: 242.78 E-value: 1.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHP-VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGL 432
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKIL 512
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 513 ILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYYYDMIQLQ 589
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
35-561 |
3.35e-74 |
|
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: 246.43 E-value: 3.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIylprVLQTF-----IDHYLKTGHATVPVMWYFAGLYFFgMVVRALMQFVQNFSSTMGAEYMLEN 109
Cdd:TIGR02857 4 ALALLALLGVLGALLI----IAQAWllarvVDGLISAGEPLAELLPALGALALV-LLLRALLGWLQERAAARAAAAVKSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 110 VRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALF-NTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLA 188
Cdd:TIGR02857 79 LRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYlPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 189 VTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYfktRQAMIRT--NSLLLSPLID 266
Cdd:TIGR02857 159 IFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEY---RERTMRVlrIAFLSSAVLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 267 LFYALGTVMVLGIFGVRGLNGYVAagVVYAFITYL--NNFYNPMTSMMDNLSDFQDGVVAGSRVLRVMDDPTiAPAQHVD 344
Cdd:TIGR02857 236 LFATLSVALVAVYIGFRLLAGDLD--LATGLFVLLlaPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAP-RPLAGKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 345 PTAKITRGKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAE 424
Cdd:TIGR02857 313 PVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 425 ELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFART 504
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 505 IVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVL 561
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
23-587 |
5.95e-71 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 239.02 E-value: 5.95e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 23 RLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHyLKTGHATVPVMWYFAGLYFFGMVVRALMqfvqnfssTMG 102
Cdd:TIGR01192 9 RALSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDA-ISSKSDVLPTLALWAGFGVFNTIAYVLV--------ARE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 103 AEYMLENVR----RQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALFN----TLFTAFFAVISSFVAMyltDA 174
Cdd:TIGR01192 80 ADRLAHGRRatllTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMrqhlATFVALFLLIPTAFAM---DW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 175 QIALWLLVfmpfLAVTIWYYQRYssrVYRRMRERLSELN-------TKLSEAITGISVIQQFrqeHRINGEfdhtndayf 247
Cdd:TIGR01192 157 RLSIVLMV----LGILYILIAKL---VMQRTKNGQAAVEhhyhnvfKHVSDSISNVSVVHSY---NRIEAE--------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 248 kTRQAMIRTNSLLLS--PLIDlFYALGT-------------VMVLGIFGVRglNGYVAAGVVYAFItylnNFYNPMTSMM 312
Cdd:TIGR01192 218 -TSALKQFTNNLLSAqyPVLD-WWALASglnrmastismmcILVIGTVLVI--KGELSVGEVIAFI----GFANLLIGRL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 313 DNLSDFQDGVVAGSRVLR---VMDDPTIAPAQHVD-PTAKITRGKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQ 388
Cdd:TIGR01192 290 DQMSGFITQIFEARAKLEdffDLEDSVFQREEPADaPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 389 TGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVK 468
Cdd:TIGR01192 370 TGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 469 ADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHR 548
Cdd:TIGR01192 450 AHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHR 529
|
570 580 590
....*....|....*....|....*....|....*....
gi 1027832812 549 LSTIQNADLILVLNQGKIVERGSNDELLQQHGYYYDMIQ 587
Cdd:TIGR01192 530 LSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLR 568
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
354-565 |
1.03e-70 |
|
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: 225.34 E-value: 1.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQ-HPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGL 432
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEPFMFYGDINSNIrmfndqisdeqvqaaarfvkaddfindlpenyqsrviergasYSSGQRQLISFARTIVTDPKIL 512
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 513 ILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGK 565
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
352-570 |
3.99e-69 |
|
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: 222.85 E-value: 3.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 352 GKIEFRHVTFAYDGQ-HPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKM 430
Cdd:cd03245 1 GRIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPK 510
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 511 ILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERG 570
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-586 |
3.32e-68 |
|
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: 234.63 E-value: 3.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 13 PVKEQLTVIRRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYLKtgHATVPVMWYFAGLYFFGMVVRALMQ 92
Cdd:TIGR01193 136 PIKEKENSLLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIP--HKMMGTLGIISIGLIIAYIIQQILS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 93 FVQNFSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTnDTMSFSNfwALFNTLFTAFF----AVISSFVA 168
Cdd:TIGR01193 214 YIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIID--ALASTILSLFLdmwiLVIVGLFL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 169 MYLtDAQIALWLLVFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQE----HRINGEFD---H 241
Cdd:TIGR01193 291 VRQ-NMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEaerySKIDSEFGdylN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 242 TNDAYFKTRQAMIRTNSLLLSPLIDLFYALGTVMVLgifgvrglNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDG 321
Cdd:TIGR01193 370 KSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVM--------RGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 322 VVAGSRVLRVMDDPTIAPAQHVDPTAKITRGKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLM 401
Cdd:TIGR01193 442 RVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLV 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 402 RFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRM-FNDQISDEQVQAAARFVKADDFINDLPENY 480
Cdd:TIGR01193 522 GFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 481 QSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQEnRTTIAIAHRLSTIQNADLILV 560
Cdd:TIGR01193 602 QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIV 680
|
570 580
....*....|....*....|....*.
gi 1027832812 561 LNQGKIVERGSNDELLQQHGYYYDMI 586
Cdd:TIGR01193 681 LDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
336-566 |
2.24e-66 |
|
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: 215.80 E-value: 2.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 336 TIAPaQHVDptakitrGKIEFRHVTFAYDGQ--HPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLI 413
Cdd:cd03248 2 SLAP-DHLK-------GIVKFQNVTFAYPTRpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 414 DDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSS 493
Cdd:cd03248 74 DGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 494 GQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKI 566
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
111-585 |
3.46e-62 |
|
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: 223.28 E-value: 3.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 111 RRQMFAKLH---RMGMRYFDQVPGGSILSRLTNDTMSFSNFWA-LFNTLFTAFFAVISSFVAMYLTDAQIAlwllVFMPF 186
Cdd:TIGR00957 1038 RVLHQDLLHnklRSPMSFFERTPSGNLVNRFSKELDTVDSMIPpVIKMFMGSLFNVIGALIVILLATPIAA----VIIPP 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 187 LAVTIWYYQRY---SSRVYRRMRE-RLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSLLLS 262
Cdd:TIGR00957 1114 LGLLYFFVQRFyvaSSRQLKRLESvSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAV 1193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 263 PL------IDLFYALgtvmvLGIFGVRGLN-GYVAAGVVYAF--ITYLNnfynPMTSMMdnlSDFQDGVVAGSRVLRVMD 333
Cdd:TIGR00957 1194 RLecvgncIVLFAAL-----FAVISRHSLSaGLVGLSVSYSLqvTFYLN----WLVRMS---SEMETNIVAVERLKEYSE 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 334 DPTIAPAQ---HVDPTAKITRGKIEFRHVTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSG 409
Cdd:TIGR00957 1262 TEKEAPWQiqeTAPPSGWPPRGRVEFRNYCLRYrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEG 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 410 EVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNdQISDEQVQAAARFVKADDFINDLPENYQSRVIERGA 489
Cdd:TIGR00957 1342 EIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFS-QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGE 1420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 490 SYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVER 569
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
490
....*....|....*.
gi 1027832812 570 GSNDELLQQHGYYYDM 585
Cdd:TIGR00957 1501 GAPSNLLQQRGIFYSM 1516
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
150-589 |
7.33e-61 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 214.05 E-value: 7.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 150 ALFNTLFTAFFAVISsFVAMYLTDAQIALWLLVFMPF-LAVTIW--YYQRyssRVYRRMRERLSELNTKLSEAITGISVI 226
Cdd:TIGR03797 252 STLTTLLSGIFALLN-LGLMFYYSWKLALVAVALALVaIAVTLVlgLLQV---RKERRLLELSGKISGLTVQLINGISKL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 227 Q----QFRQEHRINGEFDHTNDAYFKTRQAMIrtnslLLSPLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLN 302
Cdd:TIGR03797 328 RvagaENRAFARWAKLFSRQRKLELSAQRIEN-----LLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 303 NFYNPMTSMMDNLSDFQDGVVAGSRVLRVMDDPTIAPAQHVDPtaKITRGKIEFRHVTFAYD-GQHPVLKDVSFVAEPGQ 381
Cdd:TIGR03797 403 SFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAKTDP--GKLSGAIEVDRVTFRYRpDGPLILDDVSLQIEPGE 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 382 TVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNdQISDEQVQ 461
Cdd:TIGR03797 481 FVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA-PLTLDEAW 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 462 AAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRt 541
Cdd:TIGR03797 560 EAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR- 638
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1027832812 542 tIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYYYDMIQLQ 589
Cdd:TIGR03797 639 -IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
44-589 |
1.08e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 211.11 E-value: 1.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 44 LISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFssTMGAEYMLE-NVRRQMFAKLHRMG 122
Cdd:PRK10789 6 IIAMLQLIPPKVVGIIVDGVTEQHMTTGQILMWIGTMVLIAVVVYLLRYVWRVL--LFGASYQLAvELREDFYRQLSRQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 123 MRYFDQVPGGSILSRLTNDT--MSFS---NFWALFNTLFT--AFFAVISSFVAMYLTdaqiaLWLLVFMPFLAVTIwyyQ 195
Cdd:PRK10789 84 PEFYLRHRTGDLMARATNDVdrVVFAageGVLTLVDSLVMgcAVLIVMSTQISWQLT-----LLALLPMPVMAIMI---K 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 196 RYSSRVYRRMRER---LSELNTKLSEAITGISVIQQFRQEHRINGEFdhTNDAYFKTRQAM--IRTNSLLlSPLIdlFYA 270
Cdd:PRK10789 156 RYGDQLHERFKLAqaaFSSLNDRTQESLTSIRMIKAFGLEDRQSALF--AADAEDTGKKNMrvARIDARF-DPTI--YIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 271 LGTVMVLGIFGvrG----LNGYVAAGVVYAFITYLNNFYNPMTSM--MDNLsdFQDGVVAGSRVLRVMDD-PTIAPAQHV 343
Cdd:PRK10789 231 IGMANLLAIGG--GswmvVNGSLTLGQLTSFVMYLGLMIWPMLALawMFNI--VERGSAAYSRIRAMLAEaPVVKDGSEP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 344 DPTakiTRGKIEFRHVTFAYDG-QHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYP 422
Cdd:PRK10789 307 VPE---GRGELDVNIRQFTYPQtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 423 AEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFA 502
Cdd:PRK10789 384 LDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 503 RTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYY 582
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
....*..
gi 1027832812 583 YDMIQLQ 589
Cdd:PRK10789 544 RDMYRYQ 550
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
79-587 |
1.37e-59 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 215.61 E-value: 1.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 79 GLYFFGMVVRALMQFVQNFSSTMGAEYMLENVrrqMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFS-NFWALFNTLFT 157
Cdd:PLN03232 957 ALLGFGQVAVTFTNSFWLISSSLHAAKRLHDA---MLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDrNVANLMNMFMN 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 158 AFFAVISSFvAMYLTDAQIALWLLvfMPFLAV---TIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHR 234
Cdd:PLN03232 1034 QLWQLLSTF-ALIGTVSTISLWAI--MPLLILfyaAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDR 1110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 235 ---INGEFDHTNdayFKTRQAMIRTNSLLLSPLIdlfyALGTVMV--LGIFGVRGlNGYVAAGVVYA-----FITYLNNF 304
Cdd:PLN03232 1111 makINGKSMDNN---IRFTLANTSSNRWLTIRLE----TLGGVMIwlTATFAVLR-NGNAENQAGFAstmglLLSYTLNI 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 305 YNPMTSMMDNLSDFQDGVVAGSRVLRVMDDPTIAPA---QHVDPTAKITRGKIEFRHVTFAY-DGQHPVLKDVSFVAEPG 380
Cdd:PLN03232 1183 TTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAiieNNRPVSGWPSRGSIKFEDVHLRYrPGLPPVLHGLSFFVSPS 1262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 381 QTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQiSDEQV 460
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEH-NDADL 1341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 461 QAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR 540
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSC 1421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1027832812 541 TTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGY-YYDMIQ 587
Cdd:PLN03232 1422 TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFRMVH 1469
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
35-328 |
1.83e-59 |
|
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: 200.08 E-value: 1.83e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHatVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQM 114
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD--LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFW-ALFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIWY 193
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVsSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 194 YQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYALGT 273
Cdd:cd07346 159 FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSA-LFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 274 VMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd07346 238 ALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-549 |
6.30e-57 |
|
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: 200.28 E-value: 6.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 21 IRRLLPYAKPFKCFFIAAIVFSGLISVVNIYLprvlqTFIDHYLKTGHATVP-VMWYFA---GLYFFGmVVRALMQFVQN 96
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVAL-----LGVSAWLISRAAEMPpVLYLSVaavAVRAFG-IGRAVFRYLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 97 FSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFW----------ALFNTLFTAFFAVISSF 166
Cdd:TIGR02868 75 LVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYvrvivpagvaLVVGAAAVAAIAVLSVP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 167 VAMYLtdAQIALWLLVFMPFLAvtiwyyQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAY 246
Cdd:TIGR02868 155 AALIL--AAGLLLAGFVAPLVS------LRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADREL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 247 FKTRQAMIRTNSLLlSPLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFI-TYLNNFyNPMTSMMDNLSDFQDGVVAG 325
Cdd:TIGR02868 227 TRAERRAAAATALG-AALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVlLPLAAF-EAFAALPAAAQQLTRVRAAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 326 SRVLRVMDD--PTIAPAQHVDPTAKITRGKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRF 403
Cdd:TIGR02868 305 ERIVEVLDAagPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 404 YEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSR 483
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 484 VIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETE-EMIQTGLDRIQEnRTTIAIAHRL 549
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETAdELLEDLLAALSG-RTVVLITHHL 530
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
77-587 |
1.17e-55 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 203.82 E-value: 1.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 77 FAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENvrrqMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALFNTLF 156
Cdd:PLN03130 959 YALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDA----MLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMF 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 157 -TAFFAVISSFVAMYLTDAqIALWLLvfMPFLAV---TIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQE 232
Cdd:PLN03130 1035 lGQIFQLLSTFVLIGIVST-ISLWAI--MPLLVLfygAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAY 1111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 233 HR---INGEFDHTNDAYFKTRQAMIRTNSLLLSplidlfyALGTVMV--LGIFGVRGlNGYVAAGVVYA-----FITYLN 302
Cdd:PLN03130 1112 DRmaeINGRSMDNNIRFTLVNMSSNRWLAIRLE-------TLGGLMIwlTASFAVMQ-NGRAENQAAFAstmglLLSYAL 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 303 NFYNPMTSMMDNLSDFQDGVVAGSRVLRVMDDPTIAPA---QHVDPTAKITRGKIEFRHVTFAYDGQ-HPVLKDVSFVAE 378
Cdd:PLN03130 1184 NITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLvieNNRPPPGWPSSGSIKFEDVVLRYRPElPPVLHGLSFEIS 1263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 379 PGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQiSDE 458
Cdd:PLN03130 1264 PSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEH-NDA 1342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 459 QVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQE 538
Cdd:PLN03130 1343 DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFK 1422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1027832812 539 NRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQ-QHGYYYDMIQ 587
Cdd:PLN03130 1423 SCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSnEGSAFSKMVQ 1472
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
35-328 |
2.07e-54 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 186.54 E-value: 2.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVpvMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQM 114
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGV--LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFwaL---FNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTI 191
Cdd:cd18546 79 FAHLQRLSLDFHERETSGRIMTRMTSDIDALSEL--LqtgLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 192 WYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYAL 271
Cdd:cd18546 157 RWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVA-IYFPGVELLGNL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 272 GTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18546 236 ATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
352-571 |
1.07e-51 |
|
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: 176.45 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 352 GKIEFRHVTFAYDGQHP-VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKM 430
Cdd:cd03369 5 GEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEPFMFYGDINSNIRMFNDQiSDEQVQAAARfvkaddfindlpenyqsrVIERGASYSSGQRQLISFARTIVTDPK 510
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFDEY-SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 511 ILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGS 571
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
359-592 |
4.34e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 185.43 E-value: 4.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 359 VTFAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQsGEVLIDDRDIREYPAEELRQKMGLVLQEPF 438
Cdd:PRK11174 356 EILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 439 MFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEAT 518
Cdd:PRK11174 434 LPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 519 ANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYYYDMIQLQNSA 592
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
35-328 |
4.76e-51 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 177.62 E-value: 4.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVpvMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQM 114
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLREL--LWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNF--WALFNtLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIW 192
Cdd:cd18542 79 YDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFlaFGLVE-LVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 193 YYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQF-RQEHRINgEFDHTNDAYFKTRQAMIRTNSLLLsPLIDLFYAL 271
Cdd:cd18542 158 VFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFaREDYEIE-KFDKENEEYRDLNIKLAKLLAKYW-PLMDFLSGL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 272 GTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18542 236 QIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
35-328 |
2.41e-50 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 175.73 E-value: 2.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHatVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQM 114
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGD--LSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNF--WALFNtLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIW 192
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLlsNGLIN-LIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 193 YYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYALG 272
Cdd:cd18545 159 LLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNA-LFWPLVELISALG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 273 TVMVLgIFGVRGL-NGYVAAGVVYAFITYLNNFYNPMTsmmdNLSDF----QDGVVAGSRV 328
Cdd:cd18545 238 TALVY-WYGGKLVlGGAITVGVLVAFIGYVGRFWQPIR----NLSNFynqlQSAMASAERI 293
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
322-587 |
1.23e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 181.18 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 322 VVAGSRVLRVMD-DPTIA-PAQHvdpTAKITRGKIEFRHVTFAYDGQ-HPVLKDVSFVAEPGQTVALVGQTGSGKTSTIN 398
Cdd:PRK11160 308 IASARRINEITEqKPEVTfPTTS---TAAADQVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 399 VLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDlPE 478
Cdd:PRK11160 385 LLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 479 NYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLI 558
Cdd:PRK11160 464 GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543
|
250 260
....*....|....*....|....*....
gi 1027832812 559 LVLNQGKIVERGSNDELLQQHGYYYDMIQ 587
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
351-578 |
2.36e-49 |
|
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: 179.94 E-value: 2.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 351 RGKIEFRHVTFAYDGQH-PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQK 429
Cdd:COG4618 328 KGRLSVENLTVVPPGSKrPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 430 MGLVLQEPFMFYGDINSNIRMFNDqISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDP 509
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIARFGD-ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 510 KILILDEATANVDTETEEMIQTGLDRI-QENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQ 578
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
35-328 |
1.04e-48 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 171.45 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVpvMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQM 114
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEA--LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWA-LFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIWY 193
Cdd:cd18552 79 FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTsALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 194 YQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYALGT 273
Cdd:cd18552 159 IGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARA-LSSPLMELLGAIAI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 274 VMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18552 238 ALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
35-328 |
1.13e-48 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 171.43 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPV----MWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENV 110
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVdfsgLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 111 RRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNfwAL---FNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFL 187
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQ--ALsqsLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 188 AVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKT-RQAMIRTNslLLSPLID 266
Cdd:cd18547 159 LLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKAsFKAQFYSG--LLMPIMN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 267 LFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18547 237 FINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
35-328 |
3.95e-48 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 169.64 E-value: 3.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHyLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQM 114
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDL-VTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWA-LFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIWY 193
Cdd:cd18778 80 YDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIAdGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 194 YQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYALGT 273
Cdd:cd18778 160 YSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWA-IFHPLMEFLTSLGT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 274 VMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18778 239 VLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-328 |
2.20e-46 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 164.96 E-value: 2.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 34 FFIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGhaTVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQ 113
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFITPG--TLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 114 MFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNF--WALFNtLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTI 191
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIisWGLVD-LVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 192 WYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKT--RQAMIrtnSLLLSPLIDLFY 269
Cdd:cd18540 160 IYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRAsvRAARL---SALFLPIVLFLG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 270 ALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18540 237 SIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
354-579 |
6.33e-46 |
|
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: 161.73 E-value: 6.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLV 433
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEP----FMF-------YGDINSNIRmfNDQIsDEQVQAAARFVKADDF----INDLpenyqsrviergasySSGQRQL 498
Cdd:COG1122 81 FQNPddqlFAPtveedvaFGPENLGLP--REEI-RERVEEALELVGLEHLadrpPHEL---------------SGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 499 ISFARTIVTDPKILILDEATANVDTE-TEEMIQTgLDRIQENRTTIAIA-HRLSTI-QNADLILVLNQGKIVERGSNDEL 575
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRgRRELLEL-LKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
....
gi 1027832812 576 LQQH 579
Cdd:COG1122 222 FSDY 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-588 |
7.02e-46 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 174.83 E-value: 7.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 20 VIRRLLPYAKPFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDhylktghatvpvmwyFAGL------YFFGMVVRALMQF 93
Cdd:PTZ00265 816 VYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFD---------------FANLeansnkYSLYILVIAIAMF 880
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 94 V----QNFSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQ---VPGgsILSRLTNDTMSfsnfwaLFNTLFTAFFAVISSF 166
Cdd:PTZ00265 881 IsetlKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQdkhAPG--LLSAHINRDVH------LLKTGLVNNIVIFTHF 952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 167 VAMYLTDAQIALWllvFMPFLAVTIWYYQRYSSRVYRrMRERLSELNTKLSEAITGISVIQQFRQEHRIngefdhTNDAY 246
Cdd:PTZ00265 953 IVLFLVSMVMSFY---FCPIVAAVLTGTYFIFMRVFA-IRARLTANKDVEKKEINQPGTVFAYNSDDEI------FKDPS 1022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 247 FKTRQAMIRTNSLLLSPLIDLFYAL--------------GTVMVLGIFGVRGLNGYVAAGVVYAFITYL-NNFYNPMTSM 311
Cdd:PTZ00265 1023 FLIQEAFYNMNTVIIYGLEDYFCNLiekaidysnkgqkrKTLVNSMLWGFSQSAQLFINSFAYWFGSFLiRRGTILVDDF 1102
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 312 MDNLSDFQ-DGVVAGsRVLRVMDD------------PTIAPAQHVD---------PTAKITRGKIEFRHVTFAYDGQH-- 367
Cdd:PTZ00265 1103 MKSLFTFLfTGSYAG-KLMSLKGDsenaklsfekyyPLIIRKSNIDvrdnggiriKNKNDIKGKIEIMDVNFRYISRPnv 1181
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 368 PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ---------------------------------------- 407
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefslt 1261
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 408 --------------SGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFI 473
Cdd:PTZ00265 1262 keggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFI 1341
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 474 NDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRLST 551
Cdd:PTZ00265 1342 ESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIAS 1421
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1027832812 552 IQNADLILVLNQ----GKIVE-RGSNDELLQ-QHGYYYDMIQL 588
Cdd:PTZ00265 1422 IKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-589 |
1.94e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 170.21 E-value: 1.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 25 LPYAKPFKCF-----------FIAAIVFSGLisvvniyLPRVLQTF--IDHYLKTGHATVPVMwyfaglyfFGMVVRALM 91
Cdd:PTZ00265 45 IPFFLPFKCLpashrkllgvsFVCATISGGT-------LPFFVSVFgvIMKNMNLGENVNDII--------FSLVLIGIF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 92 QFVQNFSSTMGAEY----MLENVRRQMFAKLHRMGMRYFDQVPGgsilSRLTND-TMSFSNFWALFNTLFTAFFAVISSF 166
Cdd:PTZ00265 110 QFILSFISSFCMDVvttkILKTLKLEFLKSVFYQDGQFHDNNPG----SKLTSDlDFYLEQVNAGIGTKFITIFTYASAF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 167 VAMYL----TDAQIALWLLVFMPFLAVTIWYYQRyssRVYRRMRERLSELNTKLS---EAITGISVIQQFRQEHRINGEF 239
Cdd:PTZ00265 186 LGLYIwslfKNARLTLCITCVFPLIYICGVICNK---KVKINKKTSLLYNNNTMSiieEALVGIRTVVSYCGEKTILKKF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 240 DHTNDAYFKTrqaMIRTNSL------LLSPLIDLFYALG-----TVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNpM 308
Cdd:PTZ00265 263 NLSEKLYSKY---ILKANFMeslhigMINGFILASYAFGfwygtRIIISDLSNQQPNNDFHGGSVISILLGVLISMFM-L 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 309 TSMMDNLSDFQDGVVAGSRVLRVMDDPTIAPAQHVDPTAKITRgKIEFRHVTFAYDGQHPV--LKDVSFVAEPGQTVALV 386
Cdd:PTZ00265 339 TIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 387 GQTGSGKTSTINVLMRFYEFQSGEVLIDD-RDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRM--------------- 450
Cdd:PTZ00265 418 GESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyy 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 451 ------------------------FNDQ------------------ISDEQVQAAARFVKADDFINDLPENYQSRVIERG 488
Cdd:PTZ00265 498 nedgndsqenknkrnscrakcagdLNDMsnttdsneliemrknyqtIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNA 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 489 ASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQ--ENRTTIAIAHRLSTIQNADLILVL----- 561
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrer 657
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 562 -------------------------NQGK-----------------IVERGSNDELLQ-QHGYYYDMIQLQ 589
Cdd:PTZ00265 658 gstvdvdiigedptkdnkennnknnKDDNnnnnnnnnnkinnagsyIIEQGTHDALMKnKNGIYYTMINNQ 728
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
36-328 |
4.20e-44 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 158.83 E-value: 4.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 36 IAAIVFSGLISVVNIYLPRVLqtfIDHYLKT---GHATVPVMWYFAGLyFFGMVVRALMQFVQNFSSTMGAEYMLENVRR 112
Cdd:cd18563 5 FLLMLLGTALGLVPPYLTKIL---IDDVLIQlgpGGNTSLLLLLVLGL-AGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 113 QMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWAL-FNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTI 191
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDgLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 192 WYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYAL 271
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWA-TFFPLLTFLTSL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 272 GTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18563 240 GTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
30-578 |
2.00e-43 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 163.29 E-value: 2.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 30 PFKCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYF--AGLYFFGMVVRALMQFV-----QNFSSTMG 102
Cdd:TIGR01842 3 KVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVlaLGLYLFLGLLDALRSFVlvrigEKLDGALN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 103 AEYMLENVRrqmfAKLHRMGMRyfdqvpGGSILSRLTN--DTMSFSNFWALFNT-LFTAFFAVIssfvamYLTDAQIALW 179
Cdd:TIGR01842 83 QPIFAASFS----ATLRRGSGD------GLQALRDLDQlrQFLTGPGLFAFFDApWMPIYLLVC------FLLHPWIGIL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 180 LLVFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSL 259
Cdd:TIGR01842 147 ALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 260 LlSPLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRVLRVMDDPTIAP 339
Cdd:TIGR01842 227 L-SNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 340 AQHVDPTAkitRGKIEFRHVTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDI 418
Cdd:TIGR01842 306 PAMPLPEP---EGHLSVENVTIVPpGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 419 REYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQL 498
Cdd:TIGR01842 383 KQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 499 ISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQ-ENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQ 577
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
.
gi 1027832812 578 Q 578
Cdd:TIGR01842 543 K 543
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
352-578 |
9.08e-43 |
|
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: 154.30 E-value: 9.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 352 GKIEFRHVTFAYDGQ-HPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKM 430
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEPFMFYGDINSNIRMfNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPK 510
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDP-ECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 511 ILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQ 578
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
354-580 |
3.50e-42 |
|
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: 151.93 E-value: 3.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPaEELRQKMGLV 433
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMFYGD-INSNIRMFND--QISDEQVQAaarfvKADDFI--NDLPENYQSRViergASYSSGQRQLISFARTIVTD 508
Cdd:COG4555 80 PDERGLYDRLtVRENIRYFAElyGLFDEELKK-----RIEELIelLGLEEFLDRRV----GELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 509 PKILILDEATANVDTeteeMIQTGLDRI-----QENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQQHG 580
Cdd:COG4555 151 PKVLLLDEPTNGLDV----MARRLLREIlralkKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
35-328 |
4.72e-42 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 153.34 E-value: 4.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHyLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSsTMGAEYMLEN-VRRQ 113
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDA-LTAGTLTASQLLRYALLILLLALLIGIFRFLWRYL-IFGASRRIEYdLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 114 MFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWAL-FNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIW 192
Cdd:cd18541 79 LFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPgILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 193 YYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYALG 272
Cdd:cd18541 159 RLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDA-LFFPLIGLLIGLS 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1027832812 273 TVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18541 238 FLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
355-565 |
4.51e-41 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 148.00 E-value: 4.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 355 EFRHVTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLV 433
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPF-MFygdINSNIR------MFNDQISDEQVQAAARFVKADDFINDLPEnyqsRVIErgaSYSSGQRQLISFARTIV 506
Cdd:cd03225 81 FQNPDdQF---FGPTVEeevafgLENLGLPEEEIEERVEEALELVGLEGLRD----RSPF---TLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 507 TDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIA-HRLSTIQN-ADLILVLNQGK 565
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
35-321 |
1.76e-40 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 149.14 E-value: 1.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGhaTVPVMWYFAGLYFFGMVVRALMQ-FVQNFSSTMGAeYMLENVRRQ 113
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSK--NLRLILIIGAILLALYILRTLLNyFVTYWGHVMGA-RIETDMRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 114 MFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFwA--LFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTI 191
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISEL-AhhGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 192 WYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSLLLSpLIDLFYAL 271
Cdd:cd18549 160 IYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFS-GMNFFTNL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1027832812 272 GTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDG 321
Cdd:cd18549 239 LNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKG 288
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
354-566 |
1.09e-39 |
|
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: 142.74 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGL 432
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEPFMFYGDINSNIrmfndqisdeqvqaaarfvkaddfindlpenyqsrviergasYSSGQRQLISFARTIVTDPKIL 512
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 513 ILDEATANVDTETEEMIQTGLDRIQENRTT-IAIAHRLSTIQNADLILVLNQGKI 566
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATrIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
354-581 |
8.53e-39 |
|
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: 149.67 E-value: 8.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYD----GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAE---EL 426
Cdd:COG1123 261 LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrEL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 427 RQKMGLVLQEPF------MFYGDINS----NIRMFNDQISDEQVQAAARFVkaddfinDLPENYQSRvieRGASYSSGQR 496
Cdd:COG1123 341 RRRVQMVFQDPYsslnprMTVGDIIAeplrLHGLLSRAERRERVAELLERV-------GLPPDLADR---YPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 497 QLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSND 573
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
250
....*....|
gi 1027832812 574 ELLQ--QHGY 581
Cdd:COG1123 491 EVFAnpQHPY 500
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
123-575 |
7.23e-38 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 150.31 E-value: 7.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 123 MRYFDQVPGGSILSRLTNDTMSFSNFWAL-FNTLFTAFFAVISSfvaMYLTDAQIALWLLVFMP--FLAVTIWYYQRYSS 199
Cdd:PTZ00243 1046 MSFFDTTPLGRILNRFSRDIDILDNTLPMsYLYLLQCLFSICSS---ILVTSASQPFVLVALVPcgYLYYRLMQFYNSAN 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 200 RVYRRMRERL-SELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSLL------LSPLIDLFYAL- 271
Cdd:PTZ00243 1123 REIRRIKSVAkSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLgvrvefLSNIVVTVIALi 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 272 ---GTV--------------MVLGIFGVRGLNGYV--AAGV------VYAFITYLNNFYNPMTSMMDNLSDF---QDGV- 322
Cdd:PTZ00243 1203 gviGTMlratsqeiglvslsLTMAMQTTATLNWLVrqVATVeadmnsVERLLYYTDEVPHEDMPELDEEVDAlerRTGMa 1282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 323 --VAGSRVLRVMDDPTIAPaqHVdptakITRGKIEFRHVTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINV 399
Cdd:PTZ00243 1283 adVTGTVVIEPASPTSAAP--HP-----VQAGSLVFEGVQMRYrEGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLT 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 400 LMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNdQISDEQVQAAARFVKADDFINDLPEN 479
Cdd:PTZ00243 1356 FMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFL-EASSAEVWAALELVGLRERVASESEG 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 480 YQSRVIERGASYSSGQRQLISFARTIVTDPKILIL-DEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLI 558
Cdd:PTZ00243 1435 IDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKI 1514
|
490
....*....|....*..
gi 1027832812 559 LVLNQGKIVERGSNDEL 575
Cdd:PTZ00243 1515 IVMDHGAVAEMGSPREL 1531
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
36-328 |
8.96e-37 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 139.18 E-value: 8.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 36 IAAIVFSGLISVVNIYLprvLQTFIDHYLKTGHATVPVMWYF-------------AGLYFFGMVVRALMQFVQNFSSTMG 102
Cdd:cd18564 5 LLALLLETALRLLEPWP---LKVVIDDVLGDKPLPGLLGLAPllgpdplallllaAAALVGIALLRGLASYAGTYLTALV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 103 AEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWA-LFNTLFTAFFAVISSFVAMYLTDAQIALWLL 181
Cdd:cd18564 82 GQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVsGVLPLLTNLLTLVGMLGVMFWLDWQLALIAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 182 VFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLL 261
Cdd:cd18564 162 AVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQA-LL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 262 SPLIDLFYALGTVMVLGiFGVRG-LNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18564 241 SPVVDVLVAVGTALVLW-FGAWLvLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
354-570 |
1.39e-36 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 136.10 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAY---DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEEL---R 427
Cdd:cd03257 2 LEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 428 QKMGLVLQEPF------MFYGDI-----NSNIRMFNDQISDEQVQAAARFVK-ADDFINDLPenYQsrviergasYSSGQ 495
Cdd:cd03257 82 KEIQMVFQDPMsslnprMTIGEQiaeplRIHGKLSKKEARKEAVLLLLVGVGlPEEVLNRYP--HE---------LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 496 RQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRLSTIQN-ADLILVLNQGKIVERG 570
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
354-570 |
1.46e-36 |
|
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: 134.36 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQH-PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYpAEELRQKMGL 432
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEPFMFYGDINSNIrmfndqisdeqvqaaarfvkaddfindlpenyqsrvierGASYSSGQRQLISFARTIVTDPKIL 512
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 513 ILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERG 570
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
354-575 |
1.55e-36 |
|
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: 136.16 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ-----SGEVLIDDRDIRE--YPAEEL 426
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 427 RQKMGLVLQEPFMFYGDINSNIR-------MFNDQISDEQVQAAARFVkaddfinDLPENYQSRVieRGASYSSGQRQLI 499
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAyglrlhgIKLKEELDERVEEALRKA-------ALWDEVKDRL--HALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 500 SFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDEL 575
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
354-576 |
2.15e-36 |
|
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: 136.28 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLV 433
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQE----PFMfygDINSNIRMFNDQISDEQVQAAARfvkADDFINDL---PENYQSRviergasY----SSGQRQLISFA 502
Cdd:cd03295 81 IQQiglfPHM---TVEENIALVPKLLKWPKEKIRER---ADELLALVgldPAEFADR-------YphelSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 503 RTIVTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRL-STIQNADLILVLNQGKIVERGSNDELL 576
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
370-519 |
6.89e-36 |
|
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: 131.62 E-value: 6.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 370 LKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYG------- 442
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 443 DINSNIRMFNDQISDEQVQAAARFVKADDFINDlpenyqsRVIERGASYSSGQRQLISFARTIVTDPKILILDEATA 519
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADR-------PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
354-566 |
3.68e-35 |
|
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: 130.21 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPaEELRQKMGLV 433
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPfMFYGDINsnirmfndqisdeqvqaaarfvkADDFINdlpenyqsrviergasYSSGQRQLISFARTIVTDPKILI 513
Cdd:cd03230 79 PEEP-SLYENLT-----------------------VRENLK----------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 514 LDEATANVDTETEEMIQTGLDRIQENRTTIAIA-HRLSTIQN-ADLILVLNQGKI 566
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
355-565 |
5.61e-35 |
|
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: 129.29 E-value: 5.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 355 EFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVL 434
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 435 QepfmfygdinsnirmfndqisdeqvqaaarfvkaddfindlpenyqsrviergasYSSGQRQLISFARTIVTDPKILIL 514
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 515 DEATANVDTETEEMIQTGLDRI-QENRTTIAIAHRLSTIQNA-DLILVLNQGK 565
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
354-579 |
9.14e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 137.73 E-value: 9.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ---SGEVLIDDRDIREYPAEELRQK 429
Cdd:COG1123 5 LEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 430 MGLVLQEPfmfygDINSNIRMFNDQISD-------------EQVQAAARFVKADDFINDLPenyqsrviergASYSSGQR 496
Cdd:COG1123 85 IGMVFQDP-----MTQLNPVTVGDQIAEalenlglsraearARVLELLEAVGLERRLDRYP-----------HQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 497 QLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLSTI-QNADLILVLNQGKIVERGSND 573
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPE 228
|
....*.
gi 1027832812 574 ELLQQH 579
Cdd:COG1123 229 EILAAP 234
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
354-576 |
2.02e-34 |
|
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: 130.93 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGqHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLV 433
Cdd:COG1120 2 LEAENLSVGYGG-RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMFYG----DI--------NSNIRMFNDQisDEQ-VQAAARFVKADDF----INDLpenyqsrviergasySSGQR 496
Cdd:COG1120 81 PQEPPAPFGltvrELvalgryphLGLFGRPSAE--DREaVEEALERTGLEHLadrpVDEL---------------SGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 497 QLISFARTIVTDPKILILDEATANVD----TETEEMIQTgLDRiQENRTTIAIAHRLS-TIQNADLILVLNQGKIVERGS 571
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRR-LAR-ERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
....*
gi 1027832812 572 NDELL 576
Cdd:COG1120 222 PEEVL 226
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
35-312 |
2.91e-34 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 131.75 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHatVPVMWYFAGLyffgMVVRALMQFV----QNFSSTMGAEYMLENV 110
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGD--LSYILRTGLL----MLLLALLGLIagilAGYFAAKASQGFGRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 111 RRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALF-NTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAV 189
Cdd:cd18548 75 RKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLlRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 190 TIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTrqaMIRTNSL--LLSPLIDL 267
Cdd:cd18548 155 VVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDT---SLKAGRLmaLLNPLMML 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1027832812 268 FYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNP--MTSMM 312
Cdd:cd18548 232 IMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSlmMLSMV 278
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
354-581 |
6.96e-34 |
|
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: 129.15 E-value: 6.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYD---GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKM 430
Cdd:COG1124 2 LEVRNLSVSYGqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEPfmfYGDINSniRMFNDQI------------SDEQVQAAARFVkaddfinDLPENYQSRvieRGASYSSGQRQL 498
Cdd:COG1124 82 QMVFQDP---YASLHP--RHTVDRIlaeplrihglpdREERIAELLEQV-------GLPPSFLDR---YPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 499 ISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDEL 575
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
....*...
gi 1027832812 576 LQ--QHGY 581
Cdd:COG1124 227 LAgpKHPY 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
354-579 |
1.16e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.67 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGqHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRdireyPAEELRQKMGLV 433
Cdd:COG1121 7 IELENLTVSYGG-RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQepfmfYGDINSN----------------IRMFN--DQISDEQVQAAARFVKADDF----INDLpenyqsrviergasy 491
Cdd:COG1121 81 PQ-----RAEVDWDfpitvrdvvlmgrygrRGLFRrpSRADREAVDEALERVGLEDLadrpIGEL--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 492 SSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRI-QENRTTIAIAHRLSTI-QNADLILVLNQGKIVEr 569
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVrEYFDRVLLLNRGLVAH- 219
|
250
....*....|
gi 1027832812 570 GSNDELLQQH 579
Cdd:COG1121 220 GPPEEVLTPE 229
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
35-308 |
2.89e-32 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 125.45 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQM 114
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALF-NTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIWY 193
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKlGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 194 YQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYALGT 273
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANG-LSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1027832812 274 VMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPM 308
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
354-576 |
5.10e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 124.72 E-value: 5.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQH-PVLKDVSFVAEPGQTVALVGQTGSGKtSTIN-VLMRFYEFQSGEVLIDDRDIREYPAEELRQKMG 431
Cdd:PRK13632 8 IKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGK-STISkILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQEP-FMFYG-----DINSNI--RMFNDQISDEQVQAAARFVKADDFINDLPENyqsrviergasYSSGQRQLISFAR 503
Cdd:PRK13632 87 IIFQNPdNQFIGatvedDIAFGLenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 504 TIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELL 576
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
354-577 |
5.45e-32 |
|
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: 123.55 E-value: 5.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEEL---RQKM 430
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEPFMFygdiNS-----NI----RMFNDqISDEQVQAAARFVKA----DDFINDLPenyqsrviergASYSSGQRQ 497
Cdd:COG1127 85 GMLFQGGALF----DSltvfeNVafplREHTD-LSEAEIRELVLEKLElvglPGAADKMP-----------SELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 498 LISFARTIVTDPKILILDEATANVD----TETEEMIQtgldRIQENR--TTIAIAHRLSTIQN-ADLILVLNQGKIVERG 570
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpitsAVIDELIR----ELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*..
gi 1027832812 571 SNDELLQ 577
Cdd:COG1127 225 TPEELLA 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
354-570 |
9.42e-32 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 122.24 E-value: 9.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEelRQKMGLV 433
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMF-YGDINSNI-------RMFNDQIsDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFARTI 505
Cdd:cd03259 78 FQDYALFpHLTVAENIafglklrGVPKAEI-RARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 506 VTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLS-TIQNADLILVLNQGKIVERG 570
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
355-570 |
1.17e-31 |
|
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: 121.00 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 355 EFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVL 434
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 435 QepFMfygdinsnirmfndqisdEQVQAAArfvKADDFINDLpenyqsrviergasySSGQRQLISFARTIVTDPKILIL 514
Cdd:cd03214 80 Q--AL------------------ELLGLAH---LADRPFNEL---------------SGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 515 DEATANVD----TETEEMIQTgLDRiQENRTTIAIAHRLS-TIQNADLILVLNQGKIVERG 570
Cdd:cd03214 122 DEPTSHLDiahqIELLELLRR-LAR-ERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
353-578 |
2.27e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.20 E-value: 2.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 353 KIEFRHVTFAYDGQ-HPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMG 431
Cdd:PRK13635 5 IIRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQEP-FMFYG-----DIN---SNIRMFNDQISdEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFA 502
Cdd:PRK13635 85 MVFQNPdNQFVGatvqdDVAfglENIGVPREEMV-ERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 503 RTIVTDPKILILDEATANVDTE-TEEMIQTGLD-RIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQ 578
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRgRREVLETVRQlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
35-328 |
2.95e-31 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 122.98 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATvPVMWYFAGLYFFGmVVRALMQFVQNFSS---TMGAEYMLenvR 111
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRS-ALWPLVLLLLALG-VAEAVLSFLRRYLAgrlSLGVEHDL---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 112 RQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTI 191
Cdd:cd18543 76 TDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 192 WYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYAL 271
Cdd:cd18543 156 RRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRA-RFWPLLEALPEL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 272 GTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18543 235 GLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
354-568 |
6.96e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.16 E-value: 6.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEE---LRQKM 430
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEpfmfygdinsnIRMFNDQ--------------ISDEQVQAAARFV--------KADDFINDLpenyqsrvierg 488
Cdd:COG2884 82 GVVFQD-----------FRLLPDRtvyenvalplrvtgKSRKEIRRRVREVldlvglsdKAKALPHEL------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 489 asySSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIA-HRLSTIQNADL-ILVLNQGKI 566
Cdd:COG2884 139 ---SGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRL 215
|
..
gi 1027832812 567 VE 568
Cdd:COG2884 216 VR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
354-577 |
7.39e-31 |
|
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: 120.30 E-value: 7.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTstinVLMR----FYEFQSGEVLIDDRDIREY-PAE--EL 426
Cdd:cd03261 1 IELRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKS----TLLRlivgLLRPDSGEVLIDGEDISGLsEAElyRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 427 RQKMGLVLQEPFMF-----YGDINSNIRM---FNDQISDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQL 498
Cdd:cd03261 76 RRRMGMLFQSGALFdsltvFENVAFPLREhtrLSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 499 ISFARTIVTDPKILILDEATANVD----TETEEMIQtgldRIQE--NRTTIAIAHRLSTI-QNADLILVLNQGKIVERGS 571
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasGVIDDLIR----SLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGT 220
|
....*.
gi 1027832812 572 NDELLQ 577
Cdd:cd03261 221 PEELRA 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
352-586 |
2.37e-30 |
|
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: 120.34 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 352 GKIEFRHVTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQsGEVLIDDRDIREYPAEELRQKM 430
Cdd:cd03289 1 GQMTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEPFMFYGDINSNIRMfNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPK 510
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDP-YGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027832812 511 ILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYYYDMI 586
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
35-328 |
4.85e-30 |
|
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: 119.46 E-value: 4.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHyLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSstmgAEYMLENVRRQM 114
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDA-LSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRT----GERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWA--LFNtLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIW 192
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITsgLPQ-LVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 193 YYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLFYALG 272
Cdd:cd18551 155 PLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEA-LIGPLMGLAVQLA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1027832812 273 TVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18551 234 LLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
354-580 |
1.73e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.98 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTST---INVLMRFYEFQSGEVLIDDRDIREYPAEELRQK 429
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIsklINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 430 MGLVLQEP-FMFYGDINSNIRMF---NDQISDEQVQAAARFVKAD----DFINDLPENyqsrviergasYSSGQRQLISF 501
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFgleNRAVPRPEMIKIVRDVLADvgmlDYIDSEPAN-----------LSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 502 ARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRLSTIQNADLILVLNQGKIVERGS------ND 573
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpveifsKV 234
|
....*..
gi 1027832812 574 ELLQQHG 580
Cdd:PRK13640 235 EMLKEIG 241
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
38-328 |
2.39e-29 |
|
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: 117.66 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 38 AIVFSGLISVVNIYLPRVLQTFIDHYLKTGH--ATVPVMWYFAGLYFFGmvvrALMQFVQNFSSTMGAEYMLENVRRQMF 115
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDldVLNELALILLAIYLLQ----SVFTFVRYYLFNIAGERIVARLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 116 AKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWAL-FNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIWYY 194
Cdd:cd18557 77 SSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDnLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 195 QRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSLLLSpLIDLFYALGTV 274
Cdd:cd18557 157 GRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQG-ITSLLIYLSLL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 275 MVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18557 236 LVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
355-566 |
3.08e-29 |
|
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: 115.32 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 355 EFRHVTFAYDGqHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRdireyPAEELRQKMGLVL 434
Cdd:cd03235 1 EVEDLTVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 435 QepfmfYGDINSN----------------IRMF--NDQISDEQVQAAARFVKADDFINdlpenyqsRVIergASYSSGQR 496
Cdd:cd03235 75 Q-----RRSIDRDfpisvrdvvlmglyghKGLFrrLSKADKAKVDEALERVGLSELAD--------RQI---GELSGGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 497 QLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRI-QENRTTIAIAHRLSTIQN-ADLILVLNQGKI 566
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
51-328 |
6.73e-29 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 116.90 E-value: 6.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 51 YLPRVLQTFIdhylktGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQVP 130
Cdd:cd18565 36 FLPLVPASLG------PADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 131 GGSILSRLTNDTMSFSNFW-ALFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIWYYQRYSSRVYRRMRERL 209
Cdd:cd18565 110 TGDLMSVLNNDVNQLERFLdDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 210 SELNTKLSEAITGISVIQQFRQEHRingEFDHTNDA---YFKTRQAMIRTNSLLLsPLIDLFYALG--TVMVLG----IF 280
Cdd:cd18565 190 GDLNARLENNLSGIAVIKAFTAEDF---ERERVADAseeYRDANWRAIRLRAAFF-PVIRLVAGAGfvATFVVGgywvLD 265
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1027832812 281 GVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18565 266 GPPLFTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
354-565 |
2.25e-28 |
|
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: 112.56 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDG----QHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRdireypaeelrqk 429
Cdd:cd03250 1 ISVEDASFTWDSgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 430 MGLVLQEPFMFYGDINSNIRM---FNDQISDEQVQAAArfVKADdfINDLPENYQSRVIERGASYSSGQRQLISFARTIV 506
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFgkpFDEERYEKVIKACA--LEPD--LEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 507 TDPKILILDEATANVDTETEEMI--QTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGK 565
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
354-566 |
2.56e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 112.50 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEE---LRQKM 430
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEpFMFYGDIN--SNIrMFNDQISD-------EQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISF 501
Cdd:cd03292 81 GVVFQD-FRLLPDRNvyENV-AFALEVTGvppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 502 ARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNA--DLILVLNQGKI 566
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-328 |
3.16e-28 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 114.50 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 34 FFIAAIVFSGLISVVNIYLprvLQTFIDHYLktGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQ 113
Cdd:cd18550 3 LVLLLILLSALLGLLPPLL---LREIIDDAL--PQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 114 MFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNfwALFNTLFTA---FFAVISSFVAMYLTDAQIALWLLVFMPFLAVT 190
Cdd:cd18550 78 LYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQS--VVTGTLTSVvsnVVTLVATLVAMLALDWRLALLSLVLLPLFVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 191 IWYYQRYSSRVYRRMRERLSELNTKLSE--AITGISVIQQFRQEHRINGEFDHTND--AYFKTRQAMI-RTNSLLLSpli 265
Cdd:cd18550 156 TRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRelRDLGVRQALAgRWFFAALG--- 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 266 dLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18550 233 -LFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
358-581 |
5.34e-28 |
|
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: 114.38 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 358 HVTFA-YDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ---SGEVLIDDRDIREYPAEELRQ----K 429
Cdd:COG0444 8 KVYFPtRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKirgrE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 430 MGLVLQEPFmfygdiNSnirmFN------DQISD-----EQVQAAARFVKADDFIN----DLPEnyqsrviERGASY--- 491
Cdd:COG0444 88 IQMIFQDPM------TS----LNpvmtvgDQIAEplrihGGLSKAEARERAIELLErvglPDPE-------RRLDRYphe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 492 -SSGQRQLISFARTIVTDPKILILDEATANVD-TeteemIQTG----LDRIQENR--TTIAIAHRLSTI-QNADLILVLN 562
Cdd:COG0444 151 lSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQilnlLKDLQRELglAILFITHDLGVVaEIADRVAVMY 225
|
250 260
....*....|....*....|.
gi 1027832812 563 QGKIVERGSNDELLQ--QHGY 581
Cdd:COG0444 226 AGRIVEEGPVEELFEnpRHPY 246
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
354-566 |
8.83e-28 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 111.04 E-value: 8.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQ---HPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEEL---- 426
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 427 RQKMGLVLQE---------------PFMFYGDINSNIRmfndqisdEQVQAAARFVKADDFINDLPenyqsrviergASY 491
Cdd:cd03255 81 RRHIGFVFQSfnllpdltalenvelPLLLAGVPKKERR--------ERAEELLERVGLGDRLNHYP-----------SEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 492 SSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR-TTIAIA-HRLSTIQNADLILVLNQGKI 566
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
36-328 |
9.26e-28 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 112.96 E-value: 9.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 36 IAAIVFSGLISVVniyLPRVLQTFIDHYLKTGHATV--PVMWYFAGLyffgMVVRALMQFVQNFSSTMGAEYMLENVRRQ 113
Cdd:cd18576 2 LILLLLSSAIGLV---FPLLAGQLIDAALGGGDTASlnQIALLLLGL----FLLQAVFSFFRIYLFARVGERVVADLRKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 114 MFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNfwALFNTL---FTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVT 190
Cdd:cd18576 75 LYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQD--TLTTTLaefLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 191 IWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKT--RQAMIRTnslLLSPLIDLF 268
Cdd:cd18576 153 AVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLalKRARIRA---LFSSFIIFL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 269 YALGTVMVLgIFGVRG-LNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18576 230 LFGAIVAVL-WYGGRLvLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
354-575 |
1.76e-27 |
|
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: 110.79 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElRQkMGLV 433
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK-RP-VNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMF-YGDINSNI------RMFNDQISDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFARTIV 506
Cdd:cd03300 78 FQNYALFpHLTVFENIafglrlKKLPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 507 TDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLS-TIQNADLILVLNQGKIVERGSNDEL 575
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
354-588 |
2.08e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.75 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDG--QHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMG 431
Cdd:PRK13650 5 IEVKNLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQEP-FMFYGDINSNIRMF---NDQIS----DEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFAR 503
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFgleNKGIPheemKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 504 TIVTDPKILILDEATANVDTETE-EMIQTgLDRIQE--NRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHG 580
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRlELIKT-IKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
....*...
gi 1027832812 581 yyyDMIQL 588
Cdd:PRK13650 233 ---DLLQL 237
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
354-569 |
3.93e-27 |
|
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: 109.48 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAY---DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRdireyPAEELRQKM 430
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEPFMF----------YGDinsNIRMFNDQISDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLIS 500
Cdd:cd03293 76 GYVFQQDALLpwltvldnvaLGL---ELQGVPKAEARERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 501 FARTIVTDPKILILDEATANVDTETEEMIQTGLDRI--QENRTTIAIAHRLS-TIQNADLILVLNQ--GKIVER 569
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
354-576 |
7.23e-27 |
|
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: 109.21 E-value: 7.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQH---PVLKDVSFVAEPGQTVALVGQTGSGKTS---TINVLMRFyefQSGEVLIDDRDIREYPAEEL- 426
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLERP---TSGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 427 --RQKMGLVLQEpfmfYGDINS-----NIrMFNDQIS-------DEQVQAAARFVKADDFINDLPenyqsrviergASYS 492
Cdd:cd03258 79 kaRRRIGMIFQH----FNLLSSrtvfeNV-ALPLEIAgvpkaeiEERVLELLELVGLEDKADAYP-----------AQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 493 SGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLSTIQN-ADLILVLNQGKIVER 569
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
....*..
gi 1027832812 570 GSNDELL 576
Cdd:cd03258 223 GTVEEVF 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
354-579 |
7.69e-27 |
|
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: 109.19 E-value: 7.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQ---KM 430
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEpfmfYGDIN----------------SNIRMFNDQISDEQVQAAARF---VKADDFINdlpenyqsrviERGASY 491
Cdd:cd03256 81 GMIFQQ----FNLIErlsvlenvlsgrlgrrSTWRSLFGLFPKEEKQRALAAlerVGLLDKAY-----------QRADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 492 SSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRI--QENRTTIAIAHRLSTI-QNADLILVLNQGKIVE 568
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLArEYADRIVGLKDGRIVF 225
|
250
....*....|.
gi 1027832812 569 RGSNDELLQQH 579
Cdd:cd03256 226 DGPPAELTDEV 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
354-574 |
1.20e-26 |
|
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: 108.29 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEEL-RQKMGL 432
Cdd:cd03219 1 LEVRGLTKRFGGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQepfmfygdinsNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIER-----------------GASYSSGQ 495
Cdd:cd03219 80 TFQ-----------IPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARERaeellervgladladrpAGELSYGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 496 RQLISFARTIVTDPKILILDEATANV-DTETEEMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSND 573
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPD 228
|
.
gi 1027832812 574 E 574
Cdd:cd03219 229 E 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
362-577 |
5.62e-26 |
|
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: 105.98 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 362 AYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEE-LRQKMGLVLQEPfmf 440
Cdd:cd03224 8 AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 441 ygdinsniRMFNDQISDEQVQAAARFVKADDFINDLPENYQ------SRVIERGASYSSGQRQLISFARTIVTDPKILIL 514
Cdd:cd03224 85 --------RIFPELTVEENLLLGAYARRRAKRKARLERVYElfprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 515 DEATA----NVDTETEEMIQtgldRIQENRTTIAIAHrlstiQNADLIL-------VLNQGKIVERGSNDELLQ 577
Cdd:cd03224 157 DEPSEglapKIVEEIFEAIR----ELRDEGVTILLVE-----QNARFALeiadrayVLERGRVVLEGTAAELLA 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
354-565 |
6.41e-26 |
|
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: 104.58 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAE--ELRQKMG 431
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQEPFMFYG-DINSNIRMfndqisdeqvqaaarfvkaddfindlpenyqsrviergaSYSSGQRQLISFARTIVTDPK 510
Cdd:cd03229 80 MVFQDFALFPHlTVLENIAL---------------------------------------GLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 511 ILILDEATANVDTETEEMIQTGLDRIQEN--RTTIAIAHRLSTIQN-ADLILVLNQGK 565
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
354-570 |
6.57e-26 |
|
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: 105.74 E-value: 6.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTvALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPaEELRQKMGLV 433
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEpFMFYGDINsnIRMFND------QISDEQVQAAARFVKADDFINDlpenyqsRVIERGASYSSGQRQLISFARTIVT 507
Cdd:cd03264 78 PQE-FGVYPNFT--VREFLDyiawlkGIPSKEVKARVDEVLELVNLGD-------RAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 508 DPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERG 570
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
354-570 |
3.47e-25 |
|
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: 103.49 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElrQKMGLV 433
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQE----PFM-FYGDINSNIRM--FNDQISDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFARTIV 506
Cdd:cd03301 78 FQNyalyPHMtVYDNIAFGLKLrkVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 507 TDPKILILDEATANVDTETEEMIQTGLDRIQEN--RTTIAIAH-RLSTIQNADLILVLNQGKIVERG 570
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
354-570 |
3.96e-25 |
|
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: 103.51 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIreypAEELRQKMGLv 433
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGY- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMFYGD--INSNIRMFNdQISDEQVQAAARfvKADDFINDLP-ENYQSRVIERgasYSSGQRQLISFARTIVTDPK 510
Cdd:cd03269 75 LPEERGLYPKmkVIDQLVYLA-QLKGLKKEEARR--RIDEWLERLElSEYANKRVEE---LSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 511 ILILDEATANVDTETEEMIQTGLDRIQENRTTIAI-AHRLSTIQN-ADLILVLNQGKIVERG 570
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
354-578 |
4.05e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.72 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElRQkMGLV 433
Cdd:COG3842 6 LELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-RN-VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQE----PFMfygDINSNI-------RMFNDQIsDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFA 502
Cdd:COG3842 83 FQDyalfPHL---TVAENVafglrmrGVPKAEI-RARVAELLELVGLEGLADRYP-----------HQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 503 RTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLS---TIqnADLILVLNQGKIVERGSNDELLQ 577
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIYE 225
|
.
gi 1027832812 578 Q 578
Cdd:COG3842 226 R 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
354-575 |
6.76e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.45 E-value: 6.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHP-VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGL 432
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEP-FMFYGDINSNIRMF---NDQISDEQVQAAARFVKAD----DFINDLPEnyqsrviergaSYSSGQRQLISFART 504
Cdd:PRK13648 88 VFQNPdNQFVGSIVKYDVAFgleNHAVPYDEMHRRVSEALKQvdmlERADYEPN-----------ALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 505 IVTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLSTIQNADLILVLNQGKIVERGSNDEL 575
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
365-581 |
7.65e-25 |
|
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: 108.62 E-value: 7.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 365 GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEfQSGEVLIDDRDIREYPAEE---LRQKMGLVLQEPfmfY 441
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP---F 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 442 GDINSniRMFNDQISDE-------QVQAAARFVKADDFIND--LPENYQSRviergasY----SSGQRQLISFARTIVTD 508
Cdd:COG4172 373 GSLSP--RMTVGQIIAEglrvhgpGLSAAERRARVAEALEEvgLDPAARHR-------YphefSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 509 PKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQ--QHGY 581
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDapQHPY 521
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
369-576 |
1.28e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 102.80 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 369 VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEelRQKMGLVLQEPFMF-----YGD 443
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFphmtvYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 444 INSNIRM-FNDQIS-DEQVQAAARFVKADDFINDLPEnyqsrviergaSYSSGQRQLISFARTIVTDPKILILDEATANV 521
Cdd:cd03299 92 IAYGLKKrKVDKKEiERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 522 DTETEEMIQTGLDRIQENR--TTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELL 576
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
112-578 |
3.52e-24 |
|
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: 108.07 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 112 RQMFAKLHRMGMRYFDQVPGGSILSRLTNDT--------MSFSNFWALFNTLFTAFFAVisSFVAMYLTDAQIALwLLVF 183
Cdd:TIGR01271 962 EQMLHSVLQAPMAVLNTMKAGRILNRFTKDMaiiddmlpLTLFDFIQLTLIVLGAIFVV--SVLQPYIFIAAIPV-AVIF 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 184 MPFLAvtiwYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQF-RQehringefdhtndAYFKTrqamirtnslLLS 262
Cdd:TIGR01271 1039 IMLRA----YFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFgRQ-------------SYFET----------LFH 1091
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 263 PLIDL-----FYALGTvmvLGIFGVRGLNGYVAAGVVYAFITYLNNFYNP------MTSMMDNLSDFQDGVVAG------ 325
Cdd:TIGR01271 1092 KALNLhtanwFLYLST---LRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEgevgiiLTLAMNILSTLQWAVNSSidvdgl 1168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 326 ----SRVLRVMDDPTIA--PAQHVDPTAKITRGKIEFRHVTFAY----------------DGQHPVLKDVSFVAEPGQTV 383
Cdd:TIGR01271 1169 mrsvSRVFKFIDLPQEEprPSGGGGKYQLSTVLVIENPHAQKCWpsggqmdvqgltakytEAGRAVLQDLSFSVEGGQRV 1248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 384 ALVGQTGSGKTSTINVLMRFYEFQsGEVLIDDRDIREYPAEELRQKMGLVLQEPFMFYGDINSNIRMFnDQISDEQVQAA 463
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPY-EQWSDEEIWKV 1326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 464 ARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTI 543
Cdd:TIGR01271 1327 AEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVI 1406
|
490 500 510
....*....|....*....|....*....|....*
gi 1027832812 544 AIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQ 578
Cdd:TIGR01271 1407 LSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
354-570 |
3.62e-24 |
|
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: 99.93 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYD-----GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLM--RFYEFQSGEVLIDDRDIREypaEEL 426
Cdd:cd03213 4 LSFRNLTVTVKsspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK---RSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 427 RQKMGLVLQEpFMFYGdiNSNIRmfndqisdEQVQAAARFvkaddfindlpenyqsRVIergasySSGQRQLISFARTIV 506
Cdd:cd03213 81 RKIIGYVPQD-DILHP--TLTVR--------ETLMFAAKL----------------RGL------SGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 507 TDPKILILDEATANVDTETEEMIQTGLDRI-QENRTTIAIAHRLST--IQNADLILVLNQGKIVERG 570
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
354-578 |
3.63e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHP----VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAE--ELR 427
Cdd:PRK13637 3 IKIENLTHIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 428 QKMGLVLQEP----F--MFYGDIN---SNIRMFNDQISdEQVQAAARFVKADdfindlPENYQSRvieRGASYSSGQRQL 498
Cdd:PRK13637 83 KKVGLVFQYPeyqlFeeTIEKDIAfgpINLGLSEEEIE-NRVKRAMNIVGLD------YEDYKDK---SPFELSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 499 ISFARTIVTDPKILILDEATANVDTETEEMIqtgLDRIQE-----NRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSN 572
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEI---LNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTP 229
|
....*.
gi 1027832812 573 DELLQQ 578
Cdd:PRK13637 230 REVFKE 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
354-576 |
4.26e-24 |
|
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: 101.70 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGqHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRfYEFQS--GEVLIDDRDIREYPAEELRQKMG 431
Cdd:COG1119 4 LELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPPTygNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LV---LQEPFM------------FYGdinsNIRMFNdQISDEQVQAAAR---FVKADDFINdlpenyqsrviERGASYSS 493
Cdd:COG1119 82 LVspaLQLRFPrdetvldvvlsgFFD----SIGLYR-EPTDEQRERARElleLLGLAHLAD-----------RPFGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 494 GQRQLISFARTIVTDPKILILDEATANVDTE-TEEMIQTgLDRI--QENRTTIAIAHRL----STIQNAdliLVLNQGKI 566
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGaRELLLAL-LDKLaaEGAPTLVLVTHHVeeipPGITHV---LLLKDGRV 221
|
250
....*....|
gi 1027832812 567 VERGSNDELL 576
Cdd:COG1119 222 VAAGPKEEVL 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
354-558 |
1.32e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 98.71 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGqHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREyPAEELRQKMGLV 433
Cdd:COG4133 3 LEAENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFM-----------FYGdinsniRMFNDQISDEQVQAAARFVKADDFInDLPenyqsrvierGASYSSGQRQLISFA 502
Cdd:COG4133 81 GHADGLkpeltvrenlrFWA------ALYGLRADREAIDEALEAVGLAGLA-DLP----------VRQLSAGQKRRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 503 RTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIA-HRLSTIQNADLI 558
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
354-567 |
2.04e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 97.11 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREY-PAEELRQKMGL 432
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEPFmfygdinsnirmfndqisdeqvqaaarfvkaddfindlpenyqsrviergasyssGQRQLISFARTIVTDPKIL 512
Cdd:cd03216 80 VYQLSV-------------------------------------------------------GERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 513 ILDEATANV-DTETEEMIQTgLDRIQEN-RTTIAIAHRLSTIQN-ADLILVLNQGKIV 567
Cdd:cd03216 105 ILDEPTAALtPAEVERLFKV-IRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
354-566 |
7.18e-23 |
|
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: 96.83 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDI--REYPAEELRQKMG 431
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQE----PFMfygDINSNIRMFNDQI---SDEQVQAAARF----VKADDFINDLPenyqsrviergASYSSGQRQLIS 500
Cdd:cd03262 80 MVFQQfnlfPHL---TVLENITLAPIKVkgmSKAEAEERALEllekVGLADKADAYP-----------AQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 501 FARTIVTDPKILILDEATANVDTET-EEMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKI 566
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELvGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
34-328 |
2.54e-22 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 97.52 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 34 FFIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVpvMWYFAGLYFFGMVVRALMQFVQN-----FSSTMGAEYMLE 108
Cdd:cd18570 3 LLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINL--LNIISIGLILLYLFQSLLSYIRSylllkLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 109 nvrrqMFAKLHRMGMRYFDQVPGGSILSRLtNDTMSFSNFWA-LFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFL 187
Cdd:cd18570 81 -----YFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISsTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 188 AVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQE----HRINGEFDHTNDAYFKTRQAMIRTNSlllsp 263
Cdd:cd18570 155 ILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEeqflKKIEKKFSKLLKKSFKLGKLSNLQSS----- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 264 LIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18570 230 IKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
38-328 |
4.51e-22 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. 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). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 96.46 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 38 AIVFSGLISVVNIYLPRVLQTFIDHYLKTGHatVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQMFAK 117
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGS--REAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 118 LHRMGMRYFDQVPGGSILSRLTNDTMSFSN-FWALFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIWYYQR 196
Cdd:cd18572 79 LLRQDIAFFDATKTGELTSRLTSDCQKVSDpLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 197 YSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFK--TRQAMIrtnSLLLSPLIDLFYALGTV 274
Cdd:cd18572 159 YYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKlsVRQALA---YAGYVAVNTLLQNGTQV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 275 MVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18572 236 LVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
354-575 |
5.84e-22 |
|
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: 95.10 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElRQkMGLV 433
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RN-VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMF-YGDINSNI-----------RMFNDQIsDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISF 501
Cdd:cd03296 80 FQHYALFrHMTVFDNVafglrvkprseRPPEAEI-RAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 502 ARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRLS-TIQNADLILVLNQGKIVERGSNDEL 575
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
73-575 |
7.80e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.82 E-value: 7.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 73 VMWYFAGLYFFGMVVRALMQfVQNFSSTMGAEYMLenvRRQMFAKLHRMGMRYFDQ----VPGGSILSRLTNDTMSFSNF 148
Cdd:PLN03232 339 VGYVYAFLIFFGVTFGVLCE-SQYFQNVGRVGFRL---RSTLVAAIFHKSLRLTHEarknFASGKVTNMITTDANALQQI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 149 WALFNTLFTAFFAVISSFVAMY--LTDAQI--ALWLLVFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGIS 224
Cdd:PLN03232 415 AEQLHGLWSAPFRIIVSMVLLYqqLGVASLfgSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKC 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 225 VIQQFRQEHRINGeFDHTNDAYFKTRQAMIRTNSLLLS--PLIDLFYALGTVMVLGifgvrglnGYVAAGVVYAFITYLN 302
Cdd:PLN03232 495 YAWEKSFESRIQG-IRNEELSWFRKAQLLSAFNSFILNsiPVVVTLVSFGVFVLLG--------GDLTPARAFTSLSLFA 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 303 NFYNPMTSMMDNLSDFQDGVVAGSRV--LRVMDDPTIAPAQHVDPTAKitrgKIEFRHVTFAYDGQ--HPVLKDVSFVAE 378
Cdd:PLN03232 566 VLRSPLNMLPNLLSQVVNANVSLQRIeeLLLSEERILAQNPPLQPGAP----AISIKNGYFSWDSKtsKPTLSDINLEIP 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 379 PGQTVALVGQTGSGKTSTINVLMrfyefqsGEVliddrdireYPAEE----LRQKMGLVLQEPFMFYGDINSNIrMFNDQ 454
Cdd:PLN03232 642 VGSLVAIVGGTGEGKTSLISAML-------GEL---------SHAETssvvIRGSVAYVPQVSWIFNATVRENI-LFGSD 704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 455 ISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTE-TEEMIQTGL 533
Cdd:PLN03232 705 FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCM 784
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1027832812 534 DRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDEL 575
Cdd:PLN03232 785 KDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
354-571 |
9.17e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.69 E-value: 9.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAY---DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTS---TINVLMRfyeFQSGEVLIDDRDIREYPAEEL- 426
Cdd:COG1135 2 IELENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 427 --RQKMGLVLQEpfmfygdinsnirmFN--------DQIsdeqvqA----AARFVKADdfIndlpenyQSRVIE------ 486
Cdd:COG1135 79 aaRRKIGMIFQH--------------FNllssrtvaENV------AlpleIAGVPKAE--I-------RKRVAEllelvg 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 487 ---RGASY----SSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIqeNR----TTIAIAHRLSTIQN- 554
Cdd:COG1135 130 lsdKADAYpsqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVRRi 207
|
250
....*....|....*..
gi 1027832812 555 ADLILVLNQGKIVERGS 571
Cdd:COG1135 208 CDRVAVLENGRIVEQGP 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
365-588 |
1.32e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 365 GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQsGEVLIDDRDIREYPAEEL---RQKMGLVLQEPfmfy 441
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 442 gdiNS--NIRMFNDQISDEQVQAAARFVKAddfindlpENYQSRVI----ERG----------ASYSSGQRQLISFARTI 505
Cdd:PRK15134 372 ---NSslNPRLNVLQIIEEGLRVHQPTLSA--------AQREQQVIavmeEVGldpetrhrypAEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 506 VTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQ--QHG 580
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAapQQE 520
|
....*...
gi 1027832812 581 YYYDMIQL 588
Cdd:PRK15134 521 YTRQLLAL 528
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
345-575 |
1.42e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.33 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 345 PTAKITRGKIEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ-----SGEVLIDDRDI- 418
Cdd:COG1117 3 APASTLEPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 419 -REYPAEELRQKMGLVLQEPFMFYGDINSNI-------RMFNDQISDEQVQAAARfvKADdfindLPENYQSRVIERGAS 490
Cdd:COG1117 82 dPDVDVVELRRRVGMVFQKPNPFPKSIYDNVayglrlhGIKSKSELDEIVEESLR--KAA-----LWDEVKDRLKKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 491 YSSGQRQLISFARTIVTDPKILILDEATANVD---TET-EEMiqtgldrIQE--NRTTIAI-------AHRLStiqnaDL 557
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpisTAKiEEL-------ILElkKDYTIVIvthnmqqAARVS-----DY 222
|
250
....*....|....*...
gi 1027832812 558 ILVLNQGKIVERGSNDEL 575
Cdd:COG1117 223 TAFFYLGELVEFGPTEQI 240
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
354-580 |
1.57e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.80 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAY-DGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGL 432
Cdd:PRK13647 5 IEVEDLHFRYkDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEP--FMFYGDINS-------NIRMFNDQIsDEQVQAAARFVKADDFINDLPENyqsrviergasYSSGQRQLISFAR 503
Cdd:PRK13647 84 VFQDPddQVFSSTVWDdvafgpvNMGLDKDEV-ERRVEEALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 504 TIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIA-HRLS-TIQNADLILVLNQGKIVERG-----SNDELL 576
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIV 231
|
....
gi 1027832812 577 QQHG 580
Cdd:PRK13647 232 EQAG 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-581 |
3.07e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.41 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIRE-------YPAEE- 425
Cdd:COG4152 2 LELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigYLPEEr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 426 -LRQKMGLVlqepfmfygdinsnirmfnDQI---------SDEQVQAAARFV--------KADDFINDLpenyqsrvier 487
Cdd:COG4152 81 gLYPKMKVG-------------------EQLvylarlkglSKAEAKRRADEWlerlglgdRANKKVEEL----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 488 gasySSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIaI--AHRLSTIQN-ADLILVLNQG 564
Cdd:COG4152 131 ----SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTV-IfsSHQMELVEElCDRIVIINKG 205
|
250
....*....|....*..
gi 1027832812 565 KIVERGSNDELLQQHGY 581
Cdd:COG4152 206 RKVLSGSVDEIRRQFGR 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-576 |
3.37e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 351 RGKIEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ-----SGEVLIDDRDIREYPAEE 425
Cdd:PRK14247 1 MNKIEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 426 LRQKMGLVLQEP-----FMFYGDINSNIRMFNDQISDEQVQAAARFV--KADdfindLPENYQSRVIERGASYSSGQRQL 498
Cdd:PRK14247 80 LRRRVQMVFQIPnpipnLSIFENVALGLKLNRLVKSKKELQERVRWAleKAQ-----LWDEVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 499 ISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAH------RLStiqnaDLILVLNQGKIVERGSN 572
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPT 229
|
....
gi 1027832812 573 DELL 576
Cdd:PRK14247 230 REVF 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
354-570 |
3.58e-21 |
|
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: 92.43 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYD---GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEeLRQKM 430
Cdd:cd03266 2 ITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVlqepfmfygdiNSNIRMFNDQISDEQVQAAARF--VKADDF---INDLPENYQSRVI--ERGASYSSGQRQLISFAR 503
Cdd:cd03266 81 GFV-----------SDSTGLYDRLTARENLEYFAGLygLKGDELtarLEELADRLGMEELldRRVGGFSTGMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 504 TIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIA-HRLSTIQN-ADLILVLNQGKIVERG 570
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
353-589 |
3.67e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.08 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 353 KIEFRHVTFAYDG----QHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDI----REYPAE 424
Cdd:PRK13646 2 TIRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 425 ELRQKMGLVLQEPfmfygdinsNIRMFNDQISDEQVQAAARF------VKADDFINDLPENYQSRVIERGA-SYSSGQRQ 497
Cdd:PRK13646 82 PVRKRIGMVFQFP---------ESQLFEDTVEREIIFGPKNFkmnldeVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 498 LISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQ--ENRTTIAIAHRLSTI-QNADLILVLNQGKIVERGSNDE 574
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKE 232
|
250 260
....*....|....*....|..
gi 1027832812 575 LLQQHGYYY-------DMIQLQ 589
Cdd:PRK13646 233 LFKDKKKLAdwhiglpEIVQLQ 254
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
352-575 |
8.64e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.98 E-value: 8.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 352 GKIEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElRqKMG 431
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-R-NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQE----PFMFYGDinsNI-------RMFNDQIsDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLIS 500
Cdd:COG3839 79 MVFQSyalyPHMTVYE---NIafplklrKVPKAEI-DRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 501 FARTIVTDPKILILDEATANVD------TETEemiqtgLDRIQE--NRTTIAIAHRLS---TIqnADLILVLNQGKIVER 569
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrveMRAE------IKRLHRrlGTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQV 215
|
....*.
gi 1027832812 570 GSNDEL 575
Cdd:COG3839 216 GTPEEL 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
36-300 |
1.22e-20 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 92.55 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 36 IAAIVFSgliSVVNIYLPRVLQTFIDHYLKTGHATVpVMWYFAGLYFFGMVVrALMQFVQNFSSTMGAEYMLENVRRQMF 115
Cdd:cd18575 2 LIALLIA---AAATLALGQGLRLLIDQGFAAGNTAL-LNRAFLLLLAVALVL-ALASALRFYLVSWLGERVVADLRKAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 116 AKLHRMGMRYFDQVPGGSILSRLTNDTM--------SFSNfwALFNTLFtaffaVISSFVAMYLTDAQIALWLLVFMPFL 187
Cdd:cd18575 77 AHLLRLSPSFFETTRTGEVLSRLTTDTTliqtvvgsSLSI--ALRNLLL-----LIGGLVMLFITSPKLTLLVLLVIPLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 188 AVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSLLLSPLIDL 267
Cdd:cd18575 150 VLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFL 229
|
250 260 270
....*....|....*....|....*....|....
gi 1027832812 268 -FYALGTVMVLGIFGVrgLNGYVAAGVVYAFITY 300
Cdd:cd18575 230 vFGAIVFVLWLGAHDV--LAGRMSAGELSQFVFY 261
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
356-576 |
5.56e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.23 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 356 FRHVTFAYDGQH-PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDD---------------RDIR 419
Cdd:PRK15112 14 FRYRTGWFRRQTvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqriRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 420 EYPAEEL--RQKMGLVLQEPFMFYGDINSNIRmfndqisDEQVQAAARFVKAddfindLPENyqsrviergASY-----S 492
Cdd:PRK15112 94 QDPSTSLnpRQRISQILDFPLRLNTDLEPEQR-------EKQIIETLRQVGL------LPDH---------ASYyphmlA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 493 SGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLSTIQN-ADLILVLNQGKIVER 569
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVER 231
|
....*..
gi 1027832812 570 GSNDELL 576
Cdd:PRK15112 232 GSTADVL 238
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
369-581 |
6.31e-20 |
|
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: 87.97 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 369 VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRF--YEFQSGEVLIDDRDIREYPAEElRQKMGLVL--QEPFMFYGdi 444
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGIFLafQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 445 nsnirmfndqisdeqvqaaarfVKADDFINDLPENyqsrviergasYSSGQRQLISFARTIVTDPKILILDEATANVDTE 524
Cdd:cd03217 92 ----------------------VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 525 TEEMIQTGLDRI-QENRTTIAIAH--RLSTIQNADLILVLNQGKIVERGSND--ELLQQHGY 581
Cdd:cd03217 139 ALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
132-582 |
1.03e-19 |
|
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: 93.86 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 132 GSILSRLTNDTMSFSNFWALFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMpFLAVTIWYYQRYSSRVYRRMRERLSE 211
Cdd:TIGR00957 415 GEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVM-VLMVPLNAVMAMKTKTYQVAHMKSKD 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 212 LNTKL-SEAITGISVIQQFRQEhringefdhtndAYFKTRQAMIRTNSLLLSPLIDLFYALGT-----------VMVLGI 279
Cdd:TIGR00957 494 NRIKLmNEILNGIKVLKLYAWE------------LAFLDKVEGIRQEELKVLKKSAYLHAVGTftwvctpflvaLITFAV 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 280 FGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRVLRVMDDPTIAPAQHVDPTAKITRG-KIEFRH 358
Cdd:TIGR00957 562 YVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGnSITVHN 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 359 VTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVliddrdireypaeELRQKMGLVLQEP 437
Cdd:TIGR00957 642 ATFTWaRDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQA 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 438 FMFYGDINSNIrMFNDQISDEQVQAAarfVKADDFINDL---PENYQSRVIERGASYSSGQRQLISFARTIVTDPKILIL 514
Cdd:TIGR00957 709 WIQNDSLRENI-LFGKALNEKYYQQV---LEACALLPDLeilPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLF 784
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 515 DEATANVDTETEEMI---QTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQHGYY 582
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIfehVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
358-581 |
1.06e-19 |
|
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: 92.83 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 358 HVTFA-YDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRF----YEFQSGEVLIDDRDIREYPAEELRQ---- 428
Cdd:COG4172 13 SVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 429 KMGLVLQEPfmfygdinsnirM--FN------DQISdEQVQ-------AAARfvkaddfindlpenyqSRVIE------- 486
Cdd:COG4172 93 RIAMIFQEP------------MtsLNplhtigKQIA-EVLRlhrglsgAAAR----------------ARALEllervgi 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 487 -----RGASY----SSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTT--IAIAHRLSTIQN- 554
Cdd:COG4172 144 pdperRLDAYphqlSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMalLLITHDLGVVRRf 223
|
250 260
....*....|....*....|....*....
gi 1027832812 555 ADLILVLNQGKIVERGSNDELLQ--QHGY 581
Cdd:COG4172 224 ADRVAVMRQGEIVEQGPTAELFAapQHPY 252
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
354-577 |
1.64e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.84 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKtST----INVLMrfyEFQSGEVLIDDRDIREYPAEE--LR 427
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGK-STllrcINKLE---EITSGDLIVDGLKVNDPKVDErlIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 428 QKMGLVLQEpfmFYgdinsnirMFNDQISDEQVQAAARFV----KADdfINDLPENYQSRV--IERGASY----SSGQRQ 497
Cdd:PRK09493 77 QEAGMVFQQ---FY--------LFPHLTALENVMFGPLRVrgasKEE--AEKQARELLAKVglAERAHHYpselSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 498 LISFARTIVTDPKILILDEATANVDTE-TEEMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDEL 575
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVL 223
|
..
gi 1027832812 576 LQ 577
Cdd:PRK09493 224 IK 225
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
33-304 |
3.92e-19 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 87.94 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 33 CFFIAAIVFSGLISVVNIYLprvlQTFIDHYLKTGHATVP--VMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLenv 110
Cdd:cd18580 3 LLLLLLLLLAFLSQFSNIWL----DWWSSDWSSSPNSSSGyyLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLH--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 111 rRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNF--WALFNTLFTaFFAVISSFVAMyltdAQIALWLLVFMPFLA 188
Cdd:cd18580 76 -DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEElpLALLDFLQS-LFSVLGSLIVI----AIVSPYFLIVLPPLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 189 VTIWYYQRYSSRVYRRMReRL-----SELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNS-LLLS 262
Cdd:cd18580 150 VVYYLLQRYYLRTSRQLR-RLesesrSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRwLGLR 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1027832812 263 plIDLFYAL--GTVMVLGIFGVRGLN-GYVAAGVVYA--FITYLNNF 304
Cdd:cd18580 229 --LDLLGALlaLVVALLAVLLRSSISaGLVGLALTYAlsLTGSLQWL 273
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
354-579 |
4.16e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 86.73 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpvlKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEE-------- 425
Cdd:COG3840 2 LRLDDLTYRYGDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpvsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 426 ---------LRQKMGLvlqepfmfyGdINSNIRMFNDQIsdEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQR 496
Cdd:COG3840 79 ennlfphltVAQNIGL---------G-LRPGLKLTAEQR--AQVEQALERVGLAGLLDRLP-----------GQLSGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 497 QLISFARTIVTDPKILILDEATANVDTE-TEEMIQTgLDRIQENR--TTIAIAHRLSTIQN-ADLILVLNQGKIVERGSN 572
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDPAlRQEMLDL-VDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPT 214
|
....*..
gi 1027832812 573 DELLQQH 579
Cdd:COG3840 215 AALLDGE 221
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
38-282 |
5.48e-19 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 88.28 E-value: 5.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 38 AIVFSGLISVVNIYLPRVLQTFIDHYlktghatvpvmwyfaGLYFFGM-VVRALMQFVQNFSSTMGAEYMLENVRRQMFA 116
Cdd:cd18578 29 AILFSKLISVFSLPDDDELRSEANFW---------------ALMFLVLaIVAGIAYFLQGYLFGIAGERLTRRLRKLAFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 117 KLHRMGMRYFDQvPG---GSILSRLTNDTMSFSNFWALF-NTLFTAFFAVISSFV-AMYLtDAQIALWLLVFMPFLAVTI 191
Cdd:cd18578 94 AILRQDIAWFDD-PEnstGALTSRLSTDASDVRGLVGDRlGLILQAIVTLVAGLIiAFVY-GWKLALVGLATVPLLLLAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 192 WYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFK--TRQAMIRTnslllsplidLFY 269
Cdd:cd18578 172 YLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKkgLRRALISG----------LGF 241
|
250
....*....|...
gi 1027832812 270 ALGTVMVLGIFGV 282
Cdd:cd18578 242 GLSQSLTFFAYAL 254
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
361-581 |
9.61e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 87.71 E-value: 9.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 361 FAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKtSTINVLMRFYEF-QSGEVLIDDRDIREYPAEE---LRQKMGLVLQE 436
Cdd:PRK11308 22 FKPERLVKALDGVSFTLERGKTLAVVGESGCGK-STLARLLTMIETpTGGELYYQGQDLLKADPEAqklLRQKIQIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 437 PfmfYGDINSniRMFNDQISDE------QVQAAARFVKADDFINDL---PENYQSrviergasY----SSGQRQLISFAR 503
Cdd:PRK11308 101 P---YGSLNP--RKKVGQILEEpllintSLSAAERREKALAMMAKVglrPEHYDR--------YphmfSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 504 TIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTT--IAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQ--Q 578
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNnpR 247
|
...
gi 1027832812 579 HGY 581
Cdd:PRK11308 248 HPY 250
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
354-576 |
1.07e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.69 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPV--LKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMG 431
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQEP-FMFYG---DINSNIRMFNDQISDEQ----VQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFAR 503
Cdd:PRK13642 85 MVFQNPdNQFVGatvEDDVAFGMENQGIPREEmikrVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 504 TIVTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELL 576
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
368-575 |
2.32e-18 |
|
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: 89.58 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 368 PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMrfyefqsGEVLIDDRDIREypaeelRQKMGLVLQEPFMFYGDINSN 447
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM-------GELEPSEGKIKH------SGRISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 448 IrMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETE- 526
Cdd:TIGR01271 507 I-IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEk 585
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1027832812 527 EMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDEL 575
Cdd:TIGR01271 586 EIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
365-577 |
2.96e-18 |
|
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: 84.13 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 365 GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElRQKMGLVL--QEPFMFYG 442
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGYlpQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 443 -DINSNIRMFNDQISDEQvqaAARFVKADDFINDLpeNYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANV 521
Cdd:cd03218 90 lTVEENILAVLEIRGLSK---KEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 522 D----TETEEMIQTGLDR-----IQEN--RTTIAIAHRlstiqnadlILVLNQGKIVERGSNDELLQ 577
Cdd:cd03218 165 DpiavQDIQKIIKILKDRgigvlITDHnvRETLSITDR---------AYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
354-561 |
4.86e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.22 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLV 433
Cdd:PRK10247 8 LQLQNVGYLAGDA-KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMFYGDINSNIrMFNDQISDEQVQAAARFVKADDFinDLPENYQSRVIErgaSYSSGQRQLISFARTIVTDPKILI 513
Cdd:PRK10247 87 AQTPTLFGDTVYDNL-IFPWQIRNQQPDPAIFLDDLERF--ALPDTILTKNIA---ELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 514 LDEATANVD----TETEEMIqTGLDRiQENRTTIAIAHRLSTIQNADLILVL 561
Cdd:PRK10247 161 LDEITSALDesnkHNVNEII-HRYVR-EQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
354-579 |
5.30e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.50 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPV----LKDVSFVAEPGQTVALVGQTGSGKTStinvLMRFYEF----QSGEVLIDDRDIREYPA-- 423
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKST----LMQHFNAllkpSSGTITIAGYHITPETGnk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 424 --EELRQKMGLVLQ--EPFMFYGDINSNIrMF---NDQISDEQVQAAA-RFVK----ADDFINDLPenyqsrviergASY 491
Cdd:PRK13641 79 nlKKLRKKVSLVFQfpEAQLFENTVLKDV-EFgpkNFGFSEDEAKEKAlKWLKkvglSEDLISKSP-----------FEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 492 SSGQRQLISFARTIVTDPKILILDEATANVDTET-EEMIQTGLDRIQENRTTIAIAHRLSTI-QNADLILVLNQGKIVER 569
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKH 226
|
250
....*....|....*.
gi 1027832812 570 GS------NDELLQQH 579
Cdd:PRK13641 227 ASpkeifsDKEWLKKH 242
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
338-564 |
8.36e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.78 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 338 APAQHVDPTAKITR---GKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTStinvLMR----FYEFQSGE 410
Cdd:COG4178 344 AADALPEAASRIETsedGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKST----LLRaiagLWPYGSGR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 411 VliddrdirEYPAEElrqKMGLVLQEPFMFYGDI-------NSNirmfnDQISDEQVQAAARFVKADDFINDLPENYQ-S 482
Cdd:COG4178 420 I--------ARPAGA---RVLFLPQRPYLPLGTLreallypATA-----EAFSDAELREALEAVGLGHLAERLDEEADwD 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 483 RVIergasySSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLN 562
Cdd:COG4178 484 QVL------SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELT 557
|
..
gi 1027832812 563 QG 564
Cdd:COG4178 558 GD 559
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
354-576 |
1.27e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.11 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPA-EELRQKMGL 432
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEP-FMFYG-DINSNIRMFNDQISDEQVQAAARFVKADDFINdlPENYQSRVIErgaSYSSGQRQLISFARTIVTDPK 510
Cdd:PRK13644 82 VFQNPeTQFVGrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIG--LEKYRHRSPK---TLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 511 ILILDEATANVDTETEEMIQTGLDRIQEN-RTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELL 576
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
59-575 |
1.28e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 87.10 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 59 FIDHYLKTGHATVPVM--WYFAGLYFFGMVVRALMQfVQNFSSTMGAEYMLenvRRQMFAKLHRMGMRYFD----QVPGG 132
Cdd:PLN03130 323 LLNLLLESMQNGEPAWigYIYAFSIFVGVVLGVLCE-AQYFQNVMRVGFRL---RSTLVAAVFRKSLRLTHegrkKFTSG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 133 SILSRLTNDTMSFSNFWALFNTLFTAFFAVISSFVAMY--LTDAQI--ALWLLVFMPFLAVTIWYYQRYSSRVYRRMRER 208
Cdd:PLN03130 399 KITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYqqLGVASLigSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 209 LSELNtklsEAITGISVIQQFRQEHRINGEFDHTND---AYFKTRQAMIRTNSLLLSPLIdlfyALGTVMVLGIFGVRGL 285
Cdd:PLN03130 479 IGLMN----EVLAAMDTVKCYAWENSFQSKVQTVRDdelSWFRKAQLLSAFNSFILNSIP----VLVTVVSFGVFTLLGG 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 286 NGYVAAGV----VYAFITY-LNNFYNPMTSMMD---NLSDFQDGVVAGSRVLrvMDDPTIAPAQhvdPTAKITRGkiefr 357
Cdd:PLN03130 551 DLTPARAFtslsLFAVLRFpLFMLPNLITQAVNanvSLKRLEELLLAEERVL--LPNPPLEPGL---PAISIKNG----- 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 358 hvTFAYD--GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTIN-VLMRFYEFQSGEVLIddrdireypaeelRQKMGLVL 434
Cdd:PLN03130 621 --YFSWDskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI-------------RGTVAYVP 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 435 QEPFMFYGDINSNIrMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILIL 514
Cdd:PLN03130 686 QVSWIFNATVRDNI-LFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 515 DEATANVDTET-EEMIQTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDEL 575
Cdd:PLN03130 765 DDPLSALDAHVgRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
354-562 |
1.53e-17 |
|
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: 80.28 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVliddrdirEYPAEElrqKMGLV 433
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGE---DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMFYGdinsNIRmfnDQISdeqvqaaarfvkaddfindlpenYQ-SRVIergasySSGQRQLISFARTIVTDPKIL 512
Cdd:cd03223 70 PQRPYLPLG----TLR---EQLI-----------------------YPwDDVL------SGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 513 ILDEATANVDTETEEMIqtgLDRIQENRTT-IAIAHRLSTIQNADLILVLN 562
Cdd:cd03223 114 FLDEATSALDEESEDRL---YQLLKELGITvISVGHRPSLWKFHDRVLDLD 161
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
354-577 |
1.78e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHP----VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDI----REYPAEE 425
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 426 LRQKMGLVLQ--EPFMFYGDINSNIRM--FNDQISDEQVQAAARfvKADDFINdLPENYQSRviergaS---YSSGQRQL 498
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFgpMNFGVSEEDAKQKAR--EMIELVG-LPEELLAR------SpfeLSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 499 ISFARTIVTDPKILILDEATANVD----TETEEMIQTgLDRiQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSND 573
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDpkgrKEMMEMFYK-LHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....
gi 1027832812 574 ELLQ 577
Cdd:PRK13634 232 EIFA 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
354-578 |
2.57e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 83.66 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREY-PAEELRqkMGL 432
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRERR--VGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQE----PFMFYGDinsNI------RMFNDQISDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFA 502
Cdd:COG1118 80 VFQHyalfPHMTVAE---NIafglrvRPPSKAEIRARVEELLELVQLEGLADRYP-----------SQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 503 RTIVTDPKILILDEATANVDTET-----EEMIQTgLDRIQenRTTIAIAH------RLstiqnADLILVLNQGKIVERGS 571
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVrkelrRWLRRL-HDELG--GTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGT 217
|
....*..
gi 1027832812 572 NDELLQQ 578
Cdd:COG1118 218 PDEVYDR 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
370-576 |
2.93e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.31 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 370 LKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQ----KMGLVLQE----PFMFY 441
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSfalmPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 442 GDINSnirmFNDQISDeqVQAAARFVKADDFINDLP-ENYQSRVIERgasYSSGQRQLISFARTIVTDPKILILDEATAN 520
Cdd:PRK10070 124 LDNTA----FGMELAG--INAEERREKALDALRQVGlENYAHSYPDE---LSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 521 VDTETEEMIQTGLDRIQ--ENRTTIAIAHRL-STIQNADLILVLNQGKIVERGSNDELL 576
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
354-575 |
3.53e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.68 E-value: 3.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKtST-INVLMRFYEFQSGEVLIDDRDIR-EYPAEELRQKMG 431
Cdd:COG1129 5 LEMRGISKSFGGVK-ALDGVSLELRPGEVHALLGENGAGK-STlMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAAGIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQE----PFM------FYGDINSNIRMFNDQisdEQVQAAARFVkaDDFinDLPENYQSRViergASYSSGQRQLISF 501
Cdd:COG1129 83 IIHQElnlvPNLsvaeniFLGREPRRGGLIDWR---AMRRRARELL--ARL--GLDIDPDTPV----GDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 502 ARTIVTDPKILILDEATAN-VDTETEEMiqtgLDRI----QENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDEL 575
Cdd:COG1129 152 ARALSRDARVLILDEPTASlTEREVERL----FRIIrrlkAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
354-578 |
4.85e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.36 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLV 433
Cdd:PRK13548 3 LEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEP---FMFygDINSNIRM------FNDQISDEQVQAAARFVKADDFindlpenyqsrvieRGASY---SSGQRQLISF 501
Cdd:PRK13548 82 PQHSslsFPF--TVEEVVAMgraphgLSRAEDDALVAAALAQVDLAHL--------------AGRDYpqlSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 502 ARTIV------TDPKILILDEATANVDteteemI--QTGLDRI------QENRTTIAIAHRLS-TIQNADLILVLNQGKI 566
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALD------LahQHHVLRLarqlahERGLAVIVVLHDLNlAARYADRIVLLHQGRL 219
|
250
....*....|..
gi 1027832812 567 VERGSNDELLQQ 578
Cdd:PRK13548 220 VADGTPAEVLTP 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
356-568 |
5.07e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.27 E-value: 5.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 356 FRHVTFAYDGQHP-VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEE---LRQKMG 431
Cdd:PRK10419 13 YAHGGLSGKHQHQtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQEPFmfyGDIN--SNIRmfndQISDE------QVQAAARFVKADDFIN--DLPENYQSRvieRGASYSSGQRQLISF 501
Cdd:PRK10419 93 MVFQDSI---SAVNprKTVR----EIIREplrhllSLDKAERLARASEMLRavDLDDSVLDK---RPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 502 ARTIVTDPKILILDEATANVDTeteeMIQTG----LDRIQENRTT--IAIAHRLSTIQN-ADLILVLNQGKIVE 568
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDL----VLQAGvirlLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
352-578 |
5.55e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.59 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 352 GKIEFRHVTFAYDGQHP----VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDD-------RDIRE 420
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 421 ypAEELRQKMGLVLQEP--FMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINdLPENYQSRvieRGASYSSGQRQL 498
Cdd:PRK13645 85 --VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDYVKR---SPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 499 ISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQEN--RTTIAIAHRLSTI-QNADLILVLNQGKIVERG----- 570
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfei 238
|
....*....
gi 1027832812 571 -SNDELLQQ 578
Cdd:PRK13645 239 fSNQELLTK 247
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
354-570 |
5.96e-17 |
|
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: 79.84 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFvaEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElrQKMGLV 433
Cdd:cd03298 1 VRLDKIRFSY-GEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMF-YGDINSNI------RMFNDQISDEQVQAAARFVKADDFINDLPEnyqsrviergaSYSSGQRQLISFARTIV 506
Cdd:cd03298 76 FQENNLFaHLTVEQNVglglspGLKLTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 507 TDPKILILDEATANVD-TETEEMIQTGLDRIQENR-TTIAIAHRLSTIQN-ADLILVLNQGKIVERG 570
Cdd:cd03298 145 RDKPVLLLDEPFAALDpALRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
346-575 |
6.64e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.96 E-value: 6.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 346 TAKITRGKIEFRHVTFAYDGQHPVlKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAee 425
Cdd:PRK11607 12 TRKALTPLLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 426 LRQKMGLVLQEPFMF-YGDINSNI-------RMFNDQISDeQVQAAARFVKADDFINDLPENYqsrviergasySSGQRQ 497
Cdd:PRK11607 89 YQRPINMMFQSYALFpHMTVEQNIafglkqdKLPKAEIAS-RVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 498 LISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAH-RLSTIQNADLILVLNQGKIVERGSNDE 574
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
.
gi 1027832812 575 L 575
Cdd:PRK11607 237 I 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
362-577 |
8.33e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.32 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 362 AYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPA-EELRQKMGLVLQEPFMF 440
Cdd:PRK10895 12 AYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 441 -----YGDINSNIRMFNDqISDEQVQAAARFVKADDFINDLPENYqsrvierGASYSSGQRQLISFARTIVTDPKILILD 515
Cdd:PRK10895 91 rrlsvYDNLMAVLQIRDD-LSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 516 EATANVDTETEEMIQTGLDRIQENRTTIAIA-HRL-STIQNADLILVLNQGKIVERGSNDELLQ 577
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
35-328 |
8.70e-17 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 81.37 E-value: 8.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTG------HATVPVMWYFAGLyFFGMVVralMQFVQNFSSTMGAEYMLE 108
Cdd:cd18577 5 LLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESspdeflDDVNKYALYFVYL-GIGSFV---LSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 109 NVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDT----MSFSNfwaLFNTLFTAFFAVISSF-VAMYlTDAQIALWLLVF 183
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTnliqDGIGE---KLGLLIQSLSTFIAGFiIAFI-YSWKLTLVLLAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 184 MPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDayfKTRQAMIR---TNSLL 260
Cdd:cd18577 157 LPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE---KARKAGIKkglVSGLG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027832812 261 LSP---LIDLFYAL----GTVMVlgifgvrgLNGYVAAGVVY-AFITYLNNFYNpMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18577 234 LGLlffIIFAMYALafwyGSRLV--------RDGEISPGDVLtVFFAVLIGAFS-LGQIAPNLQAFAKARAAAAKI 300
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
354-578 |
1.08e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.51 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIReYPAEEL---RQKM 430
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEP--FMF---------YGDINSNIRMfnDQIsDEQVQAAARFVKADDFINDLPENyqsrviergasYSSGQRQLI 499
Cdd:PRK13639 81 GIVFQNPddQLFaptveedvaFGPLNLGLSK--EEV-EKRVKEALKAVGMEGFENKPPHH-----------LSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 500 SFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIA-HRLSTIQ-NADLILVLNQGKIVERGSNDELLQ 577
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFS 226
|
.
gi 1027832812 578 Q 578
Cdd:PRK13639 227 D 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
354-576 |
1.29e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.66 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAY-DGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIrEYPAE---ELRQK 429
Cdd:PRK13636 6 LKVEELNYNYsDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 430 MGLVLQEP--FMFYGDINSNIRM--FNDQISDEQVQAAARFVKADDFINDLPEnyqsrviERGASYSSGQRQLISFARTI 505
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFgaVNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 506 VTDPKILILDEATANVDTE-TEEMIQTGLDRIQENRTTIAIA-HRLSTIQ-NADLILVLNQGKIVERGSNDELL 576
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMgVSEIMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
354-575 |
1.42e-16 |
|
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: 78.95 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVlKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAeELRQKMGLV 433
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFM---FYGDINSNI--RMFN--DQISDEQVQAAARFVKADDFINdlpenyqsrviERGASYSSGQRQLISFARTIV 506
Cdd:cd03265 79 FQDLSVddeLTGWENLYIhaRLYGvpGAERRERIDELLDFVGLLEAAD-----------RLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 507 TDPKILILDEATANVDTETEEMIQTGLDRIQ-ENRTTIAI-AHRLSTI-QNADLILVLNQGKIVERGSNDEL 575
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeEFGMTILLtTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-576 |
1.72e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.14 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 358 HVTFAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRF------YEFqSGEVLIDDRDIREY-PAEELRQKM 430
Cdd:PRK14271 26 NLTLGFAGK-TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRY-SGDVLLGGRSIFNYrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEPFMFYGDINSNIRM---FNDQISDEQVQ--AAARFVKADdfindLPENYQSRVIERGASYSSGQRQLISFARTI 505
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVLAgvrAHKLVPRKEFRgvAQARLTEVG-----LWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 506 VTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELL 576
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
361-564 |
1.86e-16 |
|
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: 78.53 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 361 FAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQK----MGLVLQE 436
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 437 PFMFYGDINSNIrMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDE 516
Cdd:cd03290 88 PWLLNATVEENI-TFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 517 ATANVDTE-TEEMIQTG-LDRIQEN-RTTIAIAHRLSTIQNADLILVLNQG 564
Cdd:cd03290 167 PFSALDIHlSDHLMQEGiLKFLQDDkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
78-328 |
1.92e-16 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 80.16 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 78 AGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTND--------TMSFSNFW 149
Cdd:cd18554 49 GIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDveqtkdfiTTGLMNIW 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 150 ALFNTLFTAFfavissfVAMYLTDAQIALWLLVFMPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQF 229
Cdd:cd18554 129 LDMITIIIAI-------CIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 230 RQEHRINGEFDHTNDAYFKTRQAMIRTNSLLLSpLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMT 309
Cdd:cd18554 202 ALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFS-AVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLR 280
|
250
....*....|....*....
gi 1027832812 310 SMMDNLSDFQDGVVAGSRV 328
Cdd:cd18554 281 RLVNSFTTLTQSFASMDRV 299
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
354-571 |
1.97e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.00 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDG---QHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEEL---R 427
Cdd:PRK11153 2 IELKNISKVFPQggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 428 QKMGLVLQEpfmfygdinsnirmFNdqisdeqvQAAARFVkaddFIN-DLP--------ENYQSRVIE---------RGA 489
Cdd:PRK11153 82 RQIGMIFQH--------------FN--------LLSSRTV----FDNvALPlelagtpkAEIKARVTEllelvglsdKAD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 490 SY----SSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIqeNR----TTIAIAHRLSTI-QNADLILV 560
Cdd:PRK11153 136 RYpaqlSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRelglTIVLITHEMDVVkRICDRVAV 213
|
250
....*....|.
gi 1027832812 561 LNQGKIVERGS 571
Cdd:PRK11153 214 IDAGRLVEQGT 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
368-578 |
2.22e-16 |
|
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: 79.90 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 368 PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRdireypaeelrqkMGLVLQEPFMFYGDINSN 447
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 448 IrMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEE 527
Cdd:cd03291 118 I-IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 528 MI-QTGLDRIQENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQQ 578
Cdd:cd03291 197 EIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
353-576 |
2.95e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.74 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 353 KIEFRHVTFAYDGQHP----VLKDVSFVAEPGQTVALVGQTGSGKTSTI---NVLM---------------------RFY 404
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIehlNALLlpdtgtiewifkdeknkkktkEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 405 EFQSGEVLIDDRDIREYPAEELRQKMGLVLQ--EPFMFYGDINSNIrMFNdQIS-----DEQVQAAARFVKaddfINDLP 477
Cdd:PRK13651 82 KVLEKLVIQKTRFKKIKKIKEIRRRVGVVFQfaEYQLFEQTIEKDI-IFG-PVSmgvskEEAKKRAAKYIE----LVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 478 ENYqsrvIERGA-SYSSGQRQLISFARTIVTDPKILILDEATANVDTE-TEEMIQTgLDRI-QENRTTIAIAHRL-STIQ 553
Cdd:PRK13651 156 ESY----LQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEI-FDNLnKQGKTIILVTHDLdNVLE 230
|
250 260
....*....|....*....|...
gi 1027832812 554 NADLILVLNQGKIVERGSNDELL 576
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
358-569 |
3.18e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.59 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 358 HVTFAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElrqkmGLVLQ-E 436
Cdd:PRK11248 6 HLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQnE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 437 PFMFYGDINSNIrMFNDQISDeqVQAAARFVKADDFIN--DLpENYQSRVIERgasYSSGQRQLISFARTIVTDPKILIL 514
Cdd:PRK11248 80 GLLPWRNVQDNV-AFGLQLAG--VEKMQRLEIAHQMLKkvGL-EGAEKRYIWQ---LSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 515 DEATANVDTETEEMIQTGLDRI--QENRTTIAIAHrlsTIQNA-----DLILVL-NQGKIVER 569
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLwqETGKQVLLITH---DIEEAvfmatELVLLSpGPGRVVER 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
354-578 |
3.48e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.08 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLV 433
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEP----F-------MFYGDINSNIrmfNDQISDEQVQAAARFVKADDFINDLPENyqsrviergasYSSGQRQLISFA 502
Cdd:PRK13652 84 FQNPddqiFsptveqdIAFGPINLGL---DEETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 503 RTIVTDPKILILDEATANVDTETEEMIQTGLDRIQEN--RTTIAIAHRLSTI-QNADLILVLNQGKIVERGSNDELLQQ 578
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
353-579 |
4.19e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.52 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 353 KIEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGL 432
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEPFM-------------------FYGDINSNIRMFNDQiSDEQVQAAARfvkADDFINDLpenyqsrviergasySS 493
Cdd:PRK11231 81 LPQHHLTpegitvrelvaygrspwlsLWGRLSAEDNARVNQ-AMEQTRINHL---ADRRLTDL---------------SG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 494 GQRQLISFARTIVTDPKILILDEATANVDT--ETEEMiqtGLDRI--QENRTTIAIAHRLS-TIQNADLILVLNQGKIVE 568
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDInhQVELM---RLMRElnTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMA 218
|
250
....*....|.
gi 1027832812 569 RGSNDELLQQH 579
Cdd:PRK11231 219 QGTPEEVMTPG 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
354-578 |
5.11e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.59 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAY-----DGQHPVLKDVSFVAEPGQTVALVGQTGSGKtSTI----NVLMRFYEfqsGEVLIDDRDIR-EYPA 423
Cdd:PRK13633 5 IKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGK-STIakhmNALLIPSE---GKVYVDGLDTSdEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 424 EELRQKMGLVLQEPfmfygdinsnirmfndqisDEQVQAAarFVKAD-----DFINDLPENYQSRVIE-----------R 487
Cdd:PRK13633 81 WDIRNKAGMVFQNP-------------------DNQIVAT--IVEEDvafgpENLGIPPEEIRERVDEslkkvgmyeyrR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 488 GASY--SSGQRQLISFARTIVTDPKILILDEATANVD-TETEEMIQTGLDRIQE-NRTTIAIAHRLSTIQNADLILVLNQ 563
Cdd:PRK13633 140 HAPHllSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDS 219
|
250
....*....|....*
gi 1027832812 564 GKIVERGSNDELLQQ 578
Cdd:PRK13633 220 GKVVMEGTPKEIFKE 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
354-576 |
5.63e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.87 E-value: 5.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTS---TINVLMR--FYEFQSGEVLID-DRDIREYPA--EE 425
Cdd:PRK11264 4 IEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQpeAGTIRVGDITIDtARSLSQQKGliRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 426 LRQKMGLVLQEPFMF-YGDINSNI---RMFNDQISDEQVQAAARFVKADDFINDLPENYQSRViergasySSGQRQLISF 501
Cdd:PRK11264 83 LRQHVGFVFQNFNLFpHRTVLENIiegPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRL-------SGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 502 ARTIVTDPKILILDEATANVDTE-TEEMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELL 576
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPElVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
354-571 |
6.87e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.61 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGqHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElRQkMGLV 433
Cdd:PRK09452 15 VELRGISKSFDG-KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH-VNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQE----PFM-FYGDINSNIRMF---NDQIsDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFARTI 505
Cdd:PRK09452 92 FQSyalfPHMtVFENVAFGLRMQktpAAEI-TPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 506 VTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAH-RLSTIQNADLILVLNQGKIVERGS 571
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
300-578 |
7.38e-16 |
|
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: 80.64 E-value: 7.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 300 YLNNFYNPMTSMMDNLSDFQDGVVAGSRVLRVMDDPTIApAQHVD-------PTAKITRGK--IEFRHVTfAYDGQHPVL 370
Cdd:TIGR02633 196 YISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDII-TMMVGreitslyPHEPHEIGDviLEARNLT-CWDVINPHR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 371 K---DVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ-SGEVLIDDR--DIREyPAEELRQKMGLVLQE-------P 437
Cdd:TIGR02633 274 KrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRN-PAQAIRAGIAMVPEDrkrhgivP 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 438 FMFYGDiNSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGaSYSSGQRQLISFARTIVTDPKILILDEA 517
Cdd:TIGR02633 353 ILGVGK-NITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 518 TANVDTETEEMIQTGLDRI-QENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQQ 578
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHALTQE 493
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
370-582 |
9.33e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.48 E-value: 9.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 370 LKDVSFVAEPGQTVALVGQTGSGKTSTINVLMrFYEFQ----SGEVLIDDRDIReypAEELRQKMGLVLQEPfMFYGD-- 443
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPID---AKEMRAISAYVQQDD-LFIPTlt 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 444 ------INSNIRMFNDQISDEQVQAaarfvkADDFINDLP-ENYQSRVI---ERGASYSSGQRQLISFARTIVTDPKILI 513
Cdd:TIGR00955 116 vrehlmFQAHLRMPRRVTKKEKRER------VDEVLQALGlRKCANTRIgvpGRVKGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 514 LDEATANVD-TETEEMIQTGLDRIQENRTTIAIAHRLST--IQNADLILVLNQGKIVERGSNDELLQ---QHGYY 582
Cdd:TIGR00955 190 CDEPTSGLDsFMAYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVPffsDLGHP 264
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-576 |
1.18e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.01 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 361 FAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQS------GEVLIDDRDIREYPAEELRQKMGLVL 434
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 435 QEPFMF-YGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILI 513
Cdd:PRK14246 97 QQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 514 LDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELL 576
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
319-581 |
1.43e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.90 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 319 QDGVVAGSRVLRVMDDPTIAPaqhvdptakiTRGKIeFRHVTFAYdgqHPVlKDVSFVAEPGQTVALVGQTGSGKTSTIN 398
Cdd:PRK10261 304 QDTVVDGEPILQVRNLVTRFP----------LRSGL-LNRVTREV---HAV-EKVSFDLWPGETLSLVGESGSGKSTTGR 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 399 VLMRFYEFQSGEVLIDDRDIREYPA---EELRQKMGLVLQEPF------MFYGD-INSNIRMFNDQISDEqvqAAARFVK 468
Cdd:PRK10261 369 ALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYasldprQTVGDsIMEPLRVHGLLPGKA---AAARVAW 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 469 ADDFINDLPENYQSRVIErgasYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIA 546
Cdd:PRK10261 446 LLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFIS 521
|
250 260 270
....*....|....*....|....*....|....*...
gi 1027832812 547 HRLSTIQN-ADLILVLNQGKIVERGSNDELLQ--QHGY 581
Cdd:PRK10261 522 HDMAVVERiSHRVAVMYLGQIVEIGPRRAVFEnpQHPY 559
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
369-588 |
1.84e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 369 VLKDVSFVAEPGQTVALVGQTGSGKTSTI---NVLM--RFYEFQSGEVLIDDRDIREYP-----------AEELRQKMGL 432
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVthfNGLIksKYGTIQVGDIYIGDKKNNHELitnpyskkiknFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQEP--FMFYGDINSNIrMF---NDQISDEQVQAAARFvkaddFINDLPENYQsrVIERGA-SYSSGQRQLISFARTIV 506
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDI-MFgpvALGVKKSEAKKLAKF-----YLNKMGLDDS--YLERSPfGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 507 TDPKILILDEATANVDTETE-EMIQTGLDRIQENRTTIAIAHRLSTI-QNADLILVLNQGKIVERGSNDEL-LQQHGYYY 583
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIfTDQHIINS 272
|
....*
gi 1027832812 584 DMIQL 588
Cdd:PRK13631 273 TSIQV 277
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
363-577 |
1.91e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.42 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 363 YDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ-----SGEVLIDDRDI--REYPAEELRQKMGLVLQ 435
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 436 EPFMF-----YGDINSNIRMFN--------DQISDEQVQAAARFVKADDFINDLPENYqsrviergasySSGQRQLISFA 502
Cdd:PRK14267 93 YPNPFphltiYDNVAIGVKLNGlvkskkelDERVEWALKKAALWDEVKDRLNDYPSNL-----------SGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 503 RTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHrlSTIQNA---DLILVLNQGKIVERGSNDELLQ 577
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
38-328 |
2.01e-15 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. 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.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 77.17 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 38 AIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYFAGLYFFGM---VVRALMQFVQNFSSTMGAEYMLENVRRQM 114
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLgvfVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 FAKLHRMGMRYFDQVPGGSILSRLTND--------TMSFSNFwalfntlFTAFFAVISSFVAMYLTDAQIALWLLVFMPF 186
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDtsvvgkslTQNLSDG-------LRSLVSGVGGIGMMLYISPKLTLVMLLVVPP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 187 LAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSLLLSplid 266
Cdd:cd18573 154 IAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFG---- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 267 LFYALGTVMVLGIFGVRG---LNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18573 230 STGFSGNLSLLSVLYYGGslvASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
345-579 |
2.94e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.50 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 345 PTAKITRGKIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDR-----DI- 418
Cdd:COG1134 17 YHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallELg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 419 ---------REypaeelrqkmglvlqepfmfygdinsNIRmFNDQI---SDEQVQAAARFVKA----DDFInDLPenyqs 482
Cdd:COG1134 97 agfhpeltgRE--------------------------NIY-LNGRLlglSRKEIDEKFDEIVEfaelGDFI-DQP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 483 rViergASYSSGQRQLISFARTIVTDPKILILDEATANVDTE-----TEEMiqtgLDRIQENRTTIAIAHRLSTIQN-AD 556
Cdd:COG1134 144 -V----KTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkcLARI----RELRESGRTVIFVSHSMGAVRRlCD 214
|
250 260
....*....|....*....|...
gi 1027832812 557 LILVLNQGKIVERGSNDELLQQH 579
Cdd:COG1134 215 RAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
359-581 |
3.25e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 359 VTFAYDGQH-PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYE-----FQSGEVLIDDR-----DIREYPAEELR 427
Cdd:PRK10261 20 IAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEqagglVQCDKMLLRRRsrqviELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 428 Q----KMGLVLQEP-------FMFYGDINSNIRMFNDQISDEQVQAAARFVkadDFINdLPENyQSRVIERGASYSSGQR 496
Cdd:PRK10261 100 HvrgaDMAMIFQEPmtslnpvFTVGEQIAESIRLHQGASREEAMVEAKRML---DQVR-IPEA-QTILSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 497 QLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRT--TIAIAHRLSTIQN-ADLILVLNQGKIVERGSND 573
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVE 254
|
250
....*....|
gi 1027832812 574 ELLQ--QHGY 581
Cdd:PRK10261 255 QIFHapQHPY 264
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
354-578 |
3.80e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHP----VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPA----EE 425
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 426 LRQKMGLVLQ--EPFMFYGDINSNIrMFNDQ---ISDEQVQAAARFVKA-----DDFINDLPenyqsrviergASYSSGQ 495
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDV-AFGPQnfgVSQEEAEALAREKLAlvgisESLFEKNP-----------FELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 496 RQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIA-IAHRLSTIQN-ADLILVLNQGKIVERGSND 573
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPK 230
|
....*
gi 1027832812 574 ELLQQ 578
Cdd:PRK13649 231 DIFQD 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-575 |
6.23e-15 |
|
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: 77.54 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVL--MRFYEFQSGEVL------------------- 412
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 413 --------------IDDRDIREYPAEELRQKMGLVLQEPFMFYGD---INSNIRMFND--QISDEQVQAAARFVKAddfi 473
Cdd:TIGR03269 80 epcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDdtvLDNVLEALEEigYEGKEAVGRAVDLIEM---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 474 ndlpENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDR--IQENRTTIAIAHRLST 551
Cdd:TIGR03269 156 ----VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEV 231
|
250 260
....*....|....*....|....*
gi 1027832812 552 IQN-ADLILVLNQGKIVERGSNDEL 575
Cdd:TIGR03269 232 IEDlSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
371-581 |
1.05e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 371 KDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQK---MGLVLQEPF------MFY 441
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLaslnprMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 442 GDINSN-IRMFNDQISDEQVQAAarfVKA--------DDFINDLPEnyqsrviergaSYSSGQRQLISFARTIVTDPKIL 512
Cdd:PRK15079 118 GEIIAEpLRTYHPKLSRQEVKDR---VKAmmlkvgllPNLINRYPH-----------EFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 513 ILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQ--QHGY 581
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHnpLHPY 257
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
369-567 |
1.13e-14 |
|
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: 73.46 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 369 VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ---SGEVLIDDRDIReypAEELRQKMGLVLQ---------- 435
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRK---PDQFQKCVAYVRQddillpgltv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 436 EPFMFYGDINSNIRMFNDQISDEQVqaaarfvkADDFINDLpenyqsrVIERGASY-----SSGQRQLISFARTIVTDPK 510
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRV--------EDVLLRDL-------ALTRIGGNlvkgiSGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 511 ILILDEATANVDTETE-EMIQTGLDRIQENRTTIAIAH--RLSTIQNADLILVLNQGKIV 567
Cdd:cd03234 164 VLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
359-576 |
1.45e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 359 VTFaydGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQE-- 436
Cdd:PRK09536 11 VEF---GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDts 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 437 -PFMFygDINSNIRM--------FN--DQISDEQVQAAARFVKADDFINdlpenyqsRVIErgaSYSSGQRQLISFARTI 505
Cdd:PRK09536 88 lSFEF--DVRQVVEMgrtphrsrFDtwTETDRAAVERAMERTGVAQFAD--------RPVT---SLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027832812 506 VTDPKILILDEATANVD----TETEEMIQTGLDriqENRTTIAIAHRLS-TIQNADLILVLNQGKIVERGSNDELL 576
Cdd:PRK09536 155 AQATPVLLLDEPTASLDinhqVRTLELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
367-566 |
1.67e-14 |
|
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: 72.08 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 367 HPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEEL-----------RQKMGLVLQ 435
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragiayvpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 436 EPfmfygdINSNIRMfndqisdeqvqaaarfvkaddfindlpenyqsrvierGASYSSGQRQLISFARTIVTDPKILILD 515
Cdd:cd03215 93 LS------VAENIAL-------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1027832812 516 EATANVDTETEEMIQTGLDRIQENRTTIAIahrLST-----IQNADLILVLNQGKI 566
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
354-578 |
1.79e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.14 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREypaEELRQK-MGL 432
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQE----PFMFYGD-INSNIRMFN---DQISdEQVQAAARFVkaddfinDLpENYQSRVIERgasYSSGQRQLISFART 504
Cdd:PRK11432 83 VFQSyalfPHMSLGEnVGYGLKMLGvpkEERK-QRVKEALELV-------DL-AGFEDRYVDQ---ISGGQQQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 505 IVTDPKILILDEATANVDTETEEMIQtglDRIQE-----NRTTIAIAHRLS-TIQNADLILVLNQGKIVERGSNDELLQQ 578
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMR---EKIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
354-574 |
2.09e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDR--DIREyPAEELRQKMG 431
Cdd:COG3845 6 LELRGITKRFGGVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS-PRDAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQEpFM-----------FYGDINSNIRMFNDQISDEQVQA-AARF---VKADDFINDLpenyqsrviergasySSGQR 496
Cdd:COG3845 84 MVHQH-FMlvpnltvaeniVLGLEPTKGGRLDRKAARARIRElSERYgldVDPDAKVEDL---------------SVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 497 QLISFARTIVTDPKILILDEATAnVDT--ETEEMIQTgLDRIQENRTTIA-IAHRLSTI-QNADLILVLNQGKIVERGSN 572
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTA-VLTpqEADELFEI-LRRLAAEGKSIIfITHKLREVmAIADRVTVLRRGKVVGTVDT 225
|
..
gi 1027832812 573 DE 574
Cdd:COG3845 226 AE 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
354-581 |
2.96e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHvtfaYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFY-----EFQSGEVLIDDRDIREYPAEELRQ 428
Cdd:PRK15134 13 VAFRQ----QQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvVYPSGDIRFHGESLLHASEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 429 ----KMGLVLQEPFM-----------FYGDINSNIRMFNDQISDEQV---------QAAARfvkaddfINDLPENYqsrv 484
Cdd:PRK15134 89 vrgnKIAMIFQEPMVslnplhtlekqLYEVLSLHRGMRREAARGEILncldrvgirQAAKR-------LTDYPHQL---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 485 iergasySSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRLSTI-QNADLILVL 561
Cdd:PRK15134 158 -------SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVM 230
|
250 260
....*....|....*....|..
gi 1027832812 562 NQGKIVERGSNDELLQ--QHGY 581
Cdd:PRK15134 231 QNGRCVEQNRAATLFSapTHPY 252
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
365-568 |
3.94e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.12 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 365 GQH--PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAE---ELR-QKMGLVLQEpF 438
Cdd:PRK10584 19 GEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQS-F 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 439 MFYGDINS--NI------RMFNDQISDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFARTIVTDPK 510
Cdd:PRK10584 98 MLIPTLNAleNVelpallRGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 511 ILILDEATANVDTeteemiQTGlDRIQE-----NR----TTIAIAHRLSTIQNADLILVLNQGKIVE 568
Cdd:PRK10584 167 VLFADEPTGNLDR------QTG-DKIADllfslNRehgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
357-581 |
4.09e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.65 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 357 RHVTFAYDGQHPvLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRD------------------- 417
Cdd:PRK11701 10 RGLTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyalseaerrrllr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 418 -----IREYPAEELRQKM--GLVLQEPFMFYGDIN-SNIRmfnDQISD--EQVQ-AAARfvkaddfINDLPenyqsrvie 486
Cdd:PRK11701 89 tewgfVHQHPRDGLRMQVsaGGNIGERLMAVGARHyGDIR---ATAGDwlERVEiDAAR-------IDDLP--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 487 rgASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIqtgLDRIQENRTTIAIA-----HRLSTIQN-ADLILV 560
Cdd:PRK11701 150 --TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARL---LDLLRGLVRELGLAvvivtHDLAVARLlAHRLLV 224
|
250 260
....*....|....*....|...
gi 1027832812 561 LNQGKIVERGSNDELLQ--QHGY 581
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDdpQHPY 247
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
373-575 |
5.28e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 373 VSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELrQKMGLVlqEPFmfygdinSNIRMFN 452
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVV--RTF-------QHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 453 DQISDEQVQAAA-RFVKAdDFINDL---PENYQS--RVIERGASY-----------------SSGQRQLISFARTIVTDP 509
Cdd:PRK11300 94 EMTVIENLLVAQhQQLKT-GLFSGLlktPAFRRAesEALDRAATWlervgllehanrqagnlAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 510 KILILDEATANVD-TETEEMIQ-TGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDEL 575
Cdd:PRK11300 173 EILMLDEPAAGLNpKETKELDElIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
35-568 |
7.70e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.24 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIylprVLQTFIDHYL-KTGHATVPVMWYFAGLYFFGMVVRALMQFvqnfSSTMGAEYMLENVRRQ 113
Cdd:PRK10522 15 FISVMALSLASAALGI----GLIAFINQRLiETADTSLLVLPEFLGLLLLLMAVTLGSQL----ALTTLGHHFVYRLRSE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 114 MFAKLHRMGMRYFDQVPGGSILSRLTND----TMSFSNFWALFNTLftaffaVISSFVAMYLTdaqialWL-----LVFM 184
Cdd:PRK10522 87 FIKRILDTHVERIEQLGSASLLASLTSDvrniTIAFVRLPELVQGI------ILTLGSAAYLA------WLspkmlLVTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 185 PFLAVTIWYYQRYSSRVYRRMReRLSELNTKLSE----AITGIS--VIQQFRQEHRINGEFDHTNDAYfktRQAMIRTNS 258
Cdd:PRK10522 155 IWMAVTIWGGFVLVARVYKHMA-TLRETEDKLYNdyqtVLEGRKelTLNRERAEYVFENEYEPDAQEY---RHHIIRADT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 259 LLLSPLidlfyALGTVMVLGIFGV-----RGL---NGYVAAgvVYAF-ITYLNNfynPMTSMMDNLSDFQDGVVAgsrvL 329
Cdd:PRK10522 231 FHLSAV-----NWSNIMMLGAIGLvfymaNSLgwaDTNVAA--TYSLtLLFLRT---PLLSAVGALPTLLSAQVA----F 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 330 RVMDDPTIAPAQHVDPTAKITRG--KIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ 407
Cdd:PRK10522 297 NKLNKLALAPYKAEFPRPQAFPDwqTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 408 SGEVLIDDRDIREYPAEELRQKMGLVLqepfmfygdinSNIRMFNDQISDEQVQAAARFVkaDDFINDLpeNYQSRVIER 487
Cdd:PRK10522 377 SGEILLDGKPVTAEQPEDYRKLFSAVF-----------TDFHLFDQLLGPEGKPANPALV--EKWLERL--KMAHKLELE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 488 GA-----SYSSGQRQLISFARTIVTDPKILILDEATANVDTE-TEEMIQTGLDRIQE-NRTTIAIAHRLSTIQNADLILV 560
Cdd:PRK10522 442 DGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISHDDHYFIHADRLLE 521
|
....*...
gi 1027832812 561 LNQGKIVE 568
Cdd:PRK10522 522 MRNGQLSE 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
354-575 |
7.75e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDI-REYPAeeLRQKMG- 431
Cdd:PRK15439 12 LCARSISKQYSGV-EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPA--KAHQLGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 -LVLQEPFMFYG-DINSNI--RMFNDQISDEQVQAaarfvkaddFINDLpeNYQSRVIERGASYSSGQRQLISFARTIVT 507
Cdd:PRK15439 89 yLVPQEPLLFPNlSVKENIlfGLPKRQASMQKMKQ---------LLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 508 DPKILILDEATANVD-TETEEMIQtgldRIQENRTT----IAIAHRLSTI-QNADLILVLNQGKIVERGSNDEL 575
Cdd:PRK15439 158 DSRILILDEPTASLTpAETERLFS----RIRELLAQgvgiVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
362-546 |
8.34e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 362 AYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMG--------LV 433
Cdd:PRK13539 10 CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGhrnamkpaLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMFYGDINSNirmfndqiSDEQVQAAARFVKADDfINDLPENYqsrviergasYSSGQRQLISFARTIVTDPKILI 513
Cdd:PRK13539 90 VAENLEFWAAFLGG--------EELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|...
gi 1027832812 514 LDEATANVDTETEEMIqTGLDRIQENRTTIAIA 546
Cdd:PRK13539 151 LDEPTAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
365-578 |
1.30e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.15 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 365 GQHPVLKDVSFVAEPGQTVALVGQTGSGKtSTINVLMRFYEFQS-GEVLIDDRDIR-------------EYPAEELRQKM 430
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGK-STFLRCINFLEKPSeGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEpFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQSRvIERGASYSSGQRQLISFARTIVTDPK 510
Cdd:PRK10619 95 TMVFQH-FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ-GKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 511 ILILDEATANVDTE-TEEMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQQ 578
Cdd:PRK10619 173 VLLFDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
354-578 |
1.35e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.69 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHP----VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDI----REYPAEE 425
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 426 LRQKMGLVLQEP--FMFYGDINSNIrMFNDQ---ISDEQVQAAArfVKADDFINDLPENYQSRVIErgasYSSGQRQLIS 500
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDV-AFGPQnfgIPKEKAEKIA--AEKLEMVGLADEFWEKSPFE----LSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 501 FARTIVTDPKILILDEATANVDTETE-EMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQQ 578
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
356-583 |
1.68e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.37 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 356 FRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElrQKMGLVLQ 435
Cdd:PRK11000 6 LRNVTKAYGDVV-ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 436 EpFMFYGDINSNIRM-FNDQIS-------DEQVQAAARFVKADDFINDLPEnyqsrviergaSYSSGQRQLISFARTIVT 507
Cdd:PRK11000 83 S-YALYPHLSVAENMsFGLKLAgakkeeiNQRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 508 DPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAH-RLSTIQNADLILVLNQGKIVERGSNDELlqqhgYYY 583
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL-----YHY 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
363-558 |
1.95e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.57 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 363 YDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ-----SGEVLIDDRDIREYPAE--ELRQKMGLVLQ 435
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDtvDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 436 EPFMFYGDINSN------IRMFND-QISDEQVQAAARFVKADDFINDlpenyqsRVIERGASYSSGQRQLISFARTIVTD 508
Cdd:PRK14239 94 QPNPFPMSIYENvvyglrLKGIKDkQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1027832812 509 PKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHrlsTIQNADLI 558
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-567 |
2.04e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.50 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 366 QHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLVLQEPFM------ 439
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtapsm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 440 ------------------FYGDINSNIRMFNDQISDeqvqaaarfvkaddFINDLPENYQSRViergASYSSGQRQLISF 501
Cdd:COG1101 98 tieenlalayrrgkrrglRRGLTKKRRELFRELLAT--------------LGLGLENRLDTKV----GLLSGGQRQALSL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 502 ARTIVTDPKILILDEATANVDTETEEMIQTGLDRI--QENRTTIAIAHRLS-TIQNADLILVLNQGKIV 567
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
354-577 |
2.28e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYpAEELRQKMGLV 433
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-ARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQ----EPFMfygDINSNIRMFNDQISDEQVQAAARFVKADDFindlpENYQSRVIERGASYSSGQRQLISFARTIVTDP 509
Cdd:PRK13537 86 PQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEF-----AKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 510 KILILDEATANVDTETEEMIQTGLDRIQENRTTIAI-------AHRLstiqnADLILVLNQGKIVERGSNDELLQ 577
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHALIE 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
354-579 |
2.88e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.61 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpvlKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEelRQKMGLV 433
Cdd:PRK10771 2 LKLTDITWLYHHLP---MRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMF-YGDINSNI--------RMFNDQisDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFART 504
Cdd:PRK10771 77 FQENNLFsHLTVAQNIglglnpglKLNAAQ--REKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 505 IVTDPKILILDEATANVDTE-TEEMIQTgLDRIQENR--TTIAIAHRLS-TIQNADLILVLNQGKIVERGSNDELLQQH 579
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPAlRQEMLTL-VSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
354-567 |
5.66e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEE---LRQKM 430
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQE---------------PFMFYGDINSNIRmfndqisdEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQ 495
Cdd:PRK10908 82 GMIFQDhhllmdrtvydnvaiPLIIAGASGDDIR--------RRVSAALDKVGLLDKAKNFP-----------IQLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 496 RQLISFARTIVTDPKILILDEATANVDTETEEmiqtGLDRIQE--NR---TTIAIAHRLSTIQNADL-ILVLNQGKIV 567
Cdd:PRK10908 143 QQRVGIARAVVNKPAVLLADEPTGNLDDALSE----GILRLFEefNRvgvTVLMATHDIGLISRRSYrMLTLSDGHLH 216
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
354-575 |
9.20e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.73 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTfAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElrQKMGLV 433
Cdd:PRK10851 3 IEIANIK-KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMF-----YGDINSNIRMF------NDQISDEQVQAAARFVKADDFINDLPenyqsrviergASYSSGQRQLISFA 502
Cdd:PRK10851 80 FQHYALFrhmtvFDNIAFGLTVLprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027832812 503 RTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAH-RLSTIQNADLILVLNQGKIVERGSNDEL 575
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
358-581 |
1.03e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.37 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 358 HVTFAY-DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ---SGEVLIDDRDIREYPAEELR----QK 429
Cdd:PRK09473 19 RVTFSTpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNklraEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 430 MGLVLQE------PFMFYGDINSNIRMFNDQISdeQVQAAARFVKADDFINdLPENyQSRVIERGASYSSGQRQLISFAR 503
Cdd:PRK09473 99 ISMIFQDpmtslnPYMRVGEQLMEVLMLHKGMS--KAEAFEESVRMLDAVK-MPEA-RKRMKMYPHEFSGGMRQRVMIAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 504 TIVTDPKILILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQQ-- 578
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQps 254
|
...
gi 1027832812 579 HGY 581
Cdd:PRK09473 255 HPY 257
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
361-580 |
1.19e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 361 FAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDR--DIREYPAEELRQKMGLVLQEP- 437
Cdd:PRK13638 9 FRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 438 -FMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFINdlPENYQSRVIErgaSYSSGQRQLISFARTIVTDPKILILDE 516
Cdd:PRK13638 88 qQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD--AQHFRHQPIQ---CLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 517 ATANVDTETEEMIQTGLDRI--QENRTTIAiAHRLSTI-QNADLILVLNQGKIVERG------SNDELLQQHG 580
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIvaQGNHVIIS-SHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQAG 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
362-570 |
1.55e-12 |
|
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: 67.17 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 362 AYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIreypaeelrqkmglvlqEPFMFY 441
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----------------SLLGLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 442 GDINS------NIRmFNDQI---SDEQVQAAARFVKadDFiNDLPENYQSRVIErgasYSSGQRQLISFARTIVTDPKIL 512
Cdd:cd03220 93 GGFNPeltgreNIY-LNGRLlglSRKEIDEKIDEII--EF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 513 ILDEATANVDTET-EEMIQTGLDRIQENRTTIAIAHRLSTI-QNADLILVLNQGKIVERG 570
Cdd:cd03220 165 LIDEVLAVGDAAFqEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
354-565 |
2.60e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQS--GEVLIDDRDIREYPAEELRQKmG 431
Cdd:PRK13549 6 LEMKNITKTFGGV-KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERA-G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVL--QE----PFMFYGDinsNIRMFNDQISDEQVQAAARFVKADDFIND--LPENYQSRVIErgasYSSGQRQLISFAR 503
Cdd:PRK13549 84 IAIihQElalvKELSVLE---NIFLGNEITPGGIMDYDAMYLRAQKLLAQlkLDINPATPVGN----LGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 504 TIVTDPKILILDEATANVdTETEemIQTGLDRIQENR----TTIAIAHRLSTIQN-ADLILVLNQGK 565
Cdd:PRK13549 157 ALNKQARLLILDEPTASL-TESE--TAVLLDIIRDLKahgiACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
354-576 |
4.02e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYP-AEELRQKMGL 432
Cdd:PRK11614 6 LSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQepfmfygdinsNIRMFNDQISDEQVQAAARFVKADDF------INDLPENYQSRVIERGASYSSGQRQLISFARTIV 506
Cdd:PRK11614 85 VPE-----------GRRVFSRMTVEENLAMGGFFAERDQFqerikwVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 507 TDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRLS--TIQNADLILVLNQGKIVERGSNDELL 576
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
381-571 |
4.12e-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: 69.66 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 381 QTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIrEYPAEELRQKMGLVLQEPFMFYGDINSNIRMFNDQISDEQV 460
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 461 QAAArfVKADDFINDLPENYQSRviERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR 540
Cdd:TIGR01257 1036 EEAQ--LEMEAMLEDTGLHHKRN--EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR 1111
|
170 180 190
....*....|....*....|....*....|....*
gi 1027832812 541 TTIAIAHRLStiqNADL----ILVLNQGKIVERGS 571
Cdd:TIGR01257 1112 TIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
114-310 |
6.26e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 66.78 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 114 MFAKlhrmgMRYFDQVPGGSILSRLTNDT------MSFSnfwalFNTLFTAFFAVISSFVAMYltdaqIAL-WLLVFMPF 186
Cdd:cd18605 86 LFAK-----MSFFDKTPVGRILNRFSSDVytiddsLPFI-----LNILLAQLFGLLGYLVVIC-----YQLpWLLLLLLP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 187 LAVTIWYYQRYssrvYRRM-RE--RLSELN-----TKLSEAITGISVIQQFRQEHRINGEF-DHTND---AYFKTRQA-- 252
Cdd:cd18605 151 LAFIYYRIQRY----YRATsRElkRLNSVNlsplyTHFSETLKGLVTIRAFRKQERFLKEYlEKLENnqrAQLASQAAsq 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 253 --MIRTnsLLLSPLIDLFYALGTvmVLGIFGVRGLN-GYVAAGVVYA--FITYLNNFYNPMTS 310
Cdd:cd18605 227 wlSIRL--QLLGVLIVTFVALTA--VVQHFFGLSIDaGLIGLALSYAlpITGLLSGLLNSFTE 285
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
372-570 |
7.38e-12 |
|
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: 65.01 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 372 DVSFVAePGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDR---DIRE---YPAEelRQKMGLVLQEPFMF-YGDI 444
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkinLPPQ--QRKIGLVFQQYALFpHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 445 NSNI-------RMFNDQIS-DEQVQAAArfvkaddfINDLPENYQSRViergasySSGQRQLISFARTIVTDPKILILDE 516
Cdd:cd03297 93 RENLafglkrkRNREDRISvDELLDLLG--------LDHLLNRYPAQL-------SGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 517 ATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRLSTIQN-ADLILVLNQGKIVERG 570
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
363-549 |
7.93e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 363 YDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEF-----QSGEVLIDDRDI--REYPAEELRQKMGLVLQ 435
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 436 EPFMFYGDINSNIrMFNDQIS------DEQVQAAARFVKADDFINDlpenyqsRVIERGASYSSGQRQLISFARTIVTDP 509
Cdd:PRK14243 99 KPNPFPKSIYDNI-AYGARINgykgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1027832812 510 KILILDEATANVDT----ETEEMIQTgldrIQENRTTIAIAHRL 549
Cdd:PRK14243 171 EVILMDEPCSALDPistlRIEELMHE----LKEQYTIIIVTHNM 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-552 |
7.99e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 65.83 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQS-----GEVLIDDRDI--REYPAEEL 426
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 427 RQKMGLVLQEPFMF----YGDINSNIRMFN-------DQISDEQVQAAarfvkaddfinDLPENYQSRVIERGASYSSGQ 495
Cdd:PRK14258 87 RRQVSMVHPKPNLFpmsvYDNVAYGVKIVGwrpkleiDDIVESALKDA-----------DLWDEIKHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 496 RQLISFARTIVTDPKILILDEATANVD----TETEEMIQTglDRIQENRTTIAIAHRLSTI 552
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQS--LRLRSELTMVIVSHNLHQV 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
365-577 |
8.55e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.44 E-value: 8.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 365 GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEElRQKMGL--VLQEPFMFYG 442
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK-RARLGIgyLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 443 ----DinsNIRMFNDQIsdeQVQAAARFVKADDFINDLPenyqsrvIE-----RGASYSSGQRQLISFARTIVTDPKILI 513
Cdd:COG1137 93 ltveD---NILAVLELR---KLSKKEREERLEELLEEFG-------IThlrksKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 514 LDEATANVD----TETEEMIQTGLDR-----IQE-N-RTTIAIAHRLStiqnadlilVLNQGKIVERGSNDELLQ 577
Cdd:COG1137 160 LDEPFAGVDpiavADIQKIIRHLKERgigvlITDhNvRETLGICDRAY---------IISEGKVLAEGTPEEILN 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
355-579 |
1.13e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 355 EFRHVTfAYDGQHPVLK---DVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQS-GEVLIDDR--DIREyPAEELRQ 428
Cdd:PRK13549 261 EVRNLT-AWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKpvKIRN-PQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 429 KMGLVLQE-------PFMfygDINSNIRMFN-DQISD-EQVQAAARFVKADDFINDL------PEnyqsrviERGASYSS 493
Cdd:PRK13549 339 GIAMVPEDrkrdgivPVM---GVGKNITLAAlDRFTGgSRIDDAAELKTILESIQRLkvktasPE-------LAIARLSG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 494 GQRQLISFARTIVTDPKILILDEATANVDT----ETEEMIQtglDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIve 568
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLIN---QLVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL-- 483
|
250
....*....|...
gi 1027832812 569 RGS--NDELLQQH 579
Cdd:PRK13549 484 KGDliNHNLTQEQ 496
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
353-581 |
1.33e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 353 KIEFRHVTFaydGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRF--YEFQSGEVLIDDRDIREYPAEElRQKM 430
Cdd:CHL00131 9 EIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE-RAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVL--QEPFMFYGDINSNIRMfndqISDEQVQAAARFVKAD-----DFIN------DLPENYQSRVIERGasYSSGQRQ 497
Cdd:CHL00131 85 GIFLafQYPIEIPGVSNADFLR----LAYNSKRKFQGLPELDpleflEIINeklklvGMDPSFLSRNVNEG--FSGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 498 LISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQ-ENRTTIAIAH--RLSTIQNADLILVLNQGKIVERGSND- 573
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAEl 238
|
....*....
gi 1027832812 574 -ELLQQHGY 581
Cdd:CHL00131 239 aKELEKKGY 247
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
353-522 |
1.72e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.02 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 353 KIEFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKtSTinvLMRFY----EFQSGEVLIDDRDIRE-------- 420
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGK-ST---LLRMVagleRITSGEIWIGGRVVNElepadrdi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 421 ---------YPAEELRQKMGLVLQepfmfygdinsNIRMFNDQIsDEQVQAAARFVKADDFINDLPenyqsrviergASY 491
Cdd:PRK11650 79 amvfqnyalYPHMSVRENMAYGLK-----------IRGMPKAEI-EERVAEAARILELEPLLDRKP-----------REL 135
|
170 180 190
....*....|....*....|....*....|.
gi 1027832812 492 SSGQRQLISFARTIVTDPKILILDEATANVD 522
Cdd:PRK11650 136 SGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
369-529 |
1.74e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.45 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 369 VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAE---ELR-QKMGLVLQEPFMFyGDI 444
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQFHHLL-PDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 445 NS--NIRM--FNDQISDEQVQAAARFVKAddfindlPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATAN 520
Cdd:PRK11629 103 TAleNVAMplLIGKKKPAEINSRALEMLA-------AVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
....*....
gi 1027832812 521 VDTETEEMI 529
Cdd:PRK11629 176 LDARNADSI 184
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
354-565 |
2.60e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 61.70 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDrdireypaeelRQKMGLV 433
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQepfmfygdinsnirmfndqisdeqvqaaarfvkaddfindlpenyqsrviergasYSSGQRQLISFARTIVTDPKILI 513
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 514 LDEATANVDTETEEMIQTGLdrIQENRTTIAIAHRLSTIQN-ADLILVLNQGK 565
Cdd:cd03221 94 LDEPTNHLDLESIEALEEAL--KEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
369-577 |
2.97e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.73 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 369 VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIdDRDIREYPaeelrqkmglvlQEPFMFYGDINSNI 448
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-ERSIAYVP------------QQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 449 rMFNDQISDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEM 528
Cdd:PTZ00243 742 -LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1027832812 529 IqtgldrIQE-------NRTTIAIAHRLSTIQNADLILVLNQGKIVERGSNDELLQ 577
Cdd:PTZ00243 821 V------VEEcflgalaGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
368-570 |
3.60e-11 |
|
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: 63.51 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 368 PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDireyPAE---ELRQKMGLVLQEPFMFYGDI 444
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV----PWKrrkKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 445 N--SNIRMFNDQISDEQVQAAARFVKADDFINDLPENYQS-RviergaSYSSGQRQLISFARTIVTDPKILILDEATANV 521
Cdd:cd03267 111 PviDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPvR------QLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 522 DTETEEMIQTGLDRIQENR--TTIAIAHRLSTIQN-ADLILVLNQGKIVERG 570
Cdd:cd03267 185 DVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
38-328 |
6.58e-11 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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 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. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 63.27 E-value: 6.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 38 AIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYFAGLYFFGMVVRAL-MQFVQNFSSTMGAeymleNVR----R 112
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLlLHQYFFLSFRLGM-----RVRsalsS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 113 QMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALFNTLFTAFFAVIssfVAMYLTDAQI-------ALWLLVFMP 185
Cdd:cd18579 77 LIYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQII---VALYLLYRLLgwaalagLGVLLLLIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 186 FlavtiwyyQRYSSRVYRRMRERLSELNTK----LSEAITGISVI------QQFRQehRINgefdhtndayfKTRQ---A 252
Cdd:cd18579 154 L--------QAFLAKLISKLRKKLMKATDErvklTNEILSGIKVIklyaweKPFLK--RIE-----------ELRKkelK 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 253 MIRTNSLLLSPLIDLFYALGTVMVLGIFGVRGLNGYV-AAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18579 213 ALRKFGYLRALNSFLFFSTPVLVSLATFATYVLLGNPlTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
33-328 |
7.82e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 63.27 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 33 CFFIAAIVFSGLISVVNIYLprvlQTFIDHYLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGA--------E 104
Cdd:cd18603 3 LILLLYLLSQAFSVGSNIWL----SEWSDDPALNGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCvrasrnlhN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 105 YMLENVRRQMfaklhrmgMRYFDQVPGGSILSRLTNDTMSF-SNFWALFNTLFTAFFAVISSFVAmyltdaqIAL---WL 180
Cdd:cd18603 79 KLLHNILRAP--------MSFFDTTPLGRILNRFSKDIDTVdNTLPQNIRSFLNCLFQVISTLVV-------ISIstpIF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 181 LVFMPFLAVTIWYYQRY---SSRVYRRM----RerlSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAM 253
Cdd:cd18603 144 LVVIIPLAILYFFIQRFyvaTSRQLKRLesvsR---SPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPS 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 254 IRTNsLLLSPLIDLfyaLGTVMVL--GIFGVRGlNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18603 221 IVSN-RWLAVRLEF---LGNLIVLfaALFAVLS-RDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERI 292
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
340-568 |
9.97e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 64.32 E-value: 9.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 340 AQHVDPTAKITR------GK--IEFRHVTFAYDGqHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEV 411
Cdd:COG0488 294 PPRRDKTVEIRFppperlGKkvLELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 412 -----------------LIDDRDIREYPAE--------ELRQKMGLvlqepFMFYGDinsnirmfndqisdeqvqaaarf 466
Cdd:COG0488 373 klgetvkigyfdqhqeeLDPDKTVLDELRDgapggteqEVRGYLGR-----FLFSGD----------------------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 467 vKADDFINDLpenyqsrviergasySSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQEnrTTIAIA 546
Cdd:COG0488 425 -DAFKPVGVL---------------SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG--TVLLVS 486
|
250 260
....*....|....*....|....*
gi 1027832812 547 H-R--LSTIqnADLILVLNQGKIVE 568
Cdd:COG0488 487 HdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
362-561 |
1.18e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 61.10 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 362 AYDGqHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDD-----------RDIREYPAEeLRQKM 430
Cdd:NF040873 1 GYGG-RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpqrsEVPDSLPLT-VRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 431 GLVLQEPFMFYGDINSNIRMfndqisdeQVQAAARFVKADDFINdlpenyqsrviERGASYSSGQRQLISFARTIVTDPK 510
Cdd:NF040873 79 AMGRWARRGLWRRLTRDDRA--------AVDDALERVGLADLAG-----------RQLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 511 ILILDEATANVDTETEEMIQTGLDRI-QENRTTIAIAHRLSTIQNADLILVL 561
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCVLL 191
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
368-581 |
1.21e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.12 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 368 PVLKDVSFVAEPGQTVALVGQTGSGKtSTINVLM---RFYEFQSGEVLIDDRDIREY-PAEELRQKMGLVLQEP------ 437
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGK-STLSATLagrEDYEVTGGTVEFKGKDLLELsPEDRAGEGIFMAFQYPveipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 438 ---FMFYGDINSnIRMFNDQisdeqvQAAARFvKADDFIND------LPENYQSRVIERGasYSSGQRQLISFARTIVTD 508
Cdd:PRK09580 94 snqFFLQTALNA-VRSYRGQ------EPLDRF-DFQDLMEEkiallkMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 509 PKILILDEATANVDTETEEMIQTGLDRIQ-ENRTTIAIAH--RLSTIQNADLILVLNQGKIVERG--SNDELLQQHGY 581
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGdfTLVKQLEEQGY 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
320-575 |
1.42e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 320 DGVVAGSRVLRVMDDPTIA------PAQHVDPTAKITRGKI--EFRHVTFAydgqhPVLKDVSFVAEPGQTVALVGQTGS 391
Cdd:COG1129 215 DGRLVGTGPVAELTEDELVrlmvgrELEDLFPKRAAAPGEVvlEVEGLSVG-----GVVRDVSFSVRAGEILGIAGLVGA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 392 GKTSTINVLMRFYEFQSGEVLIDDRDIR-EYPAEELRQKM----------GLVLQEPfmfygdINSNIRMFN-DQIS--- 456
Cdd:COG1129 290 GRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIayvpedrkgeGLVLDLS------IRENITLASlDRLSrgg 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 457 --DEQVQAAArfvkADDFINDLpenyqsRV----IERGASYSSG--QrQLISFARTIVTDPKILILDEATANVDTETEEM 528
Cdd:COG1129 364 llDRRRERAL----AEEYIKRL------RIktpsPEQPVGNLSGgnQ-QKVVLAKWLATDPKVLILDEPTRGIDVGAKAE 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 529 IQTGLDRI-QENRTTIAIahrlST-----IQNADLILVLNQGKIVERGSNDEL 575
Cdd:COG1129 433 IYRLIRELaAEGKAVIVI----SSelpelLGLSDRILVMREGRIVGELDREEA 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
370-568 |
1.83e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.27 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 370 LKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQS--GEVLIDD-----RDIREypAEELrqkmGLVL--QE---- 436
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIRD--SEAL----GIVIihQElali 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 437 PFMfygDINSNIRMFNDQISDEQVQAAARFVKADDFIND--LPENYQSRVIERGAsyssGQRQLISFARTIVTDPKILIL 514
Cdd:NF040905 91 PYL---SIAENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 515 DEATANV-DTETEEMiqtgLDRIQENR----TTIAIAHRLSTI-QNADLILVLNQGKIVE 568
Cdd:NF040905 164 DEPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
74-300 |
1.86e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 62.24 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 74 MWYFAGLYFFGMVVRALMQFVQNFSstmgAEYMLENVRRQMFAK-LHRM---GMRYFDQVPGGSILSRLTNDT------M 143
Cdd:cd18602 49 VSYYISVYAGLSLGAVILSLVTNLA----GELAGLRAARRLHDRmLRNIvraPMRFFDTTPIGRILNRFSSDTnvidqkL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 144 SFSnfwalFNTLFTAFFAVISSFVAmyltDAQIALWLLVFMPFLAVTIWYYQRYsSRVYRRMRERL-----SELNTKLSE 218
Cdd:cd18602 125 PTT-----LERLLRFLLLCLSAIIV----NAIVTPYFLIALIPIIIVYYFLQKF-YRASSRELQRLdnitkSPVFSHFSE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 219 AITGISVIQQFRQEHRINGEFDHTNDAyFKTRQAMIRTNSLLLSPLIDLfyaLGTVMVL--GIFGVR-GLNGYVAAGVVY 295
Cdd:cd18602 195 TLGGLTTIRAFRQQARFTQQMLELIDR-NNTAFLFLNTANRWLGIRLDY---LGAVIVFlaALSSLTaALAGYISPSLVG 270
|
....*
gi 1027832812 296 AFITY 300
Cdd:cd18602 271 LAITY 275
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
365-529 |
2.12e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.45 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 365 GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDI---REYPAEELRQ-------KMGLVL 434
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHENILYlghlpglKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 435 QEpfmfygdinsNIRMFNDQISDEQ--VQAAARFVKADDFiNDLPenyqsrvierGASYSSGQRQLISFARTIVTDPKIL 512
Cdd:TIGR01189 91 LE----------NLHFWAAIHGGAQrtIEDALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLW 149
|
170
....*....|....*..
gi 1027832812 513 ILDEATANVDTETEEMI 529
Cdd:TIGR01189 150 ILDEPTTALDKAGVALL 166
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
32-319 |
3.78e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 61.37 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 32 KCFFIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHatVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVR 111
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGN--LNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 112 RQMFAKLHRMGMRYFDQVPGGSILSRLTNDTM---SFSNfwaLFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLA 188
Cdd:cd18555 79 SDFFEHLLKLPYSFFENRSSGDLLFRANSNVYirqILSN---QVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 189 VTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRI----NGEFdhtNDAYFKTRQAMIRTNslLLSPL 264
Cdd:cd18555 156 LLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIykkwENLF---KKQLKAFKKKERLSN--ILNSI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 265 IDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQ 319
Cdd:cd18555 231 SSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFI 285
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
370-595 |
4.80e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.26 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 370 LKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDireyPAE---ELRQKMGLV------------L 434
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV----PFKrrkEFARRIGVVfgqrsqlwwdlpA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 435 QEPFMFYGDINsnirmfndQISDEQVQAA-ARFVKA---DDFINDlpenyQSRviergaSYSSGQRQLISFARTIVTDPK 510
Cdd:COG4586 114 IDSFRLLKAIY--------RIPDAEYKKRlDELVELldlGELLDT-----PVR------QLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 511 ILILDEATANVDTETEEMIQTGLDRI-QENRTTIAIA-HRLSTIQN-ADLILVLNQGKIVERGSNDELLQQHGyYYDMIQ 587
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFG-PYKTIV 253
|
....*...
gi 1027832812 588 LQNSAHVD 595
Cdd:COG4586 254 LELAEPVP 261
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
354-567 |
7.22e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.66 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAY---DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEEL---- 426
Cdd:PRK10535 5 LELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 427 RQKMGLVLQEPFMFygdinsnirmfnDQISDEQ----------VQAAARFVKADDFINDLpeNYQSRVIERGASYSSGQR 496
Cdd:PRK10535 85 REHFGFIFQRYHLL------------SHLTAAQnvevpavyagLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 497 QLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQEN-RTTIAIAHRLSTIQNADLILVLNQGKIV 567
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
356-525 |
7.40e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.62 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 356 FRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIdDRDIReypaeelrqkMGLVLQ 435
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 436 EPFMF----------------------YGDINSNIrMFNDQISDEQVQAAARFV---------KADDFINDL--PENYQS 482
Cdd:COG0488 69 EPPLDddltvldtvldgdaelraleaeLEELEAKL-AEPDEDLERLAELQEEFEalggweaeaRAEEILSGLgfPEEDLD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1027832812 483 RVIergASYSSGQRQLISFARTIVTDPKILILDEATANVDTET 525
Cdd:COG0488 148 RPV---SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
354-576 |
1.11e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREY-PAEELRQKMGL 432
Cdd:PRK09700 6 ISMAGIGKSFGPVH-ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQE----------PFMFYGDINSNiRMFNDQISD--EQVQAAARFVKADDFINDLPenyqsrviERGASYSSGQRQLIS 500
Cdd:PRK09700 85 IYQElsvideltvlENLYIGRHLTK-KVCGVNIIDwrEMRVRAAMMLLRVGLKVDLD--------EKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 501 FARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQ-ENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERG-----SND 573
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGmvsdvSND 235
|
...
gi 1027832812 574 ELL 576
Cdd:PRK09700 236 DIV 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
359-573 |
1.16e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.51 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 359 VTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREY----------PAEELRQ 428
Cdd:PRK15056 12 VTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqknlvayvpQSEEVDW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 429 KMGLVLQEPFMF--YGDIN--SNIRMFNDQISDEqvqAAARFvkaddfinDLPEnYQSRVIergASYSSGQRQLISFART 504
Cdd:PRK15056 92 SFPVLVEDVVMMgrYGHMGwlRRAKKRDRQIVTA---ALARV--------DMVE-FRHRQI---GELSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 505 IVTDPKILILDEATANVDTETEEMIQTGLDRIQ-ENRTTIAIAHRLSTIQNADLILVLNQGKIVERGSND 573
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
357-578 |
1.60e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.59 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 357 RHVTFAYDGqhpvlkdVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGE--VLIDDR--DIREyPAEELR----Q 428
Cdd:TIGR03269 294 RGVVKAVDN-------VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTK-PGPDGRgrakR 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 429 KMGLVLQEPFMF-YGDINSNIrmfNDQISDE-----QVQAAARFVKADDFindlPENYQSRVIERGAS-YSSGQRQLISF 501
Cdd:TIGR03269 366 YIGILHQEYDLYpHRTVLDNL---TEAIGLElpdelARMKAVITLKMVGF----DEEKAEEILDKYPDeLSEGERHRVAL 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 502 ARTIVTDPKILILDEATANVDTETEEMIQTGL--DRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQQ 578
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
354-567 |
2.20e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQS--GEVLIDDRDIREYPAEELRQKMG 431
Cdd:TIGR02633 2 LEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 432 LVLQEPFMFYGDIN--SNIRMFND-QISDEQVQAAARFVKADDFIND--LPENYQSRVIergASYSSGQRQLISFARTIV 506
Cdd:TIGR02633 81 VIIHQELTLVPELSvaENIFLGNEiTLPGGRMAYNAMYLRAKNLLRElqLDADNVTRPV---GDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 507 TDPKILILDEATANV-DTETEEMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGKIV 567
Cdd:TIGR02633 158 KQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
34-234 |
3.33e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 58.25 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 34 FFIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYFaGLYFFGMVVRALMQFVQNFSSTMGAeymlenVR-- 111
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYL-GIYALISLLSVLLGTLRYLLFFFGS------LRas 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 112 RQMFAKL-H---RMGMRYFDQVPGGSILSRLTNDTMSF-SNFWALFNTLFTAFFAVISSFVAMyltdAQIALWLLVFMPF 186
Cdd:cd18604 76 RKLHERLlHsvlRAPLRWLDTTPVGRILNRFSKDIETIdSELADSLSSLLESTLSLLVILIAI----VVVSPAFLLPAVV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 187 LAVTIWYY-QRY--SSRVYRRMrerlsELNTK------LSEAITGISVIQQFRQEHR 234
Cdd:cd18604 152 LAALYVYIgRLYlrASRELKRL-----ESVARspilshFGETLAGLVTIRAFGAEER 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
354-579 |
3.37e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.69 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYpAEELRQKMGLV 433
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-ARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQ-----------EPFMFYGdinsniRMFndQISDEQVQAAarfvkaddfINDLPE--NYQSRVIERGASYSSGQRQLIS 500
Cdd:PRK13536 120 PQfdnldleftvrENLLVFG------RYF--GMSTREIEAV---------IPSLLEfaRLESKADARVSDLSGGMKRRLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 501 FARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAI-------AHRLstiqnADLILVLNQGKIVERGSND 573
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGRKIAEGRPH 257
|
....*.
gi 1027832812 574 ELLQQH 579
Cdd:PRK13536 258 ALIDEH 263
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
373-576 |
4.28e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 373 VSFVAEPGQTVALVGQTGSGKtSTINVLMRFYEFQSGEVLIDDRDIREYPAEEL-RQKMGLVLQEPFMF----------Y 441
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGK-STLLARMAGLLPGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFampvfqyltlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 442 GDINSNIRMFNDQISDeqvqaAARFVKADDFindLPENYQsrviergaSYSSGQRQLISFA-------RTIVTDPKILIL 514
Cdd:PRK03695 94 QPDKTRTEAVASALNE-----VAEALGLDDK---LGRSVN--------QLSGGEWQRVRLAavvlqvwPDINPAGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1027832812 515 DEATANVDTETeemiQTGLDRI-----QENRTTIAIAHRLS-TIQNADLILVLNQGKIVERGSNDELL 576
Cdd:PRK03695 158 DEPMNSLDVAQ----QAALDRLlselcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
79-282 |
5.17e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 57.87 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 79 GLYF-FGMVVrALMQFVQNFSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSN-FWALFNTLF 156
Cdd:cd18606 39 GIYAgLGVLQ-AIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNeLPDSLRMFL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 157 TAFFAVISSFVAM--YLTdaqialWLLVFMPFLAVTIWYYQRYssrvYRRM-RE--RL-----SELNTKLSEAITGISVI 226
Cdd:cd18606 118 YTLSSIIGTFILIiiYLP------WFAIALPPLLVLYYFIANY----YRASsRElkRLesilrSFVYANFSESLSGLSTI 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1027832812 227 QQFRQEHR---INGEF-DHTNDAYFKTrQAMIRTNSLLLSplidlfyALGTVMVL--GIFGV 282
Cdd:cd18606 188 RAYGAQDRfikKNEKLiDNMNRAYFLT-IANQRWLAIRLD-------LLGSLLVLivALLCV 241
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
369-565 |
6.14e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 369 VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQS--GEVLIDDRDireyPAEELRQKMGLVLQEPFMfYGDIN- 445
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK----PTKQILKRTGFVTQDDIL-YPHLTv 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 446 -------SNIRMFNDQISDEQVQAAarfvkaDDFINDLP-ENYQSRVIerGASY----SSGQRQLISFARTIVTDPKILI 513
Cdd:PLN03211 158 retlvfcSLLRLPKSLTKQEKILVA------ESVISELGlTKCENTII--GNSFirgiSGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 514 LDEATANVD-TETEEMIQTGLDRIQENRTTIAIAHRLST--IQNADLILVLNQGK 565
Cdd:PLN03211 230 LDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
73-309 |
8.34e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 56.90 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 73 VMWYFAGLYFFgMVVRALMQFVQNFSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALF 152
Cdd:cd18561 35 IMPPLAGIAGV-IVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 153 -NTLFTAFFAVISSFVAMYLTDAQIALWLLVFMP--FLAVTIWY--YQRYSSRVYRRMrerlSELNTKLSEAITGISVIQ 227
Cdd:cd18561 114 lPQLLVALLGPLLILIYLFFLDPLVALILLVFALliPLSPALWDrlAKDTGRRHWAAY----GRLSAQFLDSLQGMTTLK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 228 QFRQEHRINGEFDHTNDAYFKTRQAMIRTnSLLLSPLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNP 307
Cdd:cd18561 190 AFGASKRRGNELAARAEDLRQATMKVLAV-SLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILFLSREFFRP 268
|
..
gi 1027832812 308 MT 309
Cdd:cd18561 269 LR 270
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
106-299 |
8.81e-09 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 57.10 E-value: 8.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 106 MLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWA-LFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFM 184
Cdd:cd18585 66 LLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLrVLSPPVVALLVILATILFLAFFSPALALILLAGL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 185 PFLAVTI-WYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKtRQAMIRTNSLLLSP 263
Cdd:cd18585 146 LLAGVVIpLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIK-EQRRLARLSGLSQA 224
|
170 180 190
....*....|....*....|....*....|....*.
gi 1027832812 264 LIDLFYALGTVMVLgIFGVRGLNGYVAAGVVYAFIT 299
Cdd:cd18585 225 LMILLSGLTVWLVL-WLGAPLVQNGALDGALLAMLV 259
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
365-567 |
9.94e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 365 GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLmrfyefqSGEVLIDD-------------------RDIR----EY 421
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgriiyeqdlivarlqqdppRNVEgtvyDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 422 PAEELrQKMGLVLQEpfmfYGDINSNI------RMFNDQisdEQVQA------AARFvkaDDFINDLPENYQSRVIERGA 489
Cdd:PRK11147 87 VAEGI-EEQAEYLKR----YHDISHLVetdpseKNLNEL---AKLQEqldhhnLWQL---ENRINEVLAQLGLDPDAALS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 490 SYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQEnrTTIAIAHRLSTIQN-ADLILVLNQGKIV 567
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG--SIIFISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
357-577 |
1.08e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 357 RHVTFAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDI---------RE--YPAEE 425
Cdd:PRK10575 15 RNVSFRVPGR-TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsskafaRKvaYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 426 LRQKMGLVLQE-----PFMFYGDINsniRMfnDQISDEQVQAAARFVKADDFINDLPEnyqsrviergaSYSSGQRQLIS 500
Cdd:PRK10575 94 LPAAEGMTVRElvaigRYPWHGALG---RF--GAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 501 FARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENR--TTIAIAHRLS-TIQNADLILVLNQGKIVERGSNDELLQ 577
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
372-578 |
1.31e-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: 57.03 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 372 DVSFVAEPGQTVALVGQTGSGKTSTINV---LMRfyeFQSGEVLIDDR---DIREY---PAEelRQKMGLVLQEPFMF-- 440
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqDSARGiflPPH--RRRIGYVFQEARLFph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 441 --------YGDinSNIRMFNDQISDEQVqaaARFVKaddfINDLpenyqsrvIERG-ASYSSGQRQLISFARTIVTDPKI 511
Cdd:COG4148 92 lsvrgnllYGR--KRAPRAERRISFDEV---VELLG----IGHL--------LDRRpATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 512 LILDEATANVDTETEEMIQTGLDRIQEnRTTIAI---AHRLSTIQN-ADLILVLNQGKIVERGSNDELLQQ 578
Cdd:COG4148 155 LLMDEPLAALDLARKAEILPYLERLRD-ELDIPIlyvSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
379-561 |
1.40e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.92 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 379 PGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVL-IDDRDIREYPAEELRQKMglvlqepfmfygdinsnirmfndqisd 457
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 458 eqvqaaarfvkaddfindlpenyqsrVIERGASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLD--- 534
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|.
gi 1027832812 535 ----RIQENRTTIAIAHRLSTIQNADLILVL 561
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
364-525 |
1.73e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.35 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 364 DGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQ--SGEVLIDDRDI-REYPaeelrqkmglvLQEPFMF 440
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTpvAGCVDVPDNQFgREAS-----------LIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 441 YGDINSNIRMFND-QISDeqvqaaarfvkaddfindlPENYQSRVIErgasYSSGQRQLISFARTIVTDPKILILDEATA 519
Cdd:COG2401 109 KGDFKDAVELLNAvGLSD-------------------AVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
....*.
gi 1027832812 520 NVDTET 525
Cdd:COG2401 166 HLDRQT 171
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
373-581 |
2.45e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.90 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 373 VSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFqSGEVL-----IDDRDIREYPAEELRQkmgLVLQEPFMFYGDINSN 447
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMaekleFNGQDLQRISEKERRN---LVGAEVAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 448 IR---MFNDQISD-----EQVQAAARFVKADDFIN--DLPENyQSRVIERGASYSSGQRQLISFARTIVTDPKILILDEA 517
Cdd:PRK11022 102 LNpcyTVGFQIMEaikvhQGGNKKTRRQRAIDLLNqvGIPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 518 TANVDTETEEMIQTGLDRIQ--ENRTTIAIAHRLSTI-QNADLILVLNQGKIVERGSNDELLQ--QHGY 581
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQqkENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRapRHPY 249
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
354-531 |
2.87e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 54.42 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLV 433
Cdd:cd03231 1 LEADELTCERDGR-ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQEPFMFYGDINSNIRMFNDQISDEQVQAAARFVKADDFiNDLPENYqsrviergasYSSGQRQLISFARTIVTDPKILI 513
Cdd:cd03231 80 HAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWI 148
|
170
....*....|....*...
gi 1027832812 514 LDEATANVDTETEEMIQT 531
Cdd:cd03231 149 LDEPTTALDKAGVARFAE 166
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
110-328 |
3.10e-08 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. 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). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 55.42 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 110 VRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWAL-FNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLA 188
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALnANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 189 VTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQE----HRINGEFDHTNDayFKTRQAMIRTNSLLLSPL 264
Cdd:cd18590 151 IAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEeeeaCRYSEALERTYN--LKDRRDTVRAVYLLVRRV 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1027832812 265 IDLFyalgtVMVLGIFGVRGL--NGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18590 229 LQLG-----VQVLMLYCGRQLiqSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
371-566 |
3.54e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 371 KDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREY-PAEEL----------RQKMGLVLQEPF- 438
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLarglvylpedRQSSGLYLDAPLa 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 439 -----MFYGDINSNIRMFNDQISDEQVQAA--ARFVKADDFINDLpenyqsrviergasySSGQRQLISFARTIVTDPKI 511
Cdd:PRK15439 360 wnvcaLTHNRRGFWIKPARENAVLERYRRAlnIKFNHAEQAARTL---------------SGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 512 LILDEATANVDTETEEMIQTGLDRI-QENRTTIAIAHRLSTI-QNADLILVLNQGKI 566
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
39-319 |
6.28e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 54.39 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 39 IVFSGLISVVNIYLPRVLQTFIDHYLKTG--HATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVrrqmFA 116
Cdd:cd18567 8 LLLSLALELFALASPLYLQLVIDEVIVSGdrDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNL----FR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 117 KLHRMGMRYFDQVPGGSILSRltndtmsfsnFWALF---NTLFTAFFA-------VISSFVAMYLTDAQIALWLLVFMPF 186
Cdd:cd18567 84 HLLRLPLSYFEKRHLGDIVSR----------FGSLDeiqQTLTTGFVEalldglmAILTLVMMFLYSPKLALIVLAAVAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 187 LAVTIWYYqryssrvYRRMRERLSEL-------NTKLSEAITGISVIQQF-RQEHRINGEFDHTNDayfkTRQAMIRTN- 257
Cdd:cd18567 154 YALLRLAL-------YPPLRRATEEQivasakeQSHFLETIRGIQTIKLFgREAEREARWLNLLVD----AINADIRLQr 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 258 -SLLLSPLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQ 319
Cdd:cd18567 223 lQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKLFELR 285
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
39-328 |
6.96e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 54.49 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 39 IVFSGLISVVNIYLPRVLQTFIDHYLKtgHATVPVMWYFA-GLYFFGMVvRALMQFVQNFSSTmgaeYMLENVRRQMFAK 117
Cdd:cd18568 8 LLASLLLQLLGLALPLFTQIILDRVLV--HKNISLLNLILiGLLIVGIF-QILLSAVRQYLLD----YFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 118 L--H--RMGMRYFDQVPGGSILSR----------LTNDTMSfsnfwALFNTLFtaffaVISSFVAMYLTDAQIALWLLVF 183
Cdd:cd18568 81 FykHllSLPLSFFASRKVGDIITRfqenqkirrfLTRSALT-----TILDLLM-----VFIYLGLMFYYNLQLTLIVLAF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 184 MPFLAVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRI----NGEFDHTNDAYFKTRQAMIRtnsl 259
Cdd:cd18568 151 IPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIrwrwENKFAKALNTRFRGQKLSIV---- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 260 lLSPLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18568 227 -LQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
298-550 |
1.32e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.75 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 298 ITYLNNFYNPMTSMMDNLSDFQDGVVAGSRVLRVMDDPTIAPAQHVDPTAKITR---GKIEFRHVTFAYDGQHPVLKDVS 374
Cdd:TIGR00954 393 MTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEyqdNGIKFENIPLVTPNGDVLIESLS 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 375 FVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRdireypaeelrQKMGLVLQEPFMfygdinsNIRMFNDQ 454
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYM-------TLGTLRDQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 455 I--SDEQVQAAARFVKADDFINDLPENYQSRVIERGASYSS----------GQRQLISFARTIVTDPKILILDEATANVD 522
Cdd:TIGR00954 535 IiyPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAvqdwmdvlsgGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
250 260
....*....|....*....|....*...
gi 1027832812 523 TETEEMIQTGLDRIqeNRTTIAIAHRLS 550
Cdd:TIGR00954 615 VDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
350-577 |
1.58e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 350 TRGKIEFRHVTFAYDGqhPVLKDVSFVAEPGQTVALVGQTGSGKTST----INVLMRFYEFQSGEVLIDDrdiREYPAEE 425
Cdd:PRK10418 1 MPQQIELRNIALQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDG---KPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 426 LRQKM-GLVLQEPFMFYGDINS-------NIRMFNDQISDEQVQAAARFVKADDfindlPEnyqsRVIERGASYSSG--- 494
Cdd:PRK10418 76 LRGRKiATIMQNPRSAFNPLHTmhthareTCLALGKPADDATLTAALEAVGLEN-----AA----RVLKLYPFEMSGgml 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 495 QRQLISFArtIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRT--TIAIAHRLSTIQN-ADLILVLNQGKIVERGS 571
Cdd:PRK10418 147 QRMMIALA--LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGD 224
|
....*.
gi 1027832812 572 NDELLQ 577
Cdd:PRK10418 225 VETLFN 230
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
36-287 |
2.09e-07 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 52.80 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 36 IAAIVFSGLISVVNIYLprvLQTFIDHYLKTGHATVPVMWYFAGLyFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQMF 115
Cdd:cd18584 2 VLLGLLAALLIIAQAWL---LARIIAGVFLEGAGLAALLPLLLLL-LAALLLRALLAWAQERLAARAAARVKAELRRRLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 116 AKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALF-NTLFTAFFAVISSFVAMYLTDAQIALWLLVFMP----FLAVT 190
Cdd:cd18584 78 ARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYlPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPliplFMILI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 191 IWYYQRYSSrvyRRMRErLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYfktRQAMIRT------NSLLLspl 264
Cdd:cd18584 158 GKAAQAASR---RQWAA-LSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDY---RRRTMKVlrvaflSSAVL--- 227
|
250 260
....*....|....*....|...
gi 1027832812 265 iDLFYALGTVMVLGIFGVRGLNG 287
Cdd:cd18584 228 -EFFATLSIALVAVYIGFRLLGG 249
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
370-579 |
2.38e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.51 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 370 LKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLiddrdiREYPAEELRQKMGLVLQepfmFYGDINSNIR 449
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD------RNGEVSVIAISAGLSGQ----LTGIENIEFK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 450 MFNDQISDEQVQAAA----RFVKADDFIndlpenYQSRviergASYSSGQRQLISFARTIVTDPKILILDEATANVDtet 525
Cdd:PRK13546 110 MLCMGFKRKEIKAMTpkiiEFSELGEFI------YQPV-----KKYSSGMRAKLGFSINITVNPDILVIDEALSVGD--- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 526 EEMIQTGLDRIQE----NRTTIAIAHRLSTIQN-ADLILVLNQGKIVERGSNDELLQQH 579
Cdd:PRK13546 176 QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKY 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
345-566 |
2.97e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.99 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 345 PTAKITRG-KIEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRdireyPA 423
Cdd:PRK11247 3 NTARLNQGtPLLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 424 EELRQKMGLVLQEPFMF-YGDINSNIRM-FNDQISDEQVQAAARfVKADDFINDLPenyqsrviergASYSSGQRQLISF 501
Cdd:PRK11247 77 AEAREDTRLMFQDARLLpWKKVIDNVGLgLKGQWRDAALQALAA-VGLADRANEWP-----------AALSGGQKQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 502 ARTIVTDPKILILDEATANVDTETE-EMiQTGLDRI--QENRTTIAIAHRLS-TIQNADLILVLNQGKI 566
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRiEM-QDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
35-300 |
3.97e-07 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family 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. 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. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 51.87 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVM----WYFAGLYFFGmvvrALMQFVQNFSSTMGAEYMLENV 110
Cdd:cd18780 2 TIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALnqavLILLGVVLIG----SIATFLRSWLFTLAGERVVARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 111 RRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFwALFN--TLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLA 188
Cdd:cd18780 78 RKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNA-VTVNlsMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 189 VTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLF 268
Cdd:cd18780 157 IGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASG-GFNGFMGAA 235
|
250 260 270
....*....|....*....|....*....|..
gi 1027832812 269 YALGTVMVLGIFGVRGLNGYVAAGVVYAFITY 300
Cdd:cd18780 236 AQLAIVLVLWYGGRLVIDGELTTGLLTSFLLY 267
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
355-568 |
4.66e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 355 EFRHVTFAYDGQHpVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIReYP--AEELRQKMGL 432
Cdd:PRK11288 6 SFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-FAstTAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQE----PFM------FYGDINSNIRMFNDqiSDEQVQAAARFVK-ADDFINDLPENYqsrviergasYSSGQRQLISF 501
Cdd:PRK11288 84 IYQElhlvPEMtvaenlYLGQLPHKGGIVNR--RLLNYEAREQLEHlGVDIDPDTPLKY----------LSIGQRQMVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1027832812 502 ARTIVTDPKILILDEATANVDT-ETEEMIQTGLDRIQENRTTIAIAHRLSTI-QNADLILVLNQGKIVE 568
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
362-522 |
6.92e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 362 AYDGQHP---VLKDVSFVAEPGQTVALVGQTGSGKTS-TINVLMRFY-EFQSGEVLIDDRDIR------------EYpAE 424
Cdd:NF040905 265 VYHPLHPerkVVDDVSLNVRRGEIVGIAGLMGAGRTElAMSVFGRSYgRNISGTVFKDGKEVDvstvsdaidaglAY-VT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 425 ELRQKMGLVLQEpfmfygDINSNIRMFN-DQISDEQV-QAAARFVKADDFINDLpeNYQSRVIERGA-SYSSGQRQLISF 501
Cdd:NF040905 344 EDRKGYGLNLID------DIKRNITLANlGKVSRRGViDENEEIKVAEEYRKKM--NIKTPSVFQKVgNLSGGNQQKVVL 415
|
170 180
....*....|....*....|.
gi 1027832812 502 ARTIVTDPKILILDEATANVD 522
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGID 436
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
370-564 |
8.77e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.55 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 370 LKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYE--FQSGEVLIDDRDIReypaEELRQKMGLVLQepfmfygdinsn 447
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLD----KNFQRSTGYVEQ------------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 448 irmfNDQISDEQ-VQAAARFvkaddfindlpenyqSRVIeRGASYSsgQRQLISFARTIVTDPKILILDEATANVDTETE 526
Cdd:cd03232 87 ----QDVHSPNLtVREALRF---------------SALL-RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1027832812 527 EMIQTGLDRI-QENRTTIAIAHRLS--TIQNADLILVLNQG 564
Cdd:cd03232 145 YNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
354-577 |
9.76e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTfayDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEE-LRQKMGL 432
Cdd:PRK10982 251 LEVRNLT---SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEaINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 433 VLQE--PFMFYGDIN-------SNIRMFNDQI---SDEQVQAAARFVKadDFINDLPENYQSRViergASYSSGQRQLIS 500
Cdd:PRK10982 328 VTEErrSTGIYAYLDigfnsliSNIRNYKNKVgllDNSRMKSDTQWVI--DSMRVKTPGHRTQI----GSLSGGNQQKVI 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 501 FARTIVTDPKILILDEATANVDTETE-EMIQTGLDRIQENRTTIAIAHRLSTIQN-ADLILVLNQGK---IVE--RGSND 573
Cdd:PRK10982 402 IGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLvagIVDtkTTTQN 481
|
....
gi 1027832812 574 ELLQ 577
Cdd:PRK10982 482 EILR 485
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
38-331 |
1.37e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 50.24 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 38 AIVFSGLISVVNIYLPRVLQTFIDHYLKTGHAtvPVMWYFAGlyffGMVVRALMQFVqnfsSTMGAEYMLENVRRQM--- 114
Cdd:cd18779 7 ILLASLLLQLLGLALPLLTGVLVDRVIPRGDR--DLLGVLGL----GLAALVLTQLL----AGLLRSHLLLRLRTRLdtq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 115 -----FAKLHRMGMRYFDQVPGGSILSR----------LTNDTMSfsnfwALFNTLFtaffaVISSFVAMYLTDAQIALW 179
Cdd:cd18779 77 ltlgfLEHLLRLPYRFFQQRSTGDLLMRlssnatirelLTSQTLS-----ALLDGTL-----VLGYLALLFAQSPLLGLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 180 LLVFMPFLAVTIWYYQRyssRVYRRMRERL---SELNTKLSEAITGISVIQQFRQEHRIngeFDHTNDAYFKTRQAMIRT 256
Cdd:cd18779 147 VLGLAALQVALLLATRR---RVRELMARELaaqAEAQSYLVEALSGIETLKASGAEDRA---LDRWSNLFVDQLNASLRR 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1027832812 257 NSL--LLSPLIDLFYALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQdgvVAGSRVLRV 331
Cdd:cd18779 221 GRLdaLVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQ---LLGSHLERL 294
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
38-308 |
1.51e-06 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 50.19 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 38 AIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQMFAK 117
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 118 LHRMGMRYFDQVPGGSILSRLTNDTMSFSNF--WALFNTLFTAFFAVISSFVAMYLTDAQIALWLLV-FMPFLAVTIWyY 194
Cdd:cd18582 81 LHSLSLRFHLSRKTGALSRAIERGTRGIEFLlrFLLFNILPTILELLLVCGILWYLYGWSYALITLVtVALYVAFTIK-V 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 195 QRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYfktRQAMIRTNSLL--LSPLIDLFYALG 272
Cdd:cd18582 160 TEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKY---EKAAVKSQTSLalLNIGQALIISLG 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 1027832812 273 --TVMVLGIFGVrgLNGYVAAGVVYAFITYLNNFYNPM 308
Cdd:cd18582 237 ltAIMLLAAQGV--VAGTLTVGDFVLVNTYLLQLYQPL 272
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
369-558 |
1.54e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.10 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 369 VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIRE-------YPAEELRQKMGLVLQEPFMFY 441
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiakpyctYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 442 GDInsnirmFNdqiSDEQVQAAARFVKADDFINdlpenyqsrviERGASYSSGQRQLISFARTIVTDPKILILDEATANV 521
Cdd:PRK13541 95 SEI------YN---SAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1027832812 522 DTETEEMIQTgLDRIQENRTTIAI--AHRLSTIQNADLI 558
Cdd:PRK13541 155 SKENRDLLNN-LIVMKANSGGIVLlsSHLESSIKSAQIL 192
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
38-311 |
1.73e-06 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 49.92 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 38 AIVFSGLISVVNIYLPRVLQTFIDHYLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQMFAK 117
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 118 LHRMGMRYFDQVPGGSILSRL------TNDTMSFSNFWaLFNTLFTAfFAVISSFVAMYltDAQIALWLLVFMP-FLAVT 190
Cdd:cd18560 81 LHSLSLDWHLSKKTGEVVRIMdrgtesANTLLSYLVFY-LVPTLLEL-IVVSVVFAFHF--GAWLALIVFLSVLlYGVFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 191 IWYYQ-RYSSRvyRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIrtNSL-LLSPLIDLF 268
Cdd:cd18560 157 IKVTEwRTKFR--RAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQ--ASLsLLNVGQQLI 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1027832812 269 YALGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSM 311
Cdd:cd18560 233 IQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFL 275
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
110-328 |
1.97e-06 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the 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 the ABC_6TM exporter 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.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 50.00 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 110 VRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWAL-FNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLA 188
Cdd:cd18784 71 IRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLnLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 189 VTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEhriNGEF----DHTNDAY-FKTRQAMIRTNSLLLSP 263
Cdd:cd18784 151 IVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANE---DGEAnrysEKLKDTYkLKIKEALAYGGYVWSNE 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 264 LIDLfyALgTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18784 228 LTEL--AL-TVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
38-234 |
2.09e-06 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 49.85 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 38 AIVFSGLISVVNIYLPRVLQTFID---HYLK-TGHATVPVMW----YFAGLYffgmVVRALMQFVQ-NFSSTMGaEYMLE 108
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNvisRSLKeTNGDFIEDLKkpalKLLGLY----LLQSLLTFAYiSLLSVVG-ERVAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 109 NVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSF-SNFWALFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFMPFL 187
Cdd:cd18574 76 RLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFkSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1027832812 188 AVTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHR 234
Cdd:cd18574 156 VLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDR 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
344-581 |
2.37e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 344 DPTAKITRGKIEFRHVTFAYDGQhPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEV-LIDDRDIREYP 422
Cdd:PRK15064 310 EQDKKLHRNALEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 423 ---AEELRQKMGLVlqepfmfygDINSNIRMFNDqisDEQVQAAA--RFVKADDFINDlpenyQSRVIergasySSGQRQ 497
Cdd:PRK15064 389 qdhAYDFENDLTLF---------DWMSQWRQEGD---DEQAVRGTlgRLLFSQDDIKK-----SVKVL------SGGEKG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 498 LISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQEnrTTIAIAH-R--LSTIqnADLILVLNQGKIVE-RGSND 573
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHdRefVSSL--ATRIIEITPDGVVDfSGTYE 521
|
....*...
gi 1027832812 574 ELLQQHGY 581
Cdd:PRK15064 522 EYLRSQGI 529
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
365-519 |
6.46e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.11 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 365 GQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINV---LMRFYEfqsGEVLIDDRDIREYPaEELRQKMglvlqepfMFY 441
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRIlagLARPDA---GEVLWQGEPIRRQR-DEYHQDL--------LYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 442 GD---INS------NIRMF---NDQISDEQVQAAARFVKADDFiNDLPenyqsrviergASY-SSGQRQLISFARTIVTD 508
Cdd:PRK13538 80 GHqpgIKTeltaleNLRFYqrlHGPGDDEALWEALAQVGLAGF-EDVP-----------VRQlSAGQQRRVALARLWLTR 147
|
170
....*....|..
gi 1027832812 509 PKILILDEA-TA 519
Cdd:PRK13538 148 APLWILDEPfTA 159
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
72-233 |
9.49e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 47.94 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 72 PVMWYFAGLYFFGMVVRALMQFVQNFSS---TMGAEYMLENvrrQMFAKLHRMGMRYFDQVPGGSILSRLTNDT------ 142
Cdd:cd18599 55 PDLNFYQLVYGGSILVILLLSLIRGFVFvkvTLRASSRLHN---KLFQKILRSPMSFFDTTPTGRILNRFSKDLdevdvr 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 143 --MSFSNFWALFNTLFTAFFAVISSFVamyltdaqialWLLVFMPFLAVTIWYYQRYSSRVYRRMReRL-----SELNTK 215
Cdd:cd18599 132 lpFTLENFLQNVLLVVFSLIIIAIVFP-----------WFLIALIPLAIIFVFLSKIFRRAIRELK-RLenisrSPLFSH 199
|
170
....*....|....*...
gi 1027832812 216 LSEAITGISVIQQFRQEH 233
Cdd:cd18599 200 LTATIQGLSTIHAFNKEK 217
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
36-328 |
9.56e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 47.59 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 36 IAAIVFSGLISVVNIYLPRVLQTFIDHYLktGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQMF 115
Cdd:cd18782 5 IEVLALSFVVQLLGLANPLLFQVIIDKVL--VQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 116 AKLHRMGMRYFDQVPGGSILSRLtNDTMSFSNFwaLFNTLFTAFFAVISSFVA---MYLTDAQIALWLLVFMPFLAVTIW 192
Cdd:cd18782 83 DHLLRLPLGFFDKRPVGELSTRI-SELDTIRGF--LTGTALTTLLDVLFSVIYiavLFSYSPLLTLVVLATVPLQLLLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 193 YYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAY----FKTRqaMIRTNSLLLSPLIDLf 268
Cdd:cd18782 160 LFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSlgegFKLT--VLGTTSGSLSQFLNK- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 269 yaLGTVMVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMTSMMDNLSDFQDGVVAGSRV 328
Cdd:cd18782 237 --LSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
367-567 |
2.69e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 45.33 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 367 HPVLKDVSFVAEPGQTVALVGQTGSGKTS---TINVLMRFYEFQSGEVLIDDrdireYPAEELRQKmglvlqepfmFYGD 443
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNG-----IPYKEFAEK----------YPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 444 InsnirMFNDQiSDEQ-----VQAAARFV---KADDFIndlpenyqsRVIergasySSGQRQLISFARTIVTDPKILILD 515
Cdd:cd03233 85 I-----IYVSE-EDVHfptltVRETLDFAlrcKGNEFV---------RGI------SGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 516 EATANVDTETE-EMIQtgldRIQenrtTIAIAHRLSTI----QNA-------DLILVLNQGKIV 567
Cdd:cd03233 144 NSTRGLDSSTAlEILK----CIR----TMADVLKTTTFvslyQASdeiydlfDKVLVLYEGRQI 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
354-563 |
2.89e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 45.88 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 354 IEFRHVTFAYdGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEELRQKMGLV 433
Cdd:PRK09544 5 VSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 434 LQ-EPFMfygdinsnirMFNDQISDEQVQAAARFVKADDFInDLPENyqsrviergaSYSSGQRQLISFARTIVTDPKIL 512
Cdd:PRK09544 84 LTvNRFL----------RLRPGTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1027832812 513 ILDEATANVDTETEEMIQTGLDRIQE--NRTTIAIAHRLSTIQ-NADLILVLNQ 563
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLNH 196
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
492-587 |
3.15e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.33 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 492 SSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRI-QENRTTI-AIAHRLSTI-QNADLILVLNQGKIVE 568
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTIlLISHDLQMLsQWADKINVLYCGQTVE 239
|
90 100
....*....|....*....|.
gi 1027832812 569 RGSNDELLQ--QHGYYYDMIQ 587
Cdd:PRK15093 240 TAPSKELVTtpHHPYTQALIR 260
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
368-566 |
7.33e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 368 PVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIR-EYPAEEL----------RQKMGLVLQe 436
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLangivyisedRKRDGLVLG- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 437 pfMfygDINSNIRMFN-DQISDE--QVQAAARFVKADDFINDLPENYQSRVIERGaSYSSGQRQLISFARTIVTDPKILI 513
Cdd:PRK10762 345 --M---SVKENMSLTAlRYFSRAggSLKHADEQQAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1027832812 514 LDEATANVDTETEEMIQTGLDRI-QENRTTIAIAHRLSTIQN-ADLILVLNQGKI 566
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFkAEGLSIILVSSEMPEVLGmSDRILVMHEGRI 473
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
355-567 |
7.61e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.40 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 355 EFRHVTFAYDGQHPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLIDDRDIREYPAEEL-------- 426
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlgvayi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 427 ---RQKMGLVL--------------QEPFmfygdiNSNIRMFNDQISDEQVQAAARF-VKADDfindlpenyqsrvIERG 488
Cdd:COG3845 339 pedRLGRGLVPdmsvaenlilgryrRPPF------SRGGFLDRKAIRAFAEELIEEFdVRTPG-------------PDTP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 489 ASYSSG---QRQLIsfARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTI-----------AIAHRlstiqn 554
Cdd:COG3845 400 ARSLSGgnqQKVIL--ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVllisedldeilALSDR------ 471
|
250
....*....|...
gi 1027832812 555 adlILVLNQGKIV 567
Cdd:COG3845 472 ---IAVMYEGRIV 481
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
353-582 |
1.19e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 353 KIEFRHVTFAY------------------DGQ-HPVLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVli 413
Cdd:PRK13545 4 KVKFEHVTKKYkmynkpfdklkdlffrskDGEyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 414 ddrDIREyPAEELRQKMGLVLQepfmFYGDINSNIRMFNDQISDEQVQAAA----RFVKADDFINdlpenyqsrviERGA 489
Cdd:PRK13545 82 ---DIKG-SAALIAISSGLNGQ----LTGIENIELKGLMMGLTKEKIKEIIpeiiEFADIGKFIY-----------QPVK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 490 SYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTI-AIAHRLSTIQN-ADLILVLNQGKIV 567
Cdd:PRK13545 143 TYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIfFISHSLSQVKSfCTKALWLHYGQVK 222
|
250
....*....|....*
gi 1027832812 568 ERGSNDELLQQHGYY 582
Cdd:PRK13545 223 EYGDIKEVVDHYDEF 237
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
108-247 |
1.46e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 44.23 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 108 ENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDtMSFsnfwaLFNTLFTAFFAVISSF---VAMYLTDAQIALWLLVFM 184
Cdd:cd18601 92 KNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKD-IGH-----LDDLLPLTFLDFLQLLlqvVGVVLLAVVVNPWVLIPV 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1027832812 185 PFLAVTIWYYQRYSSRVYRRMReRL-----SELNTKLSEAITGISVIQQFRQEHRINGEFD-----HTnDAYF 247
Cdd:cd18601 166 IPLVILFLFLRRYYLKTSREVK-RIegttrSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDahqdlHS-EAWF 236
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
47-319 |
5.09e-04 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 42.52 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 47 VVNIYLPRVLQTFIDHyLKTGHATVPvmWYFAGLYffgmvvrALMQFVQNfSSTMGA----------EYMLENVRRQMFA 116
Cdd:cd18583 10 VLNVLVPRQLGIIVDS-LSGGSGKSP--WKEIGLY-------VLLRFLQS-GGGLGLlrswlwipveQYSYRALSTAAFN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 117 KLHRMGMRYFDQ---------VPGGSILSRLTNdtmsfsnfWALFNTLFTAFFAVISSFVAMYLTDAQIALWLLVFM-PF 186
Cdd:cd18583 79 HVMNLSMDFHDSkksgevlkaIEQGSSINDLLE--------QILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMvLY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 187 LAVTIwYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRingEFDHTNDAyFKTRQAMIRTNSLLLSpLID 266
Cdd:cd18583 151 VWSTI-KLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPY---EKERYREA-VKNYQKAERKYLFSLN-LLN 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 267 LFYALgtVMVLGIFGVRGLNGY-VAAG-------VVyaFITYLNNFYNPMTSMMDNLSDFQ 319
Cdd:cd18583 225 AVQSL--ILTLGLLAGCFLAAYqVSQGqatvgdfVT--LLTYWAQLSGPLNFFATLYRSIQ 281
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
76-329 |
5.44e-04 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 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 type 3 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 42.20 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 76 YFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALFNTL 155
Cdd:cd18559 39 VYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 156 FTAFFAVIssfVAMYLTDAQIALWLLVFMPfLAVTIWYYQRY---SSRVYRRMRERLSELNTKL-SEAITGISVIQQFRQ 231
Cdd:cd18559 119 WMGPLQNV---IGLYLLILLAGPMAAVGIP-LGLLYVPVNRVyaaSSRQLKRLESVSKDPRYKLfNETLLGISVIKAFEW 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 232 EHRingefdhtndayFKTRQAMIRTNSLLLSPLIDLFYALGT--------VMVLGIF----GVRGLNGYVAAGVVY--AF 297
Cdd:cd18559 195 EEA------------FIRQVDAKRDNELAYLPSIVYLRALAVrlwcvgpcIVLFASFfayvSRHSLAGLVALKVFYslAL 262
|
250 260 270
....*....|....*....|....*....|..
gi 1027832812 298 ITYLNNFYNpMTSMMDNlsdfqdGVVAGSRVL 329
Cdd:cd18559 263 TTYLNWPLN-MSPEVIT------NIVAAEVSL 287
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
372-580 |
5.65e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 372 DVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVL-----IDDRDIreypaeELRQKMGLVLQEpFMFYGD--I 444
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDI------ATRRRVGYMSQA-FSLYGEltV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 445 NSNI----RMFndQISDEQV-----QAAARFvKADDFINDLPEnyqsrviergaSYSSGQRQLISFARTIVTDPKILILD 515
Cdd:NF033858 357 RQNLelhaRLF--HLPAAEIaarvaEMLERF-DLADVADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1027832812 516 EATANVDTET-----EEMIQtgLDRiqENRTTIAIA-HRLSTIQNADLILVLNQGKIVERGSNDELLQQHG 580
Cdd:NF033858 423 EPTSGVDPVArdmfwRLLIE--LSR--EDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
488-595 |
5.71e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 488 GASYSSGQRQLISFARTIVTDPKILILDEATANVDTETEEMIQTGLDRIQENRTTIAIAHRL--STIQNADLILVLNQGK 565
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVIDRGR 221
|
90 100 110
....*....|....*....|....*....|
gi 1027832812 566 IVERGSNDELLQQHGYYYDMIQLQNSAHVD 595
Cdd:NF000106 222 VIADGKVDELKTKVGGRTLQIRPAHAAELD 251
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
369-585 |
1.14e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.02 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 369 VLKDVSFVAEPGQTVALVGQTGSGKTSTINVLM-RFYEFQ---SGEVLIDDRDireyPAEELRQKMGLVL-------QEP 437
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsNTDGFHigvEGVITYDGIT----PEEIKKHYRGDVVynaetdvHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 438 FMFYGD-INSNIRMFNDQISDEQVQAAARFVKADDF---INDLPENYQSRV---IERGASysSGQRQLISFARTIVTDPK 510
Cdd:TIGR00956 152 HLTVGEtLDFAARCKTPQNRPDGVSREEYAKHIADVymaTYGLSHTRNTKVgndFVRGVS--GGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 511 ILILDEATANVDTeteemiQTGLDRIQENRTTIAIAHRLSTI------QNA----DLILVLNQGKIVERGSNDELLQqhg 580
Cdd:TIGR00956 230 IQCWDNATRGLDS------ATALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGPADKAKQ--- 300
|
....*
gi 1027832812 581 YYYDM 585
Cdd:TIGR00956 301 YFEKM 305
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
35-287 |
1.20e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 41.03 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 35 FIAAIVFSGLISVVNIYLPRVLQTFIDHYLktGHATVPVMWYFA----GLYFFGMVVRALMQFVQNFSSTMgAEYMLENv 110
Cdd:cd18566 4 LPQVLLASLFINILALATPLFILQVYDRVI--PNESIPTLQVLVigvvIAILLESLLRLLRSYILAWIGAR-FDHRLSN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 111 rrQMFAKLHRMGMRYFDQVPGGSILSRLtNDTMSFSNFWA--LFNTLFTAFFAVISsFVAMYLTDAQIALWLLVFMPFLA 188
Cdd:cd18566 80 --AAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTgqALLALLDLPFVLIF-LGLIWYLGGKLVLVPLVLLGLFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 189 VTIWYYQRYSSRVYRRMRERLSELNTKLSEAITGISVIQQFRQEHRINGEFDHTNDAYFKTRQAMIRTNSlLLSPLIDLF 268
Cdd:cd18566 156 LVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINA-VAQTLGQLF 234
|
250
....*....|....*....
gi 1027832812 269 YALGTVMVLGIFGVRGLNG 287
Cdd:cd18566 235 SQVSMVAVVAFGALLVING 253
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
334-415 |
1.44e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 334 DPTIAPAQHVDPTAKItrgkiefrHVTFAYDGQHpvLKDVSFVAEPGQTVALVGQTGSGKTSTINVLMRFYEFQSGEVLI 413
Cdd:PRK01889 159 EEKIAEVEALAPGVPV--------LAVSALDGEG--LDVLAAWLSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVRE 228
|
..
gi 1027832812 414 DD 415
Cdd:PRK01889 229 DD 230
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
39-204 |
2.11e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the 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 the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 40.21 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 39 IVFSGLIS-VVNIYLPRVLQTFIDhYLKTGHATVPVMWYFAGLYFFGMVVRALMQFVQNFSSTMGAEYMLENVRRQMFAK 117
Cdd:cd18781 1 TVLLQWISlLANIAFVFSIANLLQ-KLLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 118 LHRMGMRYFDQVPGGSILSRLTNDT----MSFSNFWALFntlFTAFFAVISSFVAMYLTDAQIALWLLVFMPFLAVTIWY 193
Cdd:cd18781 80 LLRLGPSYQEKVSTAEVVQLSVEGVeqleIYFGRYLPQF---FYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIA 156
|
170
....*....|.
gi 1027832812 194 YQRYSSRVYRR 204
Cdd:cd18781 157 VQKIAKKLLSK 167
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
86-322 |
2.70e-03 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. 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). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 40.15 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 86 VVRALMQFVQN--FSSTMGAEYmlENVRRQMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSN---------FWALFNT 154
Cdd:cd18589 47 IASAVSEFVCDliYNITMSRIH--SRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSEslsenlsllMWYLARG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 155 LFTAFFAVISSFVAMYLTdaQIALWLLVFMPFLAVTiwYYQRYSSRVyrrmRERLSELNTKLSEAITGISVIQQFRQEhr 234
Cdd:cd18589 125 LFLFIFMLWLSPKLALLT--ALGLPLLLLVPKFVGK--FQQSLAVQV----QKSLARANQVAVETFSAMKTVRSFANE-- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 235 iNGEFDHTNDAYFKTRQ-----AMIRTNSLLLSPLIDLFYALGtvmVLGIFGVRGLNGYVAAGVVYAFITYLNNFYNPMT 309
Cdd:cd18589 195 -EGEAQRYRQRLQKTYRlnkkeAAAYAVSMWTSSFSGLALKVG---ILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVE 270
|
250
....*....|...
gi 1027832812 310 SMMDNLSDFQDGV 322
Cdd:cd18589 271 VLLSYYPSVMKAV 283
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
75-233 |
9.42e-03 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 38.38 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 75 WYFAGLYFFGMVVRALMqfvqnfsSTMgaeymlenvrrqMFAKLHRMGMRYFDQVPGGSILSRLTNDTMSFSNFWALFNT 154
Cdd:cd18594 58 PYFFGLHRYGMQLRIAL-------SSL------------IYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027832812 155 LFTAFFAVIssfVAMYLTDAQIALWLLVFMPFLAVTIwYYQRYSSRVYRRMRERLSELNTK----LSEAITGISVIQQFR 230
Cdd:cd18594 119 LWIAPLQVI---VLTGLLWREIGPSSLAGLGVLLLLL-PLQAYLGKLFAKYRRKTAGLTDErvkiMNEIISGMRVIKMYT 194
|
...
gi 1027832812 231 QEH 233
Cdd:cd18594 195 WEE 197
|
|
| |
