|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-573 |
0e+00 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 931.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 1 MRDLLPYLKLYKKHWFGLSLGMLLAFATLSASIGLLTLSGWFISASAVAGLTIArETFNYMLPGGGVRGLAMSRTAGRWG 80
Cdd:PRK11160 1 MRALLPFLKLYKRHWFMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGL-YSFNYMLPAAGVRGAAIGRTAGRYG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 81 ERVVSHNATFKLLTDLRIFFFKKLAPLIPGRISNLRDADLLNRLVADVDAMDHVYLRLVSPVTVGVFGIFFLTLFLMWFD 160
Cdd:PRK11160 80 ERLVSHDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 161 SSLGLILGSILLIMLLVWPILFYKLGKRNGGELTQNKADLRVTTLDWIEGYSELTLFGAEERYRNAILETQRKLMANQFV 240
Cdd:PRK11160 160 LTLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 241 NANLTGMASAALMLFNGLTLVLMLWLAADGVGGNA-PDPFIALMAFATMASFELLMPIAGAFQHLGQTLSSARRLNEVIL 319
Cdd:PRK11160 240 QANLTGLSQALMILANGLTVVLMLWLAAGGVGGNAqPGALIALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEITE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 320 SEPEVQFAEEKLDINKPLDITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISI 399
Cdd:PRK11160 320 QKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 400 AGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLENNA-LDSWLGDGGRQLSGG 478
Cdd:PRK11160 400 NGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDDKgLNAWLGEGGRQLSGG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 479 EKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEK 558
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQE 559
|
570
....*....|....*
gi 2020526634 559 LLNEAGRYFQLRQAI 573
Cdd:PRK11160 560 LLAQQGRYYQLKQRL 574
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-571 |
0e+00 |
|
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: 702.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 2 RDLLPYLKLYKKHWFGLSLGMLLAFATLSASIGLLTLSGWFISASAVAGLTiaretFNYMLPGGGVRGLAMSRTAGRWGE 81
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPPI-----LNLFVPIVGVRAFAIGRTVFRYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 82 RVVSHNATFKLLTDLRIFFFKKLAPLIPGRISNLRDADLLNRLVADVDAMDHVYLRLVSPVTVGVFGIFFLTLFLMWFDS 161
Cdd:COG4987 76 RLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 162 SLGLILGSILLIMLLVWPILFYKLGKRNGGELTQNKADLRVTTLDWIEGYSELTLFGAEERYRNAILETQRKLMANQFVN 241
Cdd:COG4987 156 ALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 242 ANLTGMASAALMLFNGLTLVLMLWLAADGVGGNA-PDPFIALMAFATMASFELLMPIAGAFQHLGQTLSSARRLNEVILS 320
Cdd:COG4987 236 ARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGAlSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 321 EPEVQFAEEKLDINKPLDITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIA 400
Cdd:COG4987 316 PPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 401 GIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGG 478
Cdd:COG4987 396 GVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAAlpDGLDTWLGEGGRRLSGG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 479 EKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEK 558
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE 555
|
570
....*....|...
gi 2020526634 559 LLNEAGRYFQLRQ 571
Cdd:COG4987 556 LLAQNGRYRQLYQ 568
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-533 |
3.23e-129 |
|
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: 388.64 E-value: 3.23e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 4 LLPYLKLYKKHWFGLSLGMLLAFATLSASIGLLTLSGWFISASAVAGLTIAretfnYMLPGGGVRGLAMSRTAGRWGERV 83
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLY-----LSVAAVAVRAFGIGRAVFRYLERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 84 VSHNATFKLLTDLRIFFFKKLAPLIPGRISNLRDADLLNRLVADVDAMDHVYLRLVSPVTVGVFGIFFLTLFLMWFDSSL 163
Cdd:TIGR02868 76 VGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 164 GLILGSILLIMLLVWPILFYKLGKRNGGELTQNKADLRVTTLDWIEGYSELTLFGAEERYRNAILETQRKLMANQFVNAN 243
Cdd:TIGR02868 156 ALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 244 LTGMASAALMLFNGLTLVLMLWLAADGVGGNAPDP-FIALMAFATMASFELLMPIAGAFQHLGQTLSSARRLNEVILSEP 322
Cdd:TIGR02868 236 ATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPvTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 323 EVQFAEEKLDINKPLD---ITFSNVTFNYPDSERnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISI 399
Cdd:TIGR02868 316 PVAEGSAPAAGAVGLGkptLELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 400 AGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSG 477
Cdd:TIGR02868 395 DGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRAlpDGLDTVLGEGGARLSG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 478 GEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRL 533
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
25-315 |
2.09e-127 |
|
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: 374.89 E-value: 2.09e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 25 AFATLSASIGLLTLSGWFISASAVAGLTIAreTFNYMLPGGGVRGLAMSRTAGRWGERVVSHNATFKLLTDLRIFFFKKL 104
Cdd:cd18585 1 GLLTLLASIGLLALSGWFISAAALAGLAAP--TFNYFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 105 APLIPGRISNLRDADLLNRLVADVDAMDHVYLRLVSPVTVGVFGIFFLTLFLMWFDSSLGLILGSILLIMLLVWPILFYK 184
Cdd:cd18585 79 EPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 185 LGKRNGGELTQNKADLRVTTLDWIEGYSELTLFGAEERYRNAILETQRKLMANQFVNANLTGMASAALMLFNGLTLVLML 264
Cdd:cd18585 159 LGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 265 WLAADGV-GGNAPDPFIALMAFATMASFELLMPIAGAFQHLGQTLSSARRLN 315
Cdd:cd18585 239 WLGAPLVqNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRLF 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-569 |
2.84e-113 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 349.08 E-value: 2.84e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 1 MRDLLPYLKLYKKHwfgLSLGMLLAFATLSASIGLLTLSGWFISAsavaglTIARETFNYMLP-GGGVRGLAMSRTAGRW 79
Cdd:COG1132 9 LRRLLRYLRPYRGL---LILALLLLLLSALLELLLPLLLGRIIDA------LLAGGDLSALLLlLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 80 GERVVSHNATFKLLTDLRIFFFKKLAPLIPGRISNLRDADLLNRLVADVDAMDHVYLRLVSPVTVGVFGIFFLTLFLMWF 159
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 160 DsslglilgsillimllvWP----------------ILFYKLGKRNGGELTQNKADLRVTTLDWIEGYSELTLFGAEERY 223
Cdd:COG1132 160 D-----------------WRlalivllvlpllllvlRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 224 RNAILETQRKLMANQFVNANLTGMASAALMLFNGLTLVLMLWLAADGVGGNAPDP--FIALMAFATMAsFELLMPIAGAF 301
Cdd:COG1132 223 LERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVgdLVAFILYLLRL-FGPLRQLANVL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 302 QHLGQTLSSARRLNEVILSEPEVQFAEEKLDI-NKPLDITFSNVTFNYPDsERNVLNAVDLTIPATNKVAIVGQTGSGKS 380
Cdd:COG1132 302 NQLQRALASAERIFELLDEPPEIPDPPGAVPLpPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 381 TLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLE 460
Cdd:COG1132 381 TLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 461 N--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLES 538
Cdd:COG1132 461 AlpDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRN 540
|
570 580 590
....*....|....*....|....*....|.
gi 2020526634 539 MDSIVLIEQGEIVENGSHEKLLNEAGRYFQL 569
Cdd:COG1132 541 ADRILVLDDGRIVEQGTHEELLARGGLYARL 571
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-571 |
3.19e-95 |
|
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: 305.99 E-value: 3.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 2 RDLLPYLKLYKKH-WFGLSLGMLLAFATLSASIGLLTL----------SGWFISASAVAGLTIARETFNYMlpgggvRGL 70
Cdd:COG2274 145 RWFLRLLRRYRRLlLQVLLASLLINLLALATPLFTQVVidrvlpnqdlSTLWVLAIGLLLALLFEGLLRLL------RSY 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 71 AMSRTAGR----WGERVVSHnatfklLTDLRIFFFKKlaplipgrisnlRDA-DLLNRLvadvdaMDHVYLR--LVSPVT 143
Cdd:COG2274 219 LLLRLGQRidlrLSSRFFRH------LLRLPLSFFES------------RSVgDLASRF------RDVESIRefLTGSLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 144 VGVFGIFFLTLFL--MWFDSSLGLILGSILLIMLLVWPILFYKLGKRNGGELTQNKADLRVTTLDWIEGYSELTLFGAEE 221
Cdd:COG2274 275 TALLDLLFVLIFLivLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAES 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 222 RYRNAILETQRKLMANQFVNANLTGMASAALMLFNGLTLVLMLWLAA----DG---VGgnapdpfiALMAFATMASFeLL 294
Cdd:COG2274 355 RFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAylviDGqltLG--------QLIAFNILSGR-FL 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 295 MPI---AGAFQHLGQTLSSARRLNEVILSEPEVQFAEEKLDINKPL-DITFSNVTFNYPDSERNVLNAVDLTIPATNKVA 370
Cdd:COG2274 426 APVaqlIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKgDIELENVSFRYPGDSPPVLDNISLTIKPGERVA 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 371 IVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDDHLANIL 450
Cdd:COG2274 506 IVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAA 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 451 KDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIF 528
Cdd:COG2274 586 RLAGLHDFIEAlpMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVII 665
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2020526634 529 ITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQLRQ 571
Cdd:COG2274 666 IAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-564 |
1.42e-90 |
|
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: 289.74 E-value: 1.42e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 2 RDLLPYLKLYKKHwfgLSLGMLLAFATLSASIGLLtlsgWFIsASAVAGLTIARETFNYMLPG-GGVRGLAMSRTAGRWG 80
Cdd:COG4988 6 KRLKRLARGARRW---LALAVLLGLLSGLLIIAQA----WLL-ASLLAGLIIGGAPLSALLPLlGLLLAVLLLRALLAWL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 81 ERVVSHNATFKLLTDLRIFFFKKLAPLIPGRISNLRDADLLNRLVADVDAMDH--------VYLRLVSPVTVGVF----- 147
Cdd:COG4988 78 RERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfarylpqLFLAALVPLLILVAvfpld 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 148 ----GIFFLTLFL----MWFdsslglilgsillimllvWPILFYKLGKRNGGELTQNKADLrvttLDWIEGYSELTLFGA 219
Cdd:COG4988 158 wlsgLILLVTAPLiplfMIL------------------VGKGAAKASRRQWRALARLSGHF----LDRLRGLTTLKLFGR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 220 EERYRNAILET-----QR--KLMANQFVNA---NLTGMASAAL-MLFNGLTLVlmlwlaadgvgGNAPDPFIALmaFATM 288
Cdd:COG4988 216 AKAEAERIAEAsedfrKRtmKVLRVAFLSSavlEFFASLSIALvAVYIGFRLL-----------GGSLTLFAAL--FVLL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 289 ASFELLMPI--AGAFQHLGQT-LSSARRLNEVI-LSEPEVQFAEEKLDINKPLDITFSNVTFNYPDsERNVLNAVDLTIP 364
Cdd:COG4988 283 LAPEFFLPLrdLGSFYHARANgIAAAEKIFALLdAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPG-GRPALDGLSLTIP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 365 ATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDD 444
Cdd:COG4988 362 PGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 445 HLANILKDVGLEKLLE--NNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE 522
Cdd:COG4988 442 ELEAALEAAGLDEFVAalPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK 521
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2020526634 523 GKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAG 564
Cdd:COG4988 522 GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
339-572 |
6.73e-69 |
|
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: 222.49 E-value: 6.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDsERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:cd03253 1 IEFENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPIL 496
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRfpDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 497 LLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQLRQA 572
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
339-570 |
2.01e-68 |
|
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: 220.95 E-value: 2.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPIL 496
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMElpEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 497 LLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQLR 570
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
338-560 |
1.03e-67 |
|
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: 219.02 E-value: 1.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNYpDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESIS 417
Cdd:cd03254 2 EIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPI 495
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKlpNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 496 LLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLL 560
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
339-549 |
3.77e-67 |
|
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: 215.32 E-value: 3.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLliarpeatddhlanilkdvglekllennaldswlgdggrqLSGGEKRRIGIARAILHDAPILLL 498
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 499 DEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGE 549
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
339-572 |
9.91e-66 |
|
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: 213.94 E-value: 9.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPD-SERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESIS 417
Cdd:cd03249 1 IEFKNVSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPI 495
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSlpDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 496 LLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQLRQA 572
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-570 |
3.57e-65 |
|
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: 222.67 E-value: 3.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 2 RDLLPYLKLYKKHWFGLSLGMLLAFATLSASIGLLT--LSGWFISASAVAGLTiaretfnymLPGGGVrGLAMSRTAGRW 79
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKplLDDGFGGRDRSVLWW---------VPLVVI-GLAVLRGICSF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 80 GERVVSHNATFKLLTDLRIFFFKKLAPLIPGRISNLRDADLLNRLVADVDAMDHVYLRLVSPVTVGVFGIFFLTLFLMWF 159
Cdd:TIGR02203 73 VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 160 DSSLGLILGSILLIMLLVWPILFYKLgkRNGGELTQNK-ADLRVTTLDWIEGYSELTLFGAEERYRNAILETQRKLMANQ 238
Cdd:TIGR02203 153 SWQLTLIVVVMLPVLSILMRRVSKRL--RRISKEIQNSmGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 239 FVNANLTGMASAALMLFNGLTLVLMLWLAA--DGVGGNAPDPFIALMA--FATMASFELLMPIAGAFQhlgQTLSSARRL 314
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLFIALfqAQAGSLTAGDFTAFITamIALIRPLKSLTNVNAPMQ---RGLAAAESL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 315 NEVILSEPEVQFAEEKLDINKPlDITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKK 394
Cdd:TIGR02203 308 FTLLDSPPEKDTGTRAIERARG-DVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 395 GYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDD-HLANILKDVGLEKLLEN--NALDSWLGDG 471
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRaEIERALAAAYAQDFVDKlpLGLDTPIGEN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 472 GRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIV 551
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
570
....*....|....*....
gi 2020526634 552 ENGSHEKLLNEAGRYFQLR 570
Cdd:TIGR02203 547 ERGTHNELLARNGLYAQLH 565
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
208-560 |
8.06e-63 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 218.97 E-value: 8.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 208 IEGYSELTLFGAE----ERYRNAILETQRKLMANQFVNANLTGMASAALMLFNGLTLVLMLWLAADG---VGGnapdpFI 280
Cdd:TIGR03375 331 LSGLETIKALNAEgrfqRRWEQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGeltMGG-----LI 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 281 AlmafATMASFELLMP---IAGAFQHLGQTLSSARRLNEvILSEPeVQFAEEKLDINKPL---DITFSNVTFNYPDSERN 354
Cdd:TIGR03375 406 A----CVMLSGRALAPlgqLAGLLTRYQQAKTALQSLDE-LMQLP-VERPEGTRFLHRPRlqgEIEFRNVSFAYPGQETP 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNL 434
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNI 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 435 LIARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHS 512
Cdd:TIGR03375 560 ALGAPYADDEEILRAAELAGVTEFVRRhpDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEER 639
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2020526634 513 IMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLL 560
Cdd:TIGR03375 640 FKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVL 687
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
339-554 |
3.10e-62 |
|
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: 202.93 E-value: 3.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWnESQLRESISV 418
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLliarpeatddhlanilkdvglekllennaldswlgdgGRQLSGGEKRRIGIARAILHDAPILLL 498
Cdd:cd03247 80 LNQRPYLFDTTLRNNL-------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 499 DEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENG 554
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-545 |
3.66e-61 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 210.99 E-value: 3.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 18 LSLGMLLAFATLSASIglltLSGWFISASAVAGLTIAretfnymlpGGGVRGLAMSRTAGRWGERVVSHNATFKLLTDLR 97
Cdd:TIGR02857 14 LGALLIIAQAWLLARV----VDGLISAGEPLAELLPA---------LGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 98 IFFFKKLAPLIPGRISNLRDADLLNRLVADVDAMDHVYLR--------LVSPVTVGVF---------GIFFLTLFLMwfd 160
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARylpqlvlaVIVPLAILAAvfpqdwisgLILLLTAPLI--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 161 sslglilgsillimllvwPILFYKLGKRnggelTQNKAD--LRVTT------LDWIEGYSELTLFGAEERYRNAILETQR 232
Cdd:TIGR02857 158 ------------------PIFMILIGWA-----AQAAARkqWAALSrlsghfLDRLRGLPTLKLFGRAKAQAAAIRRSSE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 233 KLMANQFVNANLTGMASAALMLFNGLTLVLM-----LWLAADGVggnapDPFIALmaFATMASFELLMPI--AGAFQHLG 305
Cdd:TIGR02857 215 EYRERTMRVLRIAFLSSAVLELFATLSVALVavyigFRLLAGDL-----DLATGL--FVLLLAPEFYLPLrqLGAQYHAR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 306 QT-LSSARRLNEVILSEPEVQFAEEKLDINKPLDITFSNVTFNYPDsERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQ 384
Cdd:TIGR02857 288 ADgVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPG-RRPALRPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 385 LLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLEN--N 462
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAlpQ 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 463 ALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSI 542
Cdd:TIGR02857 447 GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRI 526
|
...
gi 2020526634 543 VLI 545
Cdd:TIGR02857 527 VVL 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
217-572 |
9.37e-61 |
|
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: 211.60 E-value: 9.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 217 FGAEER-----------YRNAILETQRKLMANQFVNANLTGMAsaalmlfngltLVLMLWLAADGV--GGNAPDPFIALM 283
Cdd:COG5265 234 FGNEARearrydealarYERAAVKSQTSLALLNFGQALIIALG-----------LTAMMLMAAQGVvaGTMTVGDFVLVN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 284 AFAtmasFELLMPIagafQHLG-------QTLSSARRLNEVILSEPEVQFAEE--KLDINKPlDITFSNVTFNYpDSERN 354
Cdd:COG5265 303 AYL----IQLYIPL----NFLGfvyreirQALADMERMFDLLDQPPEVADAPDapPLVVGGG-EVRFENVSFGY-DPERP 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNL 434
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 435 LIARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHS 512
Cdd:COG5265 453 AYGRPDASEEEVEAAARAAQIHDFIESlpDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA 532
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 513 IMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQL--RQA 572
Cdd:COG5265 533 IQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMwaRQQ 594
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
338-554 |
5.72e-60 |
|
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: 198.20 E-value: 5.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESIS 417
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPI 495
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKhpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 496 LLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENG 554
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
338-569 |
3.45e-58 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 204.10 E-value: 3.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESIS 417
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRVDILNGTLRDNLLIARPE----------ATDDHLANILkdvglEKLleNNALDSWLGDGGRQLSGGEKRRIGIAR 487
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARTEqysreqieeaARMAYAMDFI-----NKM--DNGLDTVIGENGVLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 488 AILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYF 567
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYA 573
|
..
gi 2020526634 568 QL 569
Cdd:PRK11176 574 QL 575
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
244-572 |
1.56e-55 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 197.11 E-value: 1.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 244 LTGMASAALMLfngLTLVLMLWLAADG---VGgnapdPFIALMAFATMasfeLLMPIAGAFQHLGQTLSSARRLNEVILS 320
Cdd:PRK13657 245 LNRAASTITML---AILVLGAALVQKGqlrVG-----EVVAFVGFATL----LIGRLDQVVAFINQVFMAAPKLEEFFEV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 321 EPEVQFAEEKLDiNKPL-----DITFSNVTFNYPDSERNVLNaVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKG 395
Cdd:PRK13657 313 EDAVPDVRDPPG-AIDLgrvkgAVEFDDVSFSYDNSRQGVED-VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 396 YISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLENNA--LDSWLGDGGR 473
Cdd:PRK13657 391 RILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPdgYDTVVGERGR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 474 QLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVEN 553
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVES 550
|
330
....*....|....*....
gi 2020526634 554 GSHEKLLNEAGRYFQLRQA 572
Cdd:PRK13657 551 GSFDELVARGGRFAALLRA 569
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
338-555 |
8.07e-55 |
|
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: 184.62 E-value: 8.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESIS 417
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRVDILNGTLRDNLliaRP--EATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDA 493
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL---DPfgEYSDEELWQALERVGLKEFVESlpGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 494 PILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGS 555
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
339-571 |
8.56e-53 |
|
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: 179.99 E-value: 8.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLLIARPEATDDHLANILKDVG----LEKLLEnnALDSWLGDGGRQLSGGEKRRIGIARAILHDAP 494
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGahdfISELPE--GYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQLRQ 571
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
180-569 |
2.11e-51 |
|
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: 187.64 E-value: 2.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 180 ILFYKLGKRNGGELTQNKADLRVTTLDWIEGYSELTLFGAEERYRNAILETQRKLMANQFVNANLTGMASAALMLFNGLT 259
Cdd:TIGR01193 313 ILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLIL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 260 LVLMLWLAADGVGGNAPDpFIALMAFATMASFeLLMPIAGAFqHLGQTLSSAR----RLNEVILSEPEVQFAEEKLDINK 335
Cdd:TIGR01193 393 NVVILWTGAYLVMRGKLT-LGQLITFNALLSY-FLTPLENII-NLQPKLQAARvannRLNEVYLVDSEFINKKKRTELNN 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 336 PL-DITFSNVTFNYpDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRE 414
Cdd:TIGR01193 470 LNgDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQ 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 415 SISVVSQRVDILNGTLRDNLLI-ARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILH 491
Cdd:TIGR01193 549 FINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENmpLGYQTELSEEGSSISGGQKQRIALARALLT 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 492 DAPILLLDEPTEGLDKQTEHSIMT--LFEKHfegKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQL 569
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNnlLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
302-572 |
1.52e-50 |
|
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: 183.55 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 302 QHLGQTLSSARRLNEVILSEPEVQFAEEKLDI----NKPLDITFSNVTFNYPDSERNVLNaVDLTIPATNKVAIVGQTGS 377
Cdd:TIGR01192 294 GFITQIFEARAKLEDFFDLEDSVFQREEPADApelpNVKGAVEFRHITFEFANSSQGVFD-VSFEAKAGQTVAIVGPTGA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 378 GKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEK 457
Cdd:TIGR01192 373 GKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 458 LLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIG 535
Cdd:TIGR01192 453 FILKrsNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLST 532
|
250 260 270
....*....|....*....|....*....|....*..
gi 2020526634 536 LESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQLRQA 572
Cdd:TIGR01192 533 VRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
320-569 |
2.46e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 182.74 E-value: 2.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 320 SEPEVQFAEEKLDINKPLDITFSNVTFNYPDSERnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWdPKKGYISI 399
Cdd:PRK11174 331 PLAHPQQGEKELASNDPVTIEAEDLEILSPDGKT-LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 400 AGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLE--NNALDSWLGDGGRQLSG 477
Cdd:PRK11174 409 NGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPllPQGLDTPIGDQAAGLSV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 478 GEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHE 557
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYA 568
|
250
....*....|..
gi 2020526634 558 KLLNEAGRYFQL 569
Cdd:PRK11174 569 ELSQAGGLFATL 580
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
339-563 |
3.42e-44 |
|
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: 156.72 E-value: 3.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDsERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVD--ILNGTLRD-------NLLIARPEAtDDHLANILKDVGLEKLLENNALdswlgdggrQLSGGEKRRIGIARAI 489
Cdd:COG1122 80 VFQNPDdqLFAPTVEEdvafgpeNLGLPREEI-RERVEEALELVGLEHLADRPPH---------ELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLNEA 563
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLdLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
341-549 |
7.80e-44 |
|
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: 154.93 E-value: 7.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 341 FSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVS 420
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 421 QRVD--ILNGTLRD-------NLLIARPEAtDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILH 491
Cdd:cd03225 82 QNPDdqFFGPTVEEevafgleNLGLPEEEI-EERVEEALELVGLEGLRDRSP---------FTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 492 DAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRL-IGLESMDSIVLIEQGE 549
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
345-573 |
1.22e-41 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 158.34 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 345 TFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVD 424
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 425 ILNGTLRDNLLIARPEATDDH------LANILKDVglekLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLL 498
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEiehvarLASVHDDI----LRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 499 DEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAG------RYFQLRQA 572
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGwyrdmyRYQQLEAA 555
|
.
gi 2020526634 573 I 573
Cdd:PRK10789 556 L 556
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
217-569 |
3.26e-41 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 158.73 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 217 FGAEE----RYRNAILET----QRKLMAN--QFVNANLTGMASAALMLFNGLTLVLMLWLAADGvggnapdpfiaLMAF- 285
Cdd:TIGR00958 356 FAAEEgeasRFKEALEETlqlnKRKALAYagYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGN-----------LVSFl 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 286 -----ATMASFELLMPIAGAFQHLGqtlsSARRLNEVILSEPEVQFAEEKLDINKPLDITFSNVTFNYPD-SERNVLNAV 359
Cdd:TIGR00958 425 lyqeqLGEAVRVLSYVYSGMMQAVG----ASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNrPDVPVLKGL 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 360 DLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNLLIARP 439
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLT 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 440 EATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLf 517
Cdd:TIGR00958 581 DTPDEEIMAAAKAANAHDFIMEfpNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES- 659
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 518 eKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQL 569
Cdd:TIGR00958 660 -RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
338-571 |
1.34e-40 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 155.65 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNYPDsERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESIS 417
Cdd:PRK10790 340 RIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRVDILNGTLRDNLLIARpEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPI 495
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSlpDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 496 LLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQLRQ 571
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
339-550 |
4.31e-39 |
|
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: 142.63 E-value: 4.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYP--DSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL---- 412
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 413 RESISVVSQRVDILNG-TLRDNLLIA------RPEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGI 485
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPlllagvPKKERRERAEELLERVGLGDRLNHYP---------SELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 486 ARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITH--RLIGLesMDSIVLIEQGEI 550
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHdpELAEY--ADRIIELRDGKI 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
339-550 |
5.91e-39 |
|
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: 142.22 E-value: 5.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPD-SERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESIS 417
Cdd:cd03248 12 VKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLENNALDSW--LGDGGRQLSGGEKRRIGIARAILHDAPI 495
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDteVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 496 LLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEI 550
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
339-553 |
6.83e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 142.10 E-value: 6.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYP--DSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQL---LTRywdPKKGYISIAGIELTQWNESQL- 412
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 413 ---RESISVVSQRVDILNG-TLRDNLLIA------RPEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRR 482
Cdd:COG1136 82 rlrRRHIGFVFQFFNLLPElTALENVALPlllagvSRKERRERARELLERVGLGDRLDHRP---------SQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 483 IGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE--GKTVIFITH--RLigLESMDSIVLIEQGEIVEN 553
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHdpEL--AARADRVIRLRDGRIVSD 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
339-552 |
7.36e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.11 E-value: 7.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSeRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ---LRES 415
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQrvD---ILNGTLRDNLLIA------RPEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIA 486
Cdd:COG2884 81 IGVVFQ--DfrlLPDRTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALP---------HELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 487 RAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRLIGLESMDS-IVLIEQGEIVE 552
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
282-562 |
1.23e-38 |
|
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: 149.51 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 282 LMAFAtMASFELLMpiaGAFQHLGQTLSSARRLNEVILSEPEvqfAEEKLDINKPL-DITFSNVTFNYPDSERNVLNAVD 360
Cdd:COG4618 280 LMGRA-LAPIEQAI---GGWKQFVSARQAYRRLNELLAAVPA---EPERMPLPRPKgRLSVENLTVVPPGSKRPILRGVS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 361 LTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNllIAR-P 439
Cdd:COG4618 353 FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAEN--IARfG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 440 EATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLF 517
Cdd:COG4618 431 DADPEKVVAAAKLAGVHEMILRlpDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAI 510
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2020526634 518 EKHFE-GKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNE 562
Cdd:COG4618 511 RALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
31-311 |
1.98e-38 |
|
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: 142.80 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 31 ASIGLLTLSGWFISASAVAGLTiARETFNYMLPGGGVRGLAMSRTAGRWGERVVSHNATFKLLTDLRIFFFKKLAPLIPG 110
Cdd:cd18561 7 LITALYIAQAWLLARALARIFA-GGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 111 RISNLRDADLLNRLVADVDAMDHVYLRLVSPVTVGVFGIFFLTLFLMWFDSSLGLILGSILLIMLLVwPILFYKLGKRNG 190
Cdd:cd18561 86 YLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLS-PALWDRLAKDTG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 191 GELTQNKADLRVTTLDWIEGYSELTLFGAEERYRNAILETQRKLMANQFVNANLTGMASAALMLFNGLTLVLMLWLAADG 270
Cdd:cd18561 165 RRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2020526634 271 VGGNAPDPFIALMAFATMASFELLMPIAGAFQHLGQTLSSA 311
Cdd:cd18561 245 VLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
339-550 |
9.00e-38 |
|
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: 137.35 E-value: 9.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLliarpeatddhlanilkdvglekllennaldswlgdggrqLSGGEKRRIGIARAILHDAPILLL 498
Cdd:cd03246 81 LPQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 499 DEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRLIGLESMDSIVLIEQGEI 550
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
339-563 |
3.49e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 137.89 E-value: 3.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLRESISV 418
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNG-TLRDNL-LIAR-----PEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILH 491
Cdd:COG1131 78 VPQEPALYPDlTVRENLrFFARlyglpRKEARERIDELLELFGLTDAADRKV---------GTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 492 DAPILLLDEPTEGLDKQTEHSIMTLFEKHF-EGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLNEA 563
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
306-561 |
3.17e-36 |
|
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: 141.96 E-value: 3.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 306 QTLSSARRLNEVILSEPEVQFAEEKLDINKPLdITFSNVTFNYPDSERN---VLNAVDLTIPATNKVAIVGQTGSGKSTL 382
Cdd:COG1123 229 EILAAPQALAAVPRLGAARGRAAPAAAAAEPL-LEVRNLSKRYPVRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 383 IQLLTRYWDPKKGYISIAGIELTQWNESQLRE---SISVVSQ----------RV-DILNGTLRdNLLIARPEATDDHLAN 448
Cdd:COG1123 308 ARLLLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQdpysslnprmTVgDIIAEPLR-LHGLLSRAERRERVAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 449 ILKDVGL-EKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE--GKT 525
Cdd:COG1123 387 LLERVGLpPDLADRYP---------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLT 457
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2020526634 526 VIFITHRLigleSM-----DSIVLIEQGEIVENGSHEKLLN 561
Cdd:COG1123 458 YLFISHDL----AVvryiaDRVAVMYDGRIVEDGPTEEVFA 494
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
339-563 |
6.67e-36 |
|
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: 134.79 E-value: 6.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNG-TLRDNLLIAR---------PEATDDHLAN-ILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIAR 487
Cdd:COG1120 80 VPQEPPAPFGlTVRELVALGRyphlglfgrPSAEDREAVEeALERTGLEHLADRPV---------DELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 488 AILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLNEA 563
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVLTPE 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
340-549 |
1.22e-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: 130.83 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 340 TFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVV 419
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 420 SQrvdilngtlrdnlliarpeatddhlanilkdvglekllennaldswlgdggrqLSGGEKRRIGIARAILHDAPILLLD 499
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 500 EPTEGLDKQTEHSIMTLFEKHF-EGKTVIFITHRLIGLE-SMDSIVLIEQGE 549
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
339-561 |
1.51e-35 |
|
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: 133.09 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNV--LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRE-- 414
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 415 -SISVVSQRVDILNG-TLRDNllIARPEatddHLANILKDVGLEKLLEnnaLDSWLGDGGR------QLSGGEKRRIGIA 486
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFEN--VALPL----EIAGVPKAEIEERVLE---LLELVGLEDKadaypaQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 487 RAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFE-GKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLN 561
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDiNRElGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
339-561 |
1.64e-35 |
|
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: 133.58 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVlNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDIL-NGTLRDN------LLIARPEATDDHLANILKDVGLEKllennalDSWLGDGGRQLSGGEKRRIGIARAILH 491
Cdd:cd03295 80 VIQQIGLFpHMTVEENialvpkLLKWPKEKIRERADELLALVGLDP-------AEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 492 DAPILLLDEPTEGLDKQTEHSIMTLFEKHFE--GKTVIFITH------RLiglesMDSIVLIEQGEIVENGSHEKLLN 561
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHdideafRL-----ADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
342-554 |
2.40e-35 |
|
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: 131.02 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 342 SNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQ 421
Cdd:cd03214 3 ENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 422 rvdilngtlrdnlliarpeatddhlanILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEP 501
Cdd:cd03214 81 ---------------------------ALELLGLAHLADRPF---------NELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 502 TEGLDKQTEHSIMTLF--EKHFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENG 554
Cdd:cd03214 125 TSHLDIAHQIELLELLrrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
338-555 |
6.15e-35 |
|
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: 130.61 E-value: 6.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNY-PDSERnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESI 416
Cdd:cd03369 6 EIEVENLSVRYaPDLPP-VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQRVDILNGTLRDNLLIARpEATDDHLANILKdvglekllennaldswLGDGGRQLSGGEKRRIGIARAILHDAPIL 496
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALR----------------VSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 497 LLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGS 555
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
339-565 |
1.85e-34 |
|
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: 130.36 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLRESISV 418
Cdd:COG4555 2 IEVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDI-LNGTLRDNLLIARpEATDDHLANILKDVglEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILL 497
Cdd:COG4555 79 LPDERGLyDRLTVRENIRYFA-ELYGLFDEELKKRI--EELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 498 LDEPTEGLD---KQTEHSIMTLFEKhfEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLNEAGR 565
Cdd:COG4555 156 LDEPTNGLDvmaRRLLREILRALKK--EGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
348-550 |
4.63e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.40 E-value: 4.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 348 YPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILN 427
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 428 GTLRDNLL----IARPEATDDHLANILKDVGL-EKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPT 502
Cdd:COG4619 88 GTVRDNLPfpfqLRERKFDRERALELLERLGLpPDILDKPV---------ERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 503 EGLDKQTEHSIMTLFEKHF--EGKTVIFITHRLIGLESM-DSIVLIEQGEI 550
Cdd:COG4619 159 SALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
339-549 |
5.61e-34 |
|
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: 127.97 E-value: 5.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERN---VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieltqwnesqlreS 415
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQRVDILNGTLRDNLLIARPEatdDH--LANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILH 491
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPF---DEerYEKVIKACALEPDLEIlpDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 492 DAPILLLDEPTEGLDKQTEHSIMT--LFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGE 549
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
339-562 |
3.02e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwnesqLRESISV 418
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDI------------LNGTLRDNLLIARPEATD-DHLANILKDVGLEKLLennalDSWLGdggrQLSGGEKRRIGI 485
Cdd:COG1121 80 VPQRAEVdwdfpitvrdvvLMGRYGRRGLFRRPSRADrEAVDEALERVGLEDLA-----DRPIG----ELSGGQQQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 486 ARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRLIGLESM-DSIVLIEQGeIVENGSHEKLLNE 562
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDRVLLLNRG-LVAHGPPEEVLTP 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
339-561 |
3.44e-33 |
|
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: 133.10 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPK---KGYISIAGIELTQWNESQLRES 415
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQRVDI-LNGTLRDNLLIARPEATDDHLANILKDVglEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAP 494
Cdd:COG1123 85 IGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARV--LELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLN 561
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
339-555 |
5.26e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.04 E-value: 5.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNV--LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRE-- 414
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 415 -SISVVSQRVDILNG-TLRDNllIARP--------EATDDHLANILKDVGLEkllenNALDSWLgdggRQLSGGEKRRIG 484
Cdd:COG1135 82 rKIGMIFQHFNLLSSrTVAEN--VALPleiagvpkAEIRKRVAELLELVGLS-----DKADAYP----SQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 485 IARAILHDAPILLLDEPTEGLDKQTEHSIMTLF----EKHfeGKTVIFITHrliglEsM-------DSIVLIEQGEIVEN 553
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLkdinREL--GLTIVLITH-----E-MdvvrricDRVAVLENGRIVEQ 222
|
..
gi 2020526634 554 GS 555
Cdd:COG1135 223 GP 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
341-548 |
1.47e-32 |
|
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: 124.18 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 341 FSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwnesqLRESISVVS 420
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 421 QRVDI------------LNGTLRDNLLIARPEATDDHLA-NILKDVGLEKLLENNaldswLGdggrQLSGGEKRRIGIAR 487
Cdd:cd03235 75 QRRSIdrdfpisvrdvvLMGLYGHKGLFRRLSKADKAKVdEALERVGLSELADRQ-----IG----ELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 488 AILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRL-IGLESMDSIVLIEQG 548
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLgLVLEYFDRVLLLNRT 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
339-550 |
1.57e-32 |
|
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: 122.89 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLRESISV 418
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNG-TLRDNLliarpeatddhlanilkdvglekllennaldswlgdggrQLSGGEKRRIGIARAILHDAPILL 497
Cdd:cd03230 78 LPEEPSLYENlTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 498 LDEPTEGLDKQTEHSIMTLFEKH-FEGKTVIFITHRLIGLESM-DSIVLIEQGEI 550
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
339-573 |
2.40e-32 |
|
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: 125.74 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDpKKGYISIAGIELTQWNESQLRESISV 418
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLliaRPEA--TDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAP 494
Cdd:cd03289 82 IPQKVFIFSGTFRKNL---DPYGkwSDEEIWKVAEEVGLKSVIEQfpGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGryfQLRQAI 573
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS---HFKQAI 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
356-502 |
1.19e-31 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 119.67 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNG-TLRDNL 434
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 435 LIARP------EATDDHLANILKDVGLeklleNNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPT 502
Cdd:pfam00005 81 RLGLLlkglskREKDARAEEALEKLGL-----GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
334-562 |
1.70e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.18 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 334 NKPLDITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLR 413
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 414 ESISVVSQRVD--ILNGTLRDNllIA--------RPEATDDHLANILKDVGLEKLLENNALDswlgdggrqLSGGEKRRI 483
Cdd:PRK13632 83 KKIGIIFQNPDnqFIGATVEDD--IAfglenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN---------LSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 484 GIARAILHDAPILLLDEPTEGLD---KQTEHSIMTLFEKHfEGKTVIFITHrligleSMDSIVL------IEQGEIVENG 554
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDpkgKREIKKIMVDLRKT-RKKTLISITH------DMDEAILadkvivFSEGKLIAQG 224
|
....*...
gi 2020526634 555 SHEKLLNE 562
Cdd:PRK13632 225 KPKEILNN 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
339-573 |
4.34e-31 |
|
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: 129.26 E-value: 4.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDpKKGYISIAGIELTQWNESQLRESISV 418
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLliaRPEA--TDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAP 494
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQfpDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGryfQLRQAI 573
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETS---LFKQAM 1449
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
339-564 |
7.35e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 121.00 E-value: 7.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTqwNESQL---RES 415
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENLweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQRVD--ILNGTLRD-------NLLIARPEaTDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIA 486
Cdd:TIGR04520 79 VGMVFQNPDnqFVGATVEDdvafgleNLGVPREE-MRKRVDEALKLVGMEDFRDREP---------HLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 487 RAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENG------SHEK 558
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKlnKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228
|
....*.
gi 2020526634 559 LLNEAG 564
Cdd:TIGR04520 229 LLKEIG 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
339-554 |
8.53e-31 |
|
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: 119.92 E-value: 8.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYP--DSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRE-- 414
Cdd:cd03257 2 LEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 415 -SISVVSQ----------RV-DILNGTLRDNLLIARPEATDDHLANILKDVGLEKllennaldSWLGDGGRQLSGGEKRR 482
Cdd:cd03257 82 kEIQMVFQdpmsslnprmTIgEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPE--------EVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 483 IGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLF----EKHfeGKTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLkklqEEL--GLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
339-563 |
2.27e-30 |
|
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: 119.42 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGY-ISIAGIELTQWNESQLRESIS 417
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVS----QRVDiLNGTLRDNLLIA---------RPEATDDHLAN-ILKDVGLEKLLEnnalDSWlgdggRQLSGGEKRRI 483
Cdd:COG1119 82 LVSpalqLRFP-RDETVLDVVLSGffdsiglyrEPTDEQRERAReLLELLGLAHLAD----RPF-----GTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 484 GIARAILHDAPILLLDEPTEGLD-KQTEH---SIMTLFEKHfeGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEK 558
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDlGARELllaLLDKLAAEG--APTLVLVTHHVeEIPPGITHVLLLKDGRVVAAGPKEE 229
|
....*
gi 2020526634 559 LLNEA 563
Cdd:COG1119 230 VLTSE 234
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
343-573 |
2.29e-30 |
|
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: 119.14 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQ- 421
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 422 ---------RVDilnGTLRDNLLIARPEATDDHLANILKDVGLEkllennalDSWLGDGGRQLSGGEKRRIGIARAILHD 492
Cdd:COG1124 88 pyaslhprhTVD---RILAEPLRIHGLPDREERIAELLEQVGLP--------PSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 493 APILLLDEPTEGLDKQTEHSIMTLFE--KHFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLL----NEAGR 565
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLagpkHPYTR 236
|
....*...
gi 2020526634 566 yfQLRQAI 573
Cdd:COG1124 237 --ELLAAS 242
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
339-559 |
3.00e-30 |
|
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: 118.82 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSeRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNES---QLRES 415
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQRVD-ILNGTLRDNLLIAR---------------PEATDDHLAnILKDVGLEKLLENNAldswlgdggRQLSGGE 479
Cdd:cd03256 80 IGMIFQQFNlIERLSVLENVLSGRlgrrstwrslfglfpKEEKQRALA-ALERVGLLDKAYQRA---------DQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 480 KRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSH 556
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVdLAREYADRIVGLKDGRIVFDGPP 229
|
...
gi 2020526634 557 EKL 559
Cdd:cd03256 230 AEL 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
339-551 |
3.12e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 119.01 E-value: 3.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDsERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLREsisv 418
Cdd:COG3638 3 LELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 vsQRVDI--------LNGTLR--DNLLIAR--------------PEATDDHLANILKDVGLEKLLENNAldswlgdggRQ 474
Cdd:COG3638 78 --LRRRIgmifqqfnLVPRLSvlTNVLAGRlgrtstwrsllglfPPEDRERALEALERVGLADKAYQRA---------DQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 475 LSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRL-IGLESMDSIVLIEQGEIV 551
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRiaREDGITVVVNLHQVdLARRYADRIIGLRDGRVV 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
339-561 |
6.92e-30 |
|
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: 117.77 E-value: 6.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL---RES 415
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQrvdilNG------TLRDNL---LIAR---PEATDDHLANI-LKDVGLEkllennaldswlGDGGR---QLSGGE 479
Cdd:COG1127 84 IGMLFQ-----GGalfdslTVFENVafpLREHtdlSEAEIRELVLEkLELVGLP------------GAADKmpsELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 480 KRRIGIARAILHDAPILLLDEPTEGLD----KQTEHSIMTLFEKHfeGKTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEG 224
|
....*..
gi 2020526634 555 SHEKLLN 561
Cdd:COG1127 225 TPEELLA 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
294-532 |
2.81e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 122.22 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 294 LMPIAGAFQHLGQTLS--------------SARRL---NEVILSEPEVQFAEEKLDINKPLDITFSNVTFNYPDSERnVL 356
Cdd:COG4178 301 LMQAASAFGQVQGALSwfvdnyqslaewraTVDRLagfEEALEAADALPEAASRIETSEDGALALEDLTLRTPDGRP-LL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 357 NAVDLTIPATNKVAIVGQTGSGKSTLIQlltrywdpkkgyiSIAGIeltqWNESQLR------ESISVVSQRVDILNGTL 430
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLR-------------AIAGL----WPYGSGRiarpagARVLFLPQRPYLPLGTL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 RDNLLIARPEA--TDDHLANILKDVGLEKLLEN-NALDSWlgdgGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDK 507
Cdd:COG4178 443 REALLYPATAEafSDAELREALEAVGLGHLAERlDEEADW----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
250 260
....*....|....*....|....*
gi 2020526634 508 QTEHSIMTLFEKHFEGKTVIFITHR 532
Cdd:COG4178 519 ENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
339-561 |
4.75e-29 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 115.29 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRES--- 415
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQrvdilNGTLRDNLLI------------ARPEATDDHLAN-ILKDVGLEkllenNALDSWLGdggrQLSGGEKRR 482
Cdd:cd03261 79 MGMLFQ-----SGALFDSLTVfenvafplrehtRLSEEEIREIVLeKLEAVGLR-----GAEDLYPA----ELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 483 IGIARAILHDAPILLLDEPTEGLD----KQTEHSIMTLFEKHfeGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHE 557
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKEL--GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPE 222
|
....
gi 2020526634 558 KLLN 561
Cdd:cd03261 223 ELRA 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
337-563 |
6.51e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.27 E-value: 6.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 337 LDITFSNVTFNY-PDS--ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELT----QWNE 409
Cdd:PRK13634 1 MDITFQKVEHRYqYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 410 SQLRESISVVSQ-----------RVDILNGTLrdNLLIARPEAtDDHLANILKDVGL-EKLLENNALDswlgdggrqLSG 477
Cdd:PRK13634 81 KPLRKKVGIVFQfpehqlfeetvEKDICFGPM--NFGVSEEDA-KQKAREMIELVGLpEELLARSPFE---------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 478 GEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFE-GKTVIFITHrligleSM-------DSIVLIEQG 548
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlHKEkGLTTVLVTH------SMedaaryaDQIVVMHKG 222
|
250
....*....|....*
gi 2020526634 549 EIVENGSHEKLLNEA 563
Cdd:PRK13634 223 TVFLQGTPREIFADP 237
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
339-549 |
3.03e-28 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 111.12 E-value: 3.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNES--QLRESI 416
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQRVDILNG-TLRDNLLIArpeatddhlanilkdvglekllennaldswlgdggrqLSGGEKRRIGIARAILHDAPI 495
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 496 LLLDEPTEGLDKQTEHSIMTLFEKHFE--GKTVIFITHRLIGLESM-DSIVLIEQGE 549
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
339-544 |
4.62e-28 |
|
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: 111.42 E-value: 4.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLRESISV 418
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNG-TLRDNLLIAR----PEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDA 493
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLADLPV---------RQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 494 PILLLDEPTEGLDKQTEHSIMTLFEKHFE-GKTVIFITHRLIGLESMDSIVL 544
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLArGGAVLLTTHQPLELAAARVLDL 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
339-531 |
1.15e-27 |
|
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: 110.58 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ---LRES 415
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQRVDIL-NGTLRDNLLIA------RPEATDDHLANILKDVGLEKllENNALDSwlgdggrQLSGGEKRRIGIARA 488
Cdd:cd03292 80 IGVVFQDFRLLpDRNVYENVAFAlevtgvPPREIRKRVPAALELVGLSH--KHRALPA-------ELSGGEQQRVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2020526634 489 ILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITH 531
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATH 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
339-572 |
1.17e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 118.54 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLliaRP--EATDDHLANILKDVGLEKLLENN--ALDSWLGDGGRQLSGGEKRRIGIARAILHDAP 494
Cdd:PLN03232 1315 IPQSPVLFSGTVRFNI---DPfsEHNDADLWEALERAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLL-NEAGRYFQLRQA 572
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFRMVHS 1470
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
343-551 |
1.33e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 110.04 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYPDSeRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWnesQLRESISVVSQR 422
Cdd:cd03226 4 NISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 423 VD--ILNGTLRDNLLIARPEATDDH--LANILKDVGLEKLLENNALDswlgdggrqLSGGEKRRIGIARAILHDAPILLL 498
Cdd:cd03226 80 VDyqLFTDSVREELLLGLKELDAGNeqAETVLKDLDLYALKERHPLS---------LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 499 DEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITH--RLIGLESmDSIVLIEQGEIV 551
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRElAAQGKAVIVITHdyEFLAKVC-DRVLLLANGAIV 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
332-561 |
3.45e-27 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 117.44 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 332 DINKPLDITfsNVTFNYPdSERNVLNAVDLTIPATNK--VAIVGQTGSGKSTLIQLLTRYWDPKK--------------- 394
Cdd:PTZ00265 1161 DIKGKIEIM--DVNFRYI-SRPNVPIYKDLTFSCDSKktTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmt 1237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 395 ---------------------------------------GYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNLL 435
Cdd:PTZ00265 1238 neqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 436 IARPEATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSI 513
Cdd:PTZ00265 1318 FGKEDATREDVKRACKFAAIDEFIESlpNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 514 -MTLFE-KHFEGKTVIFITHRLIGLESMDSIVLIEQ----GEIVE-NGSHEKLLN 561
Cdd:PTZ00265 1398 eKTIVDiKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLS 1452
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
337-562 |
1.30e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 337 LDITFSNVTFNYPDS---ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELT-------- 405
Cdd:PRK13646 1 MTIRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 406 -----------QWNESQLRESisvvSQRVDILNGTLRDNLLIarpEATDDHLANILKDVGLEK-LLENNALdswlgdggr 473
Cdd:PRK13646 81 rpvrkrigmvfQFPESQLFED----TVEREIIFGPKNFKMNL---DEVKNYAHRLLMDLGFSRdVMSQSPF--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 474 QLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRLIGLES-MDSIVLIEQGEI 550
Cdd:PRK13646 145 QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSI 224
|
250
....*....|..
gi 2020526634 551 VENGSHEKLLNE 562
Cdd:PRK13646 225 VSQTSPKELFKD 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
339-531 |
1.49e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 108.64 E-value: 1.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYP--DSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwnesqLRESI 416
Cdd:COG1116 8 LELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQrvdilNGTL------RDNLLIA------RPEATDDHLANILKDVGLEKllennALDSWlgdgGRQLSGGEKRRIG 484
Cdd:COG1116 83 GVVFQ-----EPALlpwltvLDNVALGlelrgvPKAERRERARELLELVGLAG-----FEDAY----PHQLSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 485 IARAILHDAPILLLDEPTEGLDKQTEHS----IMTLFEKHfeGKTVIFITH 531
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERlqdeLLRLWQET--GKTVLFVTH 197
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
356-562 |
1.73e-26 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 108.88 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRE----SISVVSQRVDIL-NGTL 430
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 RDN----LLIA-RPEATDDHLA-NILKDVGLEKllennaldsWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEG 504
Cdd:cd03294 120 LENvafgLEVQgVPRAEREERAaEALELVGLEG---------WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 505 LD----KQTEHSIMTLFEKHfeGKTVIFITHRLIglESM---DSIVLIEQGEIVENGSHEKLLNE 562
Cdd:cd03294 191 LDplirREMQDELLRLQAEL--QKTIVFITHDLD--EALrlgDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
281-566 |
2.46e-26 |
|
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: 114.66 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 281 ALMAFATMASFELL-MPI---AGAFQHLGQTLSSARRLnEVILSEPEV--QFAEEK-LDINKPLDITFSNVTFNYPDSER 353
Cdd:TIGR00957 573 AEKAFVSLALFNILrFPLnilPMVISSIVQASVSLKRL-RIFLSHEELepDSIERRtIKPGEGNSITVHNATFTWARDLP 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 354 NVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieltqwnesqlreSISVVSQRVDILNGTLRDN 433
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLREN 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 434 LLIARP------EATDDHLAnILKDvgLEKLLENNALDswLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDK 507
Cdd:TIGR00957 719 ILFGKAlnekyyQQVLEACA-LLPD--LEILPSGDRTE--IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 508 qteHSIMTLFEK------HFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRY 566
Cdd:TIGR00957 794 ---HVGKHIFEHvigpegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
339-555 |
3.29e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.89 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNV--LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRE-- 414
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 415 -SISVVSQRVDILNG-TLRDNllIARP--------EATDDHLANILKDVGLEKLleNNALDSwlgdggrQLSGGEKRRIG 484
Cdd:PRK11153 82 rQIGMIFQHFNLLSSrTVFDN--VALPlelagtpkAEIKARVTELLELVGLSDK--ADRYPA-------QLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 485 IARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE--GKTVIFITHRliglesMDSI-------VLIEQGEIVENGS 555
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHE------MDVVkricdrvAVIDAGRLVEQGT 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
339-531 |
4.96e-26 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 106.02 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDS--ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwnesqLRESI 416
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQRvDILNG--TLRDNLL-------IARPEAtDDHLANILKDVGLEkllenNALDSWlgdgGRQLSGGEKRRIGIAR 487
Cdd:cd03293 76 GYVFQQ-DALLPwlTVLDNVAlglelqgVPKAEA-RERAEELLELVGLS-----GFENAY----PHQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2020526634 488 AILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITH 531
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
338-567 |
5.00e-26 |
|
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: 107.30 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESIS 417
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRVDILNGTLRDNLliaRPE--ATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDA 493
Cdd:cd03288 99 IILQDPILFSGSIRFNL---DPEckCTDDRLWEALEIAQLKNMVKSlpGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 494 PILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYF 567
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-559 |
5.20e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.79 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVD--ILNGTLRD-------NLLIARPEATdDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIArAI 489
Cdd:PRK13635 86 VFQNPDnqFVGATVQDdvafgleNIGVPREEMV-ERVDQALRQVGMEDFLNREP---------HRLSGGQKQRVAIA-GV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 490 LHDAP-ILLLDEPTEGLDKQTEHSIMTLFE--KHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKL 559
Cdd:PRK13635 155 LALQPdIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
339-552 |
1.17e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 105.59 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSER--NVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL---- 412
Cdd:COG4181 9 IELRGLTKTVGTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 413 RESISVVSQRVDILNG-TLRDNLLI---------ARPEATDdhlanILKDVGLEKLLENNAldswlgdggRQLSGGEKRR 482
Cdd:COG4181 89 ARHVGFVFQSFQLLPTlTALENVMLplelagrrdARARARA-----LLERVGLGHRLDHYP---------AQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 483 IGIARAILHDAPILLLDEPTEGLDKQTEHSIMTL-FEKHFE-GKTVIFITHRLIGLESMDSIVLIEQGEIVE 552
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLlFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
339-567 |
1.18e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 112.52 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLliaRP--EATDDHLANILKDVGLEKLLENNA--LDSWLGDGGRQLSGGEKRRIGIARAILHDAP 494
Cdd:PLN03130 1318 IPQAPVLFSGTVRFNL---DPfnEHNDADLWESLERAHLKDVIRRNSlgLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYF 567
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
339-559 |
1.57e-25 |
|
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: 104.96 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWD-----PKKGYISIAGIELTQWNES--Q 411
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 412 LRESISVVSQRVDILNGTLRDNL-------LIARPEATDDHLANILKDVGLEKLLENNAldswlgdGGRQLSGGEKRRIG 484
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVayglrlhGIKLKEELDERVEEALRKAALWDEVKDRL-------HALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 485 IARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRL-----IGlesmDSIVLIEQGEIVENGSHEKL 559
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMqqaarVA----DRTAFLLNGRLVEFGPTEQI 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
339-563 |
1.72e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.97 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVD--ILNGTLRDNL------LIARPEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAIL 490
Cdd:PRK13647 84 VFQDPDdqVFSSTVWDDVafgpvnMGLDKDEVERRVEEALKAVRMWDFRDKPP---------YHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 491 HDAPILLLDEPTEGLDKQTEHSIMT-LFEKHFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLNEA 563
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEiLDRLHNQGKTVIVATHDVdLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
339-569 |
2.28e-25 |
|
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: 111.58 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLliaRP--EATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAP 494
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWWALELAHLKTFVSAlpDKLDHECAEGGENLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYFQL 569
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
339-562 |
2.53e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.04 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDP---KKGYISIAGIELTQWNESQLRES 415
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQRVD--ILNGTLRD-------NLLIARPEATDDhLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIA 486
Cdd:PRK13640 86 VGIVFQNPDnqFVGATVGDdvafgleNRAVPRPEMIKI-VRDVLADVGMLDYIDSEP---------ANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 487 rAILHDAP-ILLLDEPTEGLDKQTEHSIMTLFEKHFEGK--TVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNE 562
Cdd:PRK13640 156 -GILAVEPkIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
339-554 |
3.37e-25 |
|
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: 103.43 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDseRNVLNAVDLTIPaTNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLRESISV 418
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDIL-NGTLRDNLliarpeatdDHLAnILKDVG-------LEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAIL 490
Cdd:cd03264 77 LPQEFGVYpNFTVREFL---------DYIA-WLKGIPskevkarVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 491 HDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
339-550 |
3.62e-25 |
|
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: 103.38 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQ--WNESQLRESI 416
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQRVDIL-NGTLRDNLLIA------RPEATDDHLA-NILKDVGLEkllenNALDSWlgdgGRQLSGGEKRRIGIARA 488
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENITLApikvkgMSKAEAEERAlELLEKVGLA-----DKADAY----PAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 489 ILHDAPILLLDEPTEGLDKQTEH---SIMTLFEKhfEGKTVIFITHRL-IGLESMDSIVLIEQGEI 550
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGevlDVMKDLAE--EGMTMVVVTHEMgFAREVADRVIFMDDGRI 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
310-568 |
3.13e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 107.90 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 310 SARRLNEVILSEpevqfaEEKLDINKPLD-----ITFSNVTFNY-PDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLI 383
Cdd:PLN03130 587 SLKRLEELLLAE------ERVLLPNPPLEpglpaISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 384 QLLTRYWDPKKGYISIagieltqwnesqLRESISVVSQRVDILNGTLRDNLLIARPEATDDHLANIlkDV-GLEK---LL 459
Cdd:PLN03130 661 SAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAI--DVtALQHdldLL 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 460 ENNALDSwLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKqteHSIMTLFEK----HFEGKTVIFITHRLIG 535
Cdd:PLN03130 727 PGGDLTE-IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA---HVGRQVFDKcikdELRGKTRVLVTNQLHF 802
|
250 260 270
....*....|....*....|....*....|...
gi 2020526634 536 LESMDSIVLIEQGEIVENGSHEKLLNEaGRYFQ 568
Cdd:PLN03130 803 LSQVDRIILVHEGMIKEEGTYEELSNN-GPLFQ 834
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
337-559 |
3.56e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.60 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 337 LDITFSNVTFNY-PDS--ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELT----QWNE 409
Cdd:PRK13641 1 MSIKFENVDYIYsPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 410 SQLRESISVVSQRVDIL---NGTLRD------NLLIARPEATDDHLaNILKDVGL-EKLLENNALDswlgdggrqLSGGE 479
Cdd:PRK13641 81 KKLRKKVSLVFQFPEAQlfeNTVLKDvefgpkNFGFSEDEAKEKAL-KWLKKVGLsEDLISKSPFE---------LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 480 KRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLF-EKHFEGKTVIFITHRLIGL-ESMDSIVLIEQGEIVENGSHE 557
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFkDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPK 230
|
..
gi 2020526634 558 KL 559
Cdd:PRK13641 231 EI 232
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
356-564 |
3.98e-24 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 102.85 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLRESISVVSQRV---DILNGtlRD 432
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYAsvdEDLTG--RE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 433 NL-LIARpeatddhLANILKDVG---LEKLLENNALdswlGDGG----RQLSGGEKRRIGIARAILHDAPILLLDEPTEG 504
Cdd:TIGR01188 86 NLeMMGR-------LYGLPKDEAeerAEELLELFEL----GEAAdrpvGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 505 LDKQTEHSIMTLFEK-HFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLNEAG 564
Cdd:TIGR01188 155 LDPRTRRAIWDYIRAlKEEGVTILLTTHYMEEADKLcDRIAIIDHGRIIAEGTPEELKRRLG 216
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
339-555 |
4.21e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 100.66 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLRESISV 418
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRvDILNGTL--RDNLLI-AR----PEATDDHLA-NILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAIL 490
Cdd:cd03263 80 CPQF-DALFDELtvREHLRFyARlkglPKSEIKEEVeLLLRVLGLTDKANKRA---------RTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 491 HDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHrligleSMDS-------IVLIEQGEIVENGS 555
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH------SMDEaealcdrIAIMSDGKLRCIGS 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
336-554 |
1.30e-23 |
|
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: 98.39 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 336 PLDITFSNVTFNYP----DSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPK--KGYISIAGIELTqwnE 409
Cdd:cd03213 1 GVTLSFRNLTVTVKsspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLD---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 410 SQLRESISVVSQRvDILNGTL--RDNLLIArpeatddhlANIlkdvglekllennaldswlgdggRQLSGGEKRRIGIAR 487
Cdd:cd03213 78 RSFRKIIGYVPQD-DILHPTLtvRETLMFA---------AKL-----------------------RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 488 AILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRL--IGLESMDSIVLIEQGEIVENG 554
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
353-563 |
2.45e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.46 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQ--------RVD 424
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQhsslsfpfTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 425 --ILNGTLRDNLliaRPEATDDHLANILKDVGLEKLlennaldswlgdGGR---QLSGGEKRRIGIARAIL------HDA 493
Cdd:PRK13548 95 evVAMGRAPHGL---SRAEDDALVAAALAQVDLAHL------------AGRdypQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 494 PILLLDEPTEGLDKQTEHSIMTL---FEKHfEGKTVIFITHRLiGLESM--DSIVLIEQGEIVENGSHEKLLNEA 563
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLarqLAHE-RGLAVIVVLHDL-NLAARyaDRIVLLHQGRLVADGTPAEVLTPE 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
355-567 |
2.90e-23 |
|
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: 98.56 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTqwNESQLRESISVVSQRVDIL-NGTLRDN 433
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 434 L-------LIARPEaTDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLD 506
Cdd:cd03299 92 IayglkkrKVDKKE-IERKVLEIAEMLGIDHLLNRKP---------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 507 KQTEHSIMTLFEK--HFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLNEAGRYF 567
Cdd:cd03299 162 VRTKEKLREELKKirKEFGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
339-555 |
2.92e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.82 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDS---ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNES----Q 411
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 412 LRESISVVSQ--RVDILNGT-LRD------NLLIARPEAtdDHLA-NILKDVGL-EKLLENNALDswlgdggrqLSGGEK 480
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETvLKDvafgpqNFGVSQEEA--EALArEKLALVGIsESLFEKNPFE---------LSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 481 RRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRLIGL-ESMDSIVLIEQGEIVENGS 555
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
339-562 |
6.23e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.04 E-value: 6.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNY----PDSERNVLNaVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ--- 411
Cdd:PRK13643 2 IKFEKVNYTYqpnsPFASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 412 -LRESISVVSQ--RVDILNGT-LRD------NLLIARPEAtDDHLANILKDVGLEK-LLENNALdswlgdggrQLSGGEK 480
Cdd:PRK13643 81 pVRKKVGVVFQfpESQLFEETvLKDvafgpqNFGIPKEKA-EKIAAEKLEMVGLADeFWEKSPF---------ELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 481 RRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRLIGL-ESMDSIVLIEQGEIVENGSHEK 558
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSD 230
|
....
gi 2020526634 559 LLNE 562
Cdd:PRK13643 231 VFQE 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
360-554 |
6.28e-23 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 97.18 E-value: 6.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 360 DLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESqlRESISVVSQRVDIL-NGTLRDNLLIAR 438
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 439 P------EATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHS 512
Cdd:cd03298 96 SpglkltAEDRQAIEVALARVGLAGLEKRLP---------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2020526634 513 IMTLF-EKHFE-GKTVIFITHRLIGLESMDS-IVLIEQGEIVENG 554
Cdd:cd03298 167 MLDLVlDLHAEtKMTVLMVTHQPEDAKRLAQrVVFLDNGRIAAQG 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
339-561 |
7.25e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 97.76 E-value: 7.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELT----QWNesQLRE 414
Cdd:COG1126 2 IEIENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDIN--KLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 415 SISVVSQRVDiL--NGTLRDNLLIA--------RPEATDDHLAnILKDVGL-EKLlennalDSWLGdggrQLSGGEKRRI 483
Cdd:COG1126 78 KVGMVFQQFN-LfpHLTVLENVTLApikvkkmsKAEAEERAME-LLERVGLaDKA------DAYPA----QLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 484 GIARAILHDAPILLLDEPTEGLDKQTEH---SIMTLFEKhfEGKTVIFITH-----RLIGlesmDSIVLIEQGEIVENGS 555
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGevlDVMRDLAK--EGMTMVVVTHemgfaREVA----DRVVFMDGGRIVEEGP 219
|
....*.
gi 2020526634 556 HEKLLN 561
Cdd:COG1126 220 PEEFFE 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
339-561 |
7.87e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.13 E-value: 7.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnvLNAvDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQlReSISV 418
Cdd:COG3840 2 LRLDDLTYRYGDFP---LRF-DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNG-TLRDNLLIA-----RPEATD-DHLANILKDVGLEKLLEnnaldswlgdggR---QLSGGEKRRIGIARA 488
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLD------------RlpgQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 489 ILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITH-----RLIGlesmDSIVLIEQGEIVENGSHEKLLN 561
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHdpedaARIA----DRVLLVADGRIAADGPTAALLD 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
284-568 |
1.36e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 102.75 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 284 AFATMASFELL-MPIAGAFQHLGQTLS---SARRLNEVILSEpevqfaEEKLDINKPLD-----ITFSNVTFNY-PDSER 353
Cdd:PLN03232 557 AFTSLSLFAVLrSPLNMLPNLLSQVVNanvSLQRIEELLLSE------ERILAQNPPLQpgapaISIKNGYFSWdSKTSK 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 354 NVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRywdpkkgyisiagiELTQWNESQ--LRESISVVSQRVDILNGTLR 431
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG--------------ELSHAETSSvvIRGSVAYVPQVSWIFNATVR 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 432 DNLLIARPEATDDHLANIlkDV-GLE---KLLENNALDSwLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDK 507
Cdd:PLN03232 697 ENILFGSDFESERYWRAI--DVtALQhdlDLLPGRDLTE-IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 508 QTEHSIMTLFEKH-FEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKlLNEAGRYFQ 568
Cdd:PLN03232 774 HVAHQVFDSCMKDeLKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFK 834
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
359-554 |
1.38e-22 |
|
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: 96.21 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 359 VDLTIPaTNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGielTQWNESQLRESISVVSQRVDIL--------NGTL 430
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFDSRKKINLPPQQRKIGLVfqqyalfpHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 RDNLLIARPEatddhLANILKDVGLEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTE 510
Cdd:cd03297 93 RENLAFGLKR-----KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2020526634 511 HSIMTLFE---KHFEGkTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:cd03297 168 LQLLPELKqikKNLNI-PVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
333-550 |
2.23e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.67 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 333 INKPLDITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLtrywdpkkgyisiAGIELTQWNE--- 409
Cdd:PRK11247 7 LNQGTPLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLL-------------AGLETPSAGElla 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 410 -----SQLRESISVVSQRVDILN-GTLRDNLLIA-----RPEATDdhlanILKDVGLEklleNNAldswlGDGGRQLSGG 478
Cdd:PRK11247 72 gtaplAEAREDTRLMFQDARLLPwKKVIDNVGLGlkgqwRDAALQ-----ALAAVGLA----DRA-----NEWPAALSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 479 EKRRIGIARAILHDAPILLLDEPTEGLDKQT----EHSIMTLFEKHfeGKTVIFITHRLIGLESM-DSIVLIEQGEI 550
Cdd:PRK11247 138 QKQRVALARALIHRPGLLLLDEPLGALDALTriemQDLIESLWQQH--GFTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
339-563 |
2.28e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.43 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNY-PDS--ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELT--QWNESQLR 413
Cdd:PRK13637 3 IKIENLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 414 ESISVVSQ-----------RVDILNGTLRDNLliarpeaTDDHLANILKD----VGL--EKLLENNALDswlgdggrqLS 476
Cdd:PRK13637 83 KKVGLVFQypeyqlfeetiEKDIAFGPINLGL-------SEEEIENRVKRamniVGLdyEDYKDKSPFE---------LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 477 GGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGK-TVIFITHrligleSM-------DSIVLIEQ 547
Cdd:PRK13637 147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElHKEYNmTIILVSH------SMedvaklaDRIIVMNK 220
|
250
....*....|....*.
gi 2020526634 548 GEIVENGSHEKLLNEA 563
Cdd:PRK13637 221 GKCELQGTPREVFKEV 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
339-559 |
2.32e-22 |
|
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: 95.51 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLRESISV 418
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRV---DILNGtlRDNLLI-ARpeatddhLANILKDVGLEKLLEnnALDSW-LGDGGRQL----SGGEKRRIGIARAI 489
Cdd:cd03265 78 VFQDLsvdDELTG--WENLYIhAR-------LYGVPGAERRERIDE--LLDFVgLLEAADRLvktySGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE--GKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKL 559
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
343-562 |
3.23e-22 |
|
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: 97.43 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPK---KGYISIAGIELTQWNESQLRE----S 415
Cdd:COG0444 8 KVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKirgrE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQ----------RV-DILNGTLRDNLLIARPEAtDDHLANILKDVGL---EKLLennaldswlgdgGR---QLSGG 478
Cdd:COG0444 88 IQMIFQdpmtslnpvmTVgDQIAEPLRIHGGLSKAEA-RERAIELLERVGLpdpERRL------------DRyphELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 479 EKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLF----EKHfeGKTVIFITHRL-IGLESMDSIVLIEQGEIVEN 553
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLkdlqREL--GLAILFITHDLgVVAEIADRVAVMYAGRIVEE 232
|
....*....
gi 2020526634 554 GSHEKLLNE 562
Cdd:COG0444 233 GPVEELFEN 241
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
355-573 |
4.25e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 96.03 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLR-----------ESISVVSQRV 423
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRafrrdvqlvfqDSPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 424 ---DILNGTLRdNLLIARPEATDDHLANILKDVGLEkllennalDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDE 500
Cdd:TIGR02769 106 tvrQIIGEPLR-HLTSLDESEQKARIAELLDMVGLR--------SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 501 PTEGLDKQTEHSIMTLFEKHFE--GKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLL---NEAGRyfQLRQAI 573
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECDVAQLLsfkHPAGR--NLQSAV 253
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
359-560 |
5.13e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 97.88 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 359 VDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGielTQWNES----QL---RESISVVSQRVDIL-NGTL 430
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG---RTLFDSrkgiFLppeKRRIGYVFQEARLFpHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 RDNLLI----ARPEATDDHLANILKDVGLEKLLENnaldswlgdGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLD 506
Cdd:TIGR02142 93 RGNLRYgmkrARPSERRISFERVIELLGIGHLLGR---------LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 507 KQTEHSIMTLFEK-HFE-GKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLL 560
Cdd:TIGR02142 164 DPRKYEILPYLERlHAEfGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVW 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
341-559 |
5.96e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 101.01 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 341 FSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVS 420
Cdd:PTZ00243 1311 FEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 421 QRVDILNGTLRDNLliaRP--EATDDHLANILKDVGLEKLL--ENNALDSWLGDGGRQLSGGEKRRIGIARAIL-HDAPI 495
Cdd:PTZ00243 1391 QDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVasESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGF 1467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 496 LLLDEPTE----GLDKQTEHSIMTLFEKHfegkTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKL 559
Cdd:PTZ00243 1468 ILMDEATAnidpALDRQIQATVMSAFSAY----TVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
339-532 |
9.32e-22 |
|
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: 92.22 E-value: 9.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNaVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieltqwnesqlRESISV 418
Cdd:cd03223 1 IELENLSLATPDGRVLLKD-LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDnlLIARPeatddhlanilkdvglekllennaldsWlgdgGRQLSGGEKRRIGIARAILHDAPILLL 498
Cdd:cd03223 69 LPQRPYLPLGTLRE--QLIYP---------------------------W----DDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....
gi 2020526634 499 DEPTEGLDKQTEHSIMTLFEKHfeGKTVIFITHR 532
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKEL--GITVISVGHR 147
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
337-563 |
1.23e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 337 LDITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESI 416
Cdd:PRK11231 1 MTLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQRVDILNG-TLRDnlLIA-----------RPEATDDHLANI-LKDVGLEKLLENNALDswlgdggrqLSGGEKRRI 483
Cdd:PRK11231 79 ALLPQHHLTPEGiTVRE--LVAygrspwlslwgRLSAEDNARVNQaMEQTRINHLADRRLTD---------LSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 484 GIARAILHDAPILLLDEPTEGLDKQTEHSIMTLF-EKHFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLN 561
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
..
gi 2020526634 562 EA 563
Cdd:PRK11231 228 PG 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
339-554 |
1.45e-21 |
|
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: 92.97 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESqlRESISV 418
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRvDIL--NGTLRDNL-------LIARPEATDDHLAnILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAI 489
Cdd:cd03259 77 VFQD-YALfpHLTVAENIafglklrGVPKAEIRARVRE-LLELVGLEGLLNRYP---------HELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
343-559 |
1.77e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.48 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYpDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQR 422
Cdd:PRK13652 8 DLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 423 VD--ILNGTLRDNLL-----IARPEATDDH-LANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAP 494
Cdd:PRK13652 87 PDdqIFSPTVEQDIAfgpinLGLDEETVAHrVSSALHMLGLEELRDRVP---------HHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEKHFE--GKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKL 559
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
339-562 |
1.80e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNaVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ-LRESIS 417
Cdd:PRK13644 2 IRLENVSYSYPDGTPALEN-INLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQ--RVDILNGTLRDNL------LIARPEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAI 489
Cdd:PRK13644 81 IVFQnpETQFVGRTVEEDLafgpenLCLPPIEIRKRVDRALAEIGLEKYRHRSP---------KTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNE 562
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
338-561 |
2.28e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.08 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFS--NVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRES 415
Cdd:PRK10575 9 DTTFAlrNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQRVDILNG-TLRDNLLIAR-P---------EATDDHLANILKDVGLeKLLENNALDSwlgdggrqLSGGEKRRIG 484
Cdd:PRK10575 87 VAYLPQQLPAAEGmTVRELVAIGRyPwhgalgrfgAADREKVEEAISLVGL-KPLAHRLVDS--------LSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 485 IARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLN 561
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlsQERGLTVIAVLHDInMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
355-557 |
2.79e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 98.70 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYIsiagieltqWNEsqlrESISVVSQRVDILNGTLRDNL 434
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAE----RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 435 LIARPEATDDhLANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHS 512
Cdd:PTZ00243 742 LFFDEEDAAR-LADAVRVSQLEADLAQlgGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2020526634 513 IM-TLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHE 557
Cdd:PTZ00243 821 VVeECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA 866
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
338-555 |
6.81e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.15 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNYPDS---ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKG------YISIAGIELTQwN 408
Cdd:PRK13645 6 DIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdYAIPANLKKIK-E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 409 ESQLRESISVVSQ--RVDILNGTLRDNL------LIARPEATDDHLANILKDVGLEKllennaldSWLGDGGRQLSGGEK 480
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIafgpvnLGENKQEAYKKVPELLKLVQLPE--------DYVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 481 RRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRLIG-LESMDSIVLIEQGEIVENGS 555
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQvLRIADEVIVMHEGKVISIGS 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
339-567 |
7.91e-21 |
|
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: 91.63 E-value: 7.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNeSQLREsISV 418
Cdd:cd03296 3 IEVRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-VQERN-VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDIL-NGTLRDNL---LIARPEATDDHLANILKDVglEKLLENNALDsWLGDggR---QLSGGEKRRIGIARAILH 491
Cdd:cd03296 79 VFQHYALFrHMTVFDNVafgLRVKPRSERPPEAEIRAKV--HELLKLVQLD-WLAD--RypaQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 492 DAPILLLDEPTEGLDKQTEHSIMT-LFEKHFE-GKTVIFITH-RLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRYF 567
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRwLRRLHDElHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
346-554 |
8.01e-21 |
|
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: 91.18 E-value: 8.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 346 FNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKK---GYISIAGIELtqwNESQLRESISVVSQR 422
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR---KPDQFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 423 VDILNG-TLRDNLLIARPEATDDHLANILKDVGLEKLLENNALDSWLGDGG-RQLSGGEKRRIGIARAILHDAPILLLDE 500
Cdd:cd03234 90 DILLPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 501 PTEGLDKQTEHSIM-TLFEKHFEGKTVIFITH--RLIGLESMDSIVLIEQGEIVENG 554
Cdd:cd03234 170 PTSGLDSFTALNLVsTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
339-554 |
1.23e-20 |
|
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: 90.50 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNV--LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLRESI 416
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQRVDILNG-TLRDNLL-------IARPEATD--DHLANILkdvGLEKLLENNALDswlgdggrqLSGGEKRRIGIA 486
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEyfaglygLKGDELTArlEELADRL---GMEELLDRRVGG---------FSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 487 RAILHDAPILLLDEPTEGLDKQtehSIMTLFE--KHF--EGKTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVM---ATRALREfiRQLraLGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
342-562 |
1.25e-20 |
|
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: 90.57 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 342 SNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ-LRESISVVS 420
Cdd:cd03224 4 ENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 421 QRVDILNG-TLRDNLLIARPEATDDHLANILkdvglEKLLEN-NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLL 498
Cdd:cd03224 82 EGRRIFPElTVEENLLLGAYARRRAKRKARL-----ERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 499 DEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLNE 562
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNArFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
339-554 |
1.31e-20 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 90.35 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIElTQWNESQLRESISV 418
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNLLIARpeatddhLANILKDVGLEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLL 498
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLA-------RLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 499 DEPTEGLDKQTEHSIMTLFEKHF-EGKTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
355-563 |
1.36e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.99 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIpATNKV-AIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQ----------------WNESQLRESIS 417
Cdd:PRK13631 41 ALNNISYTF-EKNKIyFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhelitnpyskkiKNFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQ-----------RVDILNGTLrdNLLIARPEATDdHLANILKDVGLEkllennalDSWLGDGGRQLSGGEKRRIGIA 486
Cdd:PRK13631 120 MVFQfpeyqlfkdtiEKDIMFGPV--ALGVKKSEAKK-LAKFYLNKMGLD--------DSYLERSPFGLSGGQKRRVAIA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 487 RAILHDAPILLLDEPTEGLDKQTEHSIMTLF-EKHFEGKTVIFITHRLIG-LESMDSIVLIEQGEIVENGS-HEKLLNEA 563
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGTpYEIFTDQH 268
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
339-562 |
2.04e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.07 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPD---SERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQ----LLT----------RYWDPKKGYISIAG 401
Cdd:PRK13651 3 IKVKNIVKIFNKklpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnaLLLpdtgtiewifKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 402 ------IELTQW----NESQLRESISVVSQ-----------RVDILNGTLrdNLLIARPEATDdHLANILKDVGL-EKLL 459
Cdd:PRK13651 83 vleklvIQKTRFkkikKIKEIRRRVGVVFQfaeyqlfeqtiEKDIIFGPV--SMGVSKEEAKK-RAAKYIELVGLdESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 460 ENNALDswlgdggrqLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRLIG-LE 537
Cdd:PRK13651 160 QRSPFE---------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNvLE 230
|
250 260
....*....|....*....|....*
gi 2020526634 538 SMDSIVLIEQGEIVENGSHEKLLNE 562
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
339-552 |
2.11e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAgieltqwneSQLResISV 418
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------ETVK--IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNG--TLRDNLLIARPEATDDHLANILKDVGLekllennaldswlgDGGRQ------LSGGEKRRIGIARAIL 490
Cdd:COG0488 383 FDQHQEELDPdkTVLDELRDGAPGGTEQEVRGYLGRFLF--------------SGDDAfkpvgvLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 491 HDAPILLLDEPTEGLDKQTehsiMTLFE---KHFEGkTVIFITH--RLigLESM-DSIVLIEQGEIVE 552
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIET----LEALEealDDFPG-TVLLVSHdrYF--LDRVaTRILEFEDGGVRE 509
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
342-558 |
2.28e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.18 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 342 SNVTFNYPDSER--NVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL----RES 415
Cdd:PRK10535 8 KDIRRSYPSGEEqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQRVDILNG-TLRDNLLIARPEAtddhlanilkdvGLEK---LLENNALDSWLGDGGR------QLSGGEKRRIGI 485
Cdd:PRK10535 88 FGFIFQRYHLLSHlTAAQNVEVPAVYA------------GLERkqrLLRAQELLQRLGLEDRveyqpsQLSGGQQQRVSI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 486 ARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE-GKTVIFITHRLIGLESMDSIVLIEQGEIVEN-GSHEK 558
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNpPAQEK 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
339-564 |
2.61e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.97 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQrvdilngtlrdnlliaRPEatDDHLANILK-DV--GLE--------------KLLENNALDSWLGDGGRQLSGGEKR 481
Cdd:PRK13648 88 VFQ----------------NPD--NQFVGSIVKyDVafGLEnhavpydemhrrvsEALKQVDMLERADYEPNALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 482 RIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGK--TVIFITHRLIGLESMDSIVLIEQGEIVENG----- 554
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGtptei 229
|
250
....*....|.
gi 2020526634 555 -SHEKLLNEAG 564
Cdd:PRK13648 230 fDHAEELTRIG 240
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
306-549 |
3.65e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 95.10 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 306 QTLSSARRLNEVILSEPEVQFAE--EKL-DINKpldITFSNVTFNYpDSERNVLNAVDL--TIPATNKVAIVGQTGSGKS 380
Cdd:PTZ00265 350 KSLEATNSLYEIINRKPLVENNDdgKKLkDIKK---IQFKNVRFHY-DTRKDVEIYKDLnfTLTEGKTYAFVGESGCGKS 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 381 TLIQLLTRYWDPKKGYI------SIAGIELTQWnesqlRESISVVSQRV------------------------------- 423
Cdd:PTZ00265 426 TILKLIERLYDPTEGDIiindshNLKDINLKWW-----RSKIGVVSQDPllfsnsiknnikyslyslkdlealsnyyned 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 424 -----------------------DILNGTLRDNLLIARPE---ATDDHLANILKDVGLEKLLEN--NALDSWLGDGGRQL 475
Cdd:PTZ00265 501 gndsqenknkrnscrakcagdlnDMSNTTDSNELIEMRKNyqtIKDSEVVDVSKKVLIHDFVSAlpDKYETLVGSNASKL 580
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 476 SGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFE--KHFEGKTVIFITHRLIGLESMDSIVLIEQGE 549
Cdd:PTZ00265 581 SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
339-551 |
4.07e-20 |
|
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: 87.48 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ-LRESIS 417
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQrvdilngtlrdnlliarpeatddhlanilkdvglekllennaldswlgdggrqLSGGEKRRIGIARAILHDAPILL 497
Cdd:cd03216 79 MVYQ-----------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 498 LDEPTEGL-DKQTEH--SIMTLFEKhfEGKTVIFITHRLIglESM---DSIVLIEQGEIV 551
Cdd:cd03216 106 LDEPTAALtPAEVERlfKVIRRLRA--QGVAVIFISHRLD--EVFeiaDRVTVLRDGRVV 161
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
333-560 |
6.40e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.15 E-value: 6.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 333 INKPLDItfSNVTFNY-PDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ 411
Cdd:PRK13642 1 MNKILEV--ENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 412 LRESISVVSQRVD--ILNGTLRDNLLIARpEATDDHLANILKDVGlEKLLENNALDSWLGDGGRqLSGGEKRRIGIARAI 489
Cdd:PRK13642 79 LRRKIGMVFQNPDnqFVGATVEDDVAFGM-ENQGIPREEMIKRVD-EALLAVNMLDFKTREPAR-LSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMTLFE--KHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLL 560
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
352-537 |
9.48e-20 |
|
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: 87.55 E-value: 9.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQrvDILNGTL- 430
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHA--PGIKTTLs 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 -RDNLLIARPEATDDHLANILKDVGLEKLlENNALDswlgdggrQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQT 509
Cdd:cd03231 90 vLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVA--------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....*....
gi 2020526634 510 EHSIMTLFEKHFE-GKTVIFITHRLIGLE 537
Cdd:cd03231 161 VARFAEAMAGHCArGGMVVLTTHQDLGLS 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
341-531 |
2.01e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 341 FSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieltqwnesqlRESISVVS 420
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 421 QRVDIL-NGTLRDNLLIARPE-------------ATDDHLANILKDVGLEKLLEnnALDSW------------LG----D 470
Cdd:COG0488 68 QEPPLDdDLTVLDTVLDGDAElraleaeleeleaKLAEPDEDLERLAELQEEFE--ALGGWeaearaeeilsgLGfpeeD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 471 GGRQ---LSGGEKRRIGIARAILHDAPILLLDEPTEGLDkqtEHSIMTL--FEKHFEGkTVIFITH 531
Cdd:COG0488 146 LDRPvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWLeeFLKNYPG-TVLVVSH 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
339-561 |
2.69e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.46 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELT--QWNESQLRESI 416
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQRVDIL-NGTLRDNLLI-------ARPEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARA 488
Cdd:PRK09493 80 GMVFQQFYLFpHLTALENVMFgplrvrgASKEEAEKQARELLAKVGLAERAHHYP---------SELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 489 ILHDAPILLLDEPTEGLDKQTEHSIMT----LFEkhfEGKTVIFITHRLIGLESMDS-IVLIEQGEIVENGSHEKLLN 561
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKvmqdLAE---EGMTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
355-555 |
2.72e-19 |
|
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: 87.11 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL-RESISVVSQRVDILNG-TLRD 432
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 433 NLLIARPEATDDHL----------------ANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPIL 496
Cdd:cd03219 95 NVMVAAQARTGSGLllararreereareraEELLERVGLADLADRPA---------GELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 497 LLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGS 555
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMdVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
339-554 |
3.81e-19 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 86.15 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQlrESISV 418
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDIL-NGTLRDN------LLIARPEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILH 491
Cdd:cd03301 77 VFQNYALYpHMTVYDNiafglkLRKVPKDEIDERVREVAELLQIEHLLDRKP---------KQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 492 DAPILLLDEPTEGLDK----QTEHSIMTLFEKHfeGKTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:cd03301 148 EPKVFLMDEPLSNLDAklrvQMRAELKRLQQRL--GTTTIYVTHDQVEAMTMaDRIAVMNDGQIQQIG 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
348-531 |
4.12e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 85.55 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 348 YPDSERnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELtQWNESQLREsisvVSQRVDILN 427
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLE----RRQRVGLVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 428 GTLRDNLLIARpeaTDDHLANILKDVGL-EKLLE---NNALDSWLGDGGR-----QLSGGEKRRIGIARAILHDAPILLL 498
Cdd:TIGR01166 75 QDPDDQLFAAD---VDQDVAFGPLNLGLsEAEVErrvREALTAVGASGLRerpthCLSGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|....
gi 2020526634 499 DEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITH 531
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRlRAEGMTVVISTH 185
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
336-562 |
5.20e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.35 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 336 PLDITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQlRES 415
Cdd:PRK13536 39 TVAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQ--RVDiLNGTLRDNLLI--------ARP-EATddhlanilkdvgLEKLLENNALDSWLGDGGRQLSGGEKRRIG 484
Cdd:PRK13536 116 IGVVPQfdNLD-LEFTVRENLLVfgryfgmsTREiEAV------------IPSLLEFARLESKADARVSDLSGGMKRRLT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 485 IARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHF-EGKTVIFITHRLIGLESM-DSIVLIEQG-EIVENGSHEkLLN 561
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVLEAGrKIAEGRPHA-LID 261
|
.
gi 2020526634 562 E 562
Cdd:PRK13536 262 E 262
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
339-563 |
5.43e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.68 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDI-LNGTLRDnlLIA---------RPEATD-DHLANILKDVGLEKLlENNALDswlgdggrQLSGGEKRRIGIAR 487
Cdd:COG4604 80 LRQENHInSRLTVRE--LVAfgrfpyskgRLTAEDrEIIDEAIAYLDLEDL-ADRYLD--------ELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 488 AILHDAPILLLDEPTEGLDKQteHS--IMTLFEKHFE--GKTVIFITHRlIGLESM--DSIVLIEQGEIVENGSHEKLLN 561
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMK--HSvqMMKLLRRLADelGKTVVIVLHD-INFASCyaDHIVAMKDGRVVAQGTPEEIIT 225
|
..
gi 2020526634 562 EA 563
Cdd:COG4604 226 PE 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
356-561 |
5.51e-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: 90.13 E-value: 5.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYwDPKKGYISIAGIELTQWNESQ---LRESISVVSQ----------R 422
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQdpfgslsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 423 V-DIlngtLRDNLLIARPEAT----DDHLANILKDVGLEKllenNALDswlgdggR---QLSGGEKRRIGIARAILHDAP 494
Cdd:COG4172 381 VgQI----IAEGLRVHGPGLSaaerRARVAEALEEVGLDP----AARH-------RyphEFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLF----EKHfeGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLN 561
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLrdlqREH--GLAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
338-555 |
7.61e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.21 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQL---LTrywDPKKGYISIAGIELTQWnESQLRe 414
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMiagLE---DPTSGEILIGGRDVTDL-PPKDR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 415 SISVVSQRvDIL--NGTLRDN----LLIAR-PEAT-DDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIA 486
Cdd:COG3839 76 NIAMVFQS-YALypHMTVYENiafpLKLRKvPKAEiDRRVREAAELLGLEDLLDRKP---------KQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 487 RAILHDAPILLLDEPTEGLD----KQTEHSIMTLFEKHfeGKTVIFITHRLIglESM---DSIVLIEQGEIVENGS 555
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL--GTTTIYVTHDQV--EAMtlaDRIAVMNDGRIQQVGT 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
353-573 |
9.23e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.28 E-value: 9.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLR-----------ESISVVSQ 421
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrrdiqmvfqDSISAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 422 RVD---ILNGTLRdNLLIARPEATDDHLANILKDVGLEkllennalDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLL 498
Cdd:PRK10419 105 RKTvreIIREPLR-HLLSLDKAERLARASEMLRAVDLD--------DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 499 DEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRLIGLESMDSIVLI-EQGEIVEN---GSHEKLLNEAGRyfQLRQA 572
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKlqQQFGTACLFITHDLRLVERFCQRVMVmDNGQIVETqpvGDKLTFSSPAGR--VLQNA 253
|
.
gi 2020526634 573 I 573
Cdd:PRK10419 254 V 254
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
353-545 |
9.98e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.21 E-value: 9.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieltqwnesqlRESISVVSQRV---DILNGT 429
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSevpDSLPLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 430 LRDnlLIA----------RPEATDDHLA--NILKDVGLEKLlENNALDSwlgdggrqLSGGEKRRIGIARAILHDAPILL 497
Cdd:NF040873 74 VRD--LVAmgrwarrglwRRLTRDDRAAvdDALERVGLADL-AGRQLGE--------LSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2020526634 498 LDEPTEGLDKQTEHSIMTLF-EKHFEGKTVIFITHRLIGLESMDSIVLI 545
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
355-562 |
1.38e-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: 89.97 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieltqwnesqlreSISVVSQRVDILNGTLRDNL 434
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 435 LIARpeATDDH-LANILKDVGLEKLLEN--NALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEH 511
Cdd:TIGR01271 508 IFGL--SYDEYrYTSVIKACQLEEDIALfpEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 512 SImtlFE----KHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNE 562
Cdd:TIGR01271 586 EI---FEsclcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
343-562 |
2.46e-18 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 85.29 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTF-NYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieltqwnesqlreSISVVSQ 421
Cdd:cd03291 39 NLFFsNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 422 RVDILNGTLRDNLLIARpeATDDH-LANILKDVGLE----KLLENNalDSWLGDGGRQLSGGEKRRIGIARAILHDAPIL 496
Cdd:cd03291 106 FSWIMPGTIKENIIFGV--SYDEYrYKSVVKACQLEeditKFPEKD--NTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 497 LLDEPTEGLDKQTEHSImtlFE----KHFEGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNE 562
Cdd:cd03291 182 LLDSPFGYLDVFTEKEI---FEscvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
343-555 |
3.12e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.13 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYPDSERnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL--RESISVVS 420
Cdd:PRK13639 6 DLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 421 QRVD--ILNGTLRD-------NLLIARPEaTDDHLANILKDVGLEKLlENNAldswlgdgGRQLSGGEKRRIGIARAILH 491
Cdd:PRK13639 85 QNPDdqLFAPTVEEdvafgplNLGLSKEE-VEKRVKEALKAVGMEGF-ENKP--------PHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 492 DAPILLLDEPTEGLDKQTEHSIMT-LFEKHFEGKTVIFITHR--LIGLESmDSIVLIEQGEIVENGS 555
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKlLYDLNKEGITIIISTHDvdLVPVYA-DKVYVMSDGKIIKEGT 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
339-531 |
3.88e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.39 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSeRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ---LRES 415
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQRVDIL-NGTLRDNL---LIARPEATDD---HLANILKDVGLEKLLENNALdswlgdggrQLSGGEKRRIGIARA 488
Cdd:PRK10908 81 IGMIFQDHHLLmDRTVYDNVaipLIIAGASGDDirrRVSAALDKVGLLDKAKNFPI---------QLSGGEQQRVGIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2020526634 489 ILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE-GKTVIFITH 531
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATH 195
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
355-560 |
4.18e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIEL--------TQWNESQLRESISVVSQRVDIL 426
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 427 -NGTLRDNL----LIARPEATDDHLA---NILKDVGLeklleNNALDSWlgdgGRQLSGGEKRRIGIARAILHDAPILLL 498
Cdd:PRK11264 98 pHRTVLENIiegpVIVKGEPKEEATArarELLAKVGL-----AGKETSY----PRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 499 DEPTEGLDK----QTEHSIMTLFEkhfEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLL 560
Cdd:PRK11264 169 DEPTSALDPelvgEVLNTIRQLAQ---EKRTMVIVTHEMsFARDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
359-560 |
4.65e-18 |
|
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: 85.92 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 359 VDLTIPATNKVAIVGQTGSGKSTLIQL---LTRywdPKKGYISIAGielTQWNESQL-------RESISVVSQ------- 421
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGG---EVLQDSARgiflpphRRRIGYVFQearlfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 422 -RVdilngtlRDNLLIAR----PEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPIL 496
Cdd:COG4148 92 lSV-------RGNLLYGRkrapRAERRISFDEVVELLGIGHLLDRRP---------ATLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 497 LLDEPTEGLDKQTEHSIMTLFEK-HFEGKT-VIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLL 560
Cdd:COG4148 156 LMDEPLAALDLARKAEILPYLERlRDELDIpILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVL 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-565 |
6.31e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.39 E-value: 6.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWN---------E 409
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylpeE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 410 SQLRESISVVSQRVDIlnGTLRDnllIARPEATDDhlanilkdvgLEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAI 489
Cdd:COG4152 80 RGLYPKMKVGEQLVYL--ARLKG---LSKAEAKRR----------ADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 490 LHDAPILLLDEPTEGLD-------KQtehsimTLFEKHFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLN 561
Cdd:COG4152 145 LHDPELLILDEPFSGLDpvnvellKD------VIRELAAKGTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRR 218
|
....
gi 2020526634 562 EAGR 565
Cdd:COG4152 219 QFGR 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
339-557 |
6.67e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.14 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIEL---TQWNESQ---L 412
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAireL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 413 RESISVVSQRVDIL-NGTLRDNLLIA--RPEATDDHLANILKDVGLEKLLENNALDSWlgdgGRQLSGGEKRRIGIARAI 489
Cdd:PRK11124 81 RRNVGMVFQQYNLWpHLTVQQNLIEApcRVLGLSKDQALARAEKLLERLRLKPYADRF----PLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE-GKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHE 557
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVeVARKTASRVVYMENGHIVEQGDAS 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
339-564 |
8.47e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.47 E-value: 8.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGiELTQWNESQLRESISV 418
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQrVDILNG--TLRDNLLI-ARPEATDDHLANILkdvgLEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPI 495
Cdd:PRK13537 85 VPQ-FDNLDPdfTVRENLLVfGRYFGLSAAAARAL----VPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 496 LLLDEPTEGLDKQTEHSIMTLFEKHF-EGKTVIFITHRLIGLESM-DSIVLIEQG-EIVENGSHEKLLNEAG 564
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVIEEGrKIAEGAPHALIESEIG 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
336-560 |
9.12e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.66 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 336 PLDITFSNVTFnypdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRES 415
Cdd:PRK09536 3 MIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQRVDI-LNGTLRDNLLIAR-PEATDDHLANILKDVGLEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDA 493
Cdd:PRK09536 79 VASVPQDTSLsFEFDVRQVVEMGRtPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 494 PILLLDEPTEGLD----KQTEHSIMTLFEkhfEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLL 560
Cdd:PRK09536 159 PVLLLDEPTASLDinhqVRTLELVRRLVD---DGKTAVAAIHDLdLAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
361-561 |
9.86e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.47 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 361 LTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRE----SISVVSQRVDIL-NGTLRDNll 435
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVLDN-- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 436 iarpEATDDHLANILKDVGLEKLLE---NNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLD----KQ 508
Cdd:PRK10070 127 ----TAFGMELAGINAEERREKALDalrQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 509 TEHSIMTLFEKHfeGKTVIFITHRLIglESM---DSIVLIEQGEIVENGSHEKLLN 561
Cdd:PRK10070 203 MQDELVKLQAKH--QRTIVFISHDLD--EAMrigDRIAIMQNGEVVQVGTPDEILN 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
339-531 |
1.01e-17 |
|
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: 80.19 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieltqwnesqlRESISV 418
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQrvdilngtlrdnlliarpeatddhlanilkdvglekllennaldswlgdggrqLSGGEKRRIGIARAILHDAPILLL 498
Cdd:cd03221 68 FEQ-----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|....
gi 2020526634 499 DEPTEGLDKQT-EHSIMTLfeKHFEGkTVIFITH 531
Cdd:cd03221 95 DEPTNHLDLESiEALEEAL--KEYPG-TVILVSH 125
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
369-555 |
1.14e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.64 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 369 VAIVGQTGSGKSTLIQLLTRYwDPK----KGYISIAGIELTQWnesQLREsISVVSQRVDILNGTL--RDNLLIA----- 437
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFR-SPKgvkgSGSVLLNGMPIDAK---EMRA-ISAYVQQDDLFIPTLtvREHLMFQahlrm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 438 -RPEATDDHLA---NILKDVGLEKllennALDSWLGDGGRQ--LSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEH 511
Cdd:TIGR00955 129 pRRVTKKEKRErvdEVLQALGLRK-----CANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2020526634 512 S-IMTLFEKHFEGKTVIFITH----RLIGLesMDSIVLIEQGEIVENGS 555
Cdd:TIGR00955 204 SvVQVLKGLAQKGKTIICTIHqpssELFEL--FDKIILMAEGRVAYLGS 250
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
355-554 |
1.35e-17 |
|
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: 82.38 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieLTQW-NESQLRESISVV-SQRVD-ILNGTLR 431
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWkRRKKFLRRIGVVfGQKTQlWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 432 DNLLI---------ARPEATDDHLANILKdvgLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPT 502
Cdd:cd03267 114 DSFYLlaaiydlppARFKKRLDELSELLD---LEELLDTPV---------RQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 503 EGLDKQTEHSI----MTLFEKHfeGKTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:cd03267 182 IGLDVVAQENIrnflKEYNRER--GTTVLLTSHYMKDIEALaRRVLVIDKGRLLYDG 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
339-562 |
1.57e-17 |
|
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: 81.90 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTqwNESQLRESISV 418
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDIL-NGTLRDN----LLIAR--PEATDDHLANILKDVGLEKLlENNALDswlgdggrQLSGGEKRRIGIARAILH 491
Cdd:cd03300 77 VFQNYALFpHLTVFENiafgLRLKKlpKAEIKERVAEALDLVQLEGY-ANRKPS--------QLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 492 DAPILLLDEPTEGLDKQ-TEHSIMTLFEKHFE-GKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLNE 562
Cdd:cd03300 148 EPKVLLLDEPLGALDLKlRKDMQLELKRLQKElGITFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
339-557 |
1.69e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIEL---TQWNESQ---L 412
Cdd:COG4161 3 IQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAirlL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 413 RESISVVSQRVDIL-NGTLRDNLLIARPEatddhLANILKDVGLEK---LLENNALDSWLGDGGRQLSGGEKRRIGIARA 488
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENLIEAPCK-----VLGLSKEQAREKamkLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 489 ILHDAPILLLDEPTEGLD----KQTEHSIMTLFEKhfeGKTVIFITHRLIGLESMDSIVL-IEQGEIVENGSHE 557
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDpeitAQVVEIIRELSQT---GITQVIVTHEVEFARKVASQVVyMEKGRIIEQGDAS 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
352-536 |
2.40e-17 |
|
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: 80.48 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNEsQLRESISVVSQRvDILNGTL- 430
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHL-PGLKPELs 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 -RDNLLIARP--EATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDK 507
Cdd:TIGR01189 90 aLENLHFWAAihGGAQRTIEDALAAVGLTGFEDLPA---------AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190
....*....|....*....|....*....|
gi 2020526634 508 QTEHSIMTLFEKHFE-GKTVIFITHRLIGL 536
Cdd:TIGR01189 161 AGVALLAGLLRAHLArGGIVLLTTHQDLGL 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
352-561 |
3.14e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKST----LIQLLtrywdPKKGYISIAGIELTQWNESQL---RESISVVSQ--- 421
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQdpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 422 -----RVDILNgTLRDNLLIARPEAT----DDHLANILKDVGLEKLLENNAldswlgdgGRQLSGGEKRRIGIARAILHD 492
Cdd:PRK15134 373 sslnpRLNVLQ-IIEEGLRVHQPTLSaaqrEQQVIAVMEEVGLDPETRHRY--------PAEFSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 493 APILLLDEPTEGLDKQTEHSIMTLF----EKHfeGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLN 561
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLkslqQKH--QLAYLFISHDLHVVRALcHQVIVLRQGEVVEQGDCERVFA 515
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
343-566 |
3.21e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.07 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGY-----ISIAGIELTQWNES-QLRESI 416
Cdd:PRK14271 26 NLTLGF--AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVlEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQRVDILNGTLRDNLL--------IARPEATDDHLANiLKDVGLEkllenNALDSWLGDGGRQLSGGEKRRIGIARA 488
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVLagvrahklVPRKEFRGVAQAR-LTEVGLW-----DAVKDRLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 489 ILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLN-----E 562
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSspkhaE 257
|
....
gi 2020526634 563 AGRY 566
Cdd:PRK14271 258 TARY 261
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
353-569 |
3.29e-17 |
|
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: 85.84 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELtQWNESQLRESISVVSQRvDIL--NGTL 430
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQH-NILfhHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 RDNLLI-ARPEATDDHLANIlkdvGLEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQT 509
Cdd:TIGR01257 1021 AEHILFyAQLKGRSWEEAQL----EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 510 EHSIMTLFEKHFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLNEAGRYFQL 569
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTPLFLKNCFGTGFYL 1157
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
350-531 |
4.34e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.59 E-value: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 350 DSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNE---SQLR-ESISVVSQR--- 422
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRaKHVGFVFQSfml 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 423 VDILNgTLRDNLLIA--RPEA---TDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILL 497
Cdd:PRK10584 100 IPTLN-ALENVELPAllRGESsrqSRNGAKALLEQLGLGKRLDHLP---------AQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2020526634 498 LDEPTEGLDKQTEHSIMT-LFE-KHFEGKTVIFITH 531
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADlLFSlNREHGTTLILVTH 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
352-561 |
5.31e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.17 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAG--IELTQWNESQL-----------RESISV 418
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtINLVRDKDGQLkvadknqlrllRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNG-TLRDNLL--------IARPEATDDHLANILKdVGLEkllennalDSWLGDGGRQLSGGEKRRIGIARAI 489
Cdd:PRK10619 97 VFQHFNLWSHmTVLENVMeapiqvlgLSKQEARERAVKYLAK-VGID--------ERAQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRLIGLESMDS-IVLIEQGEIVENGSHEKLLN 561
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFG 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
360-561 |
6.07e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.40 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 360 DLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTqwNESQLRESISVVSQRVDILNG-TLRDNL-LIA 437
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPVSMLFQENNLFSHlTVAQNIgLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 438 RP-----EATDDHLANILKDVGLEKLLENnaLDSwlgdggrQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHS 512
Cdd:PRK10771 97 NPglklnAAQREKLHAIARQMGIEDLLAR--LPG-------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 513 IMTLFEK--HFEGKTVIFITHRL-----IGLESmdsiVLIEQGEIVENGSHEKLLN 561
Cdd:PRK10771 168 MLTLVSQvcQERQLTLLMVSHSLedaarIAPRS----LVVADGRIAWDGPTDELLS 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
355-531 |
8.51e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 79.79 E-value: 8.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISI----AGIELTQWNESQL----RESISVVSQ----- 421
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREIlalrRRTIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 422 -RV---DILNGTLRDnLLIARPEATDDhLANILKDVGL-EKLlennaldsWlgdggrQL-----SGGEKRRIGIARAILH 491
Cdd:COG4778 106 pRVsalDVVAEPLLE-RGVDREEARAR-ARELLARLNLpERL--------W------DLppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2020526634 492 DAPILLLDEPTEGLDKQTEHSIMTLF-EKHFEGKTVIFITH 531
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIeEAKARGTAIIGIFH 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
352-554 |
8.81e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 79.25 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYIsiagieltQWNESQLRESISvvsQRVDIL----- 426
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEV--------LFDGKPLDIAAR---NRIGYLpeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 427 ---NGTLRDNLLiarpeatddHLANiLKDVGLEKLLENnaLDSWLGDGG---------RQLSGGEKRRIGIARAILHDAP 494
Cdd:cd03269 81 lypKMKVIDQLV---------YLAQ-LKGLKKEEARRR--IDEWLERLElseyankrvEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMT-LFEKHFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDvIRELARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
338-555 |
1.00e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.68 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWnESQLREsIS 417
Cdd:COG3842 5 ALELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKRN-VG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRVDI---LngTLRDNllIA--------RPEATDDHLANILKDVGLEKLlennaldswlgdGGR---QLSGGEKRRI 483
Cdd:COG3842 81 MVFQDYALfphL--TVAEN--VAfglrmrgvPKAEIRARVAELLELVGLEGL------------ADRyphQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 484 GIARAILHDAPILLLDEPTEGLDK----QTEHSIMTLFEKHfeGKTVIFITHRLigLESM---DSIVLIEQGEIVENGS 555
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAklreEMREELRRLQREL--GITFIYVTHDQ--EEALalaDRIAVMNDGRIEQVGT 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
353-559 |
1.38e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 80.93 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVD---LTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRE---SISVVSQ----- 421
Cdd:COG4608 28 VGVVKAVDgvsFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQdpyas 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 422 -----RV-DILNGTLRDNLlIARPEATDDHLANILKDVGLEKllennaldswlGDGGR---QLSGGEKRRIGIARAILHD 492
Cdd:COG4608 108 lnprmTVgDIIAEPLRIHG-LASKAERRERVAELLELVGLRP-----------EHADRyphEFSGGQRQRIGIARALALN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 493 APILLLDEPTEGLDKQTEHSIMTLFE---KHFeGKTVIFITHRLigleSM-----DSIVLIEQGEIVENGSHEKL 559
Cdd:COG4608 176 PKLIVCDEPVSALDVSIQAQVLNLLEdlqDEL-GLTYLFISHDL----SVvrhisDRVAVMYLGKIVEIAPRDEL 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-554 |
1.56e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.57 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 330 KLDInKPLDITFSNVtfnypdserNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTR----YWDPK-KGYISIAGIEL 404
Cdd:PRK14247 3 KIEI-RDLKVSFGQV---------EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARvSGEVYLDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 405 TQWNESQLRESISVVSQRVD-ILNGTLRDN----LLIARPEATDDHLANILKDvGLEKLLENNALDSWLGDGGRQLSGGE 479
Cdd:PRK14247 73 FKMDVIELRRRVQMVFQIPNpIPNLSIFENvalgLKLNRLVKSKKELQERVRW-ALEKAQLWDEVKDRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 480 KRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITH------RLiglesMDSIVLIEQGEIVEN 553
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEW 226
|
.
gi 2020526634 554 G 554
Cdd:PRK14247 227 G 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
343-560 |
1.67e-16 |
|
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: 82.42 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKS----TLIQLLTRYWDPKKGYISIAGIELTQWNESQLRE---- 414
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 415 SISVVSQ----------RV-DILNGTLRDNLLIARPEATDDHLAnILKDVGL---EKLLennalDSWlgdgGRQLSGGEK 480
Cdd:COG4172 93 RIAMIFQepmtslnplhTIgKQIAEVLRLHRGLSGAAARARALE-LLERVGIpdpERRL-----DAY----PHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 481 RRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFE--KHFEGKTVIFITHRLiGL-ESM-DSIVLIEQGEIVENGSH 556
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKdlQRELGMALLLITHDL-GVvRRFaDRVAVMRQGEIVEQGPT 241
|
....
gi 2020526634 557 EKLL 560
Cdd:COG4172 242 AELF 245
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
339-561 |
2.40e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 80.58 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQ----LLTrywdPKKGYISIAGIELTQWNESQLRE 414
Cdd:COG1118 3 IEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRiiagLET----PDSGRIVLNGRDLFTNLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 415 sISVVSQ-----RvdilNGTLRDNllIA-----RP---EATDDHLANILKDVGLEkllennaldsWLGDggR---QLSGG 478
Cdd:COG1118 77 -VGFVFQhyalfP----HMTVAEN--IAfglrvRPpskAEIRARVEELLELVQLE----------GLAD--RypsQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 479 EKRRIGIARAILHDAPILLLDEPTEGLD----KQTEHSIMTLFEKhfEGKTVIFITHRLigLESM---DSIVLIEQGEIV 551
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDE--LGGTTVFVTHDQ--EEALelaDRVVVMNQGRIE 213
|
250
....*....|
gi 2020526634 552 ENGSHEKLLN 561
Cdd:COG1118 214 QVGTPDEVYD 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
355-555 |
2.65e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 78.93 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL-RESISVVSQRVDILNG-TLRD 432
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 433 NLLIARP---------------------EATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILH 491
Cdd:COG0411 99 NVLVAAHarlgrgllaallrlprarreeREARERAEELLERVGLADRADEPA---------GNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 492 DAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITH--RLIglesM---DSIVLIEQGEIVENGS 555
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEETEELAELIRRlrDERGITILLIEHdmDLV----MglaDRIVVLDFGRVIAEGT 236
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
218-557 |
2.68e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 81.77 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 218 GAEERYRNAILETQRklmanQFVNANLTGMasaaLMLFngLTLVLMLWLAADGVGGNAPdpfiALMAFATMASFeLLMPI 297
Cdd:COG4615 216 PTAERYRDLRIRADT-----IFALANNWGN----LLFF--ALIGLILFLLPALGWADPA----VLSGFVLVLLF-LRGPL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 298 A---GAFQHLGQTLSSARRLNEVILSEPEVQFAEEKLDINKPLD----ITFSNVTFNYPDSERN---VLNAVDLTIPATN 367
Cdd:COG4615 280 SqlvGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPAdfqtLELRGVTYRYPGEDGDegfTLGPIDLTIRRGE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 368 KVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQrvdilNGTLRDNLLIARPEATDDHLA 447
Cdd:COG4615 360 LVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFS-----DFHLFDRLLGLDGEADPARAR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 448 NILKDVGLE-KL-LENNALDSwlgdggRQLSGGEKRRIGIARAILHDAPILLLDE------PTegldkqtehsimtlFEK 519
Cdd:COG4615 435 ELLERLELDhKVsVEDGRFST------TDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPE--------------FRR 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2020526634 520 HF----------EGKTVIFITH--RLIGLesMDSIVLIEQGEIVENGSHE 557
Cdd:COG4615 495 VFytellpelkaRGKTVIAISHddRYFDL--ADRVLKMDYGKLVELTGPA 542
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
339-569 |
2.95e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.39 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNY-PDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESIS 417
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRvdilngtlRDNLLIArpeAT-DDHLANILKDVGLEKLLENNALDSWLGDGGRQ---------LSGGEKRRIGIAR 487
Cdd:PRK13650 85 MVFQN--------PDNQFVG---ATvEDDVAFGLENKGIPHEEMKERVNEALELVGMQdfkereparLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 488 AILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE--GKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGR 565
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
....
gi 2020526634 566 YFQL 569
Cdd:PRK13650 234 LLQL 237
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
359-570 |
3.43e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.75 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 359 VDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieLTQW-NESQLRESISVVS-QRV----DIlngTLRD 432
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG--YVPFkRRKEFARRIGVVFgQRSqlwwDL---PAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 433 NLLIAR-----PEA----TDDHLANILkdvGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPTE 503
Cdd:COG4586 116 SFRLLKaiyriPDAeykkRLDELVELL---DLGELLDTPV---------RQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 504 GLD---KQTEHS-IMTLFEKHfeGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLNEAGRYFQLR 570
Cdd:COG4586 184 GLDvvsKEAIREfLKEYNRER--GTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERFGPYKTIV 253
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
355-569 |
4.12e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.13 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLltrywdpkkgyisIAGIEltQWNESQLR---ESISVVSQRvDILNG--- 428
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRI-------------IAGLE--HQTSGHIRfhgTDVSRLHAR-DRKVGfvf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 429 ---------TLRDNllIA----------RPEAtddhlANILKDVglEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAI 489
Cdd:PRK10851 81 qhyalfrhmTVFDN--IAfgltvlprreRPNA-----AAIKAKV--TQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMT-LFEKHFEGK-TVIFITH-RLIGLESMDSIVLIEQGEIVENGSHEKLLNEAGRY 566
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRwLRQLHEELKfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATR 231
|
...
gi 2020526634 567 FQL 569
Cdd:PRK10851 232 FVL 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
339-531 |
6.14e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 77.98 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYP--DSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwnESQLResi 416
Cdd:COG4525 4 LTVRHVSVRYPggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQrvdilNGTL------RDNL-----LIARPEATDDHLAN-ILKDVGLEKLLENNaldSWlgdggrQLSGGEKRRIG 484
Cdd:COG4525 79 GVVFQ-----KDALlpwlnvLDNVafglrLRGVPKAERRARAEeLLALVGLADFARRR---IW------QLSGGMRQRVG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2020526634 485 IARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITH 531
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
339-557 |
8.55e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 8.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVLNAVdLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwnesQLRES-IS 417
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDAS-FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNlVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VV--SQRVD----------ILNGTLRDNLLIARPEATDDHLAnilkDVGLEKLLENNALDSWLGdggrQLSGGEKRRIGI 485
Cdd:PRK15056 82 YVpqSEEVDwsfpvlvedvVMMGRYGHMGWLRRAKKRDRQIV----TAALARVDMVEFRHRQIG----ELSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 486 ARAILHDAPILLLDEPTEGLDKQTEHSIMTLF-EKHFEGKTVIFITHRLIGL-ESMDSIVLIeQGEIVENGSHE 557
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLrELRDEGKTMLVSTHNLGSVtEFCDYTVMV-KGTVLASGPTE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
339-561 |
1.03e-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: 79.85 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLtRYWD----------------PKKGYI----- 397
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVL-RGMDqyeptsgriiyhvalcEKCGYVerpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 398 ----------SIAGIELTQWNESQ-----LRESISVVSQRVDILNG--TLRDNLLIARPEATDDHLANILKDVgleKLLE 460
Cdd:TIGR03269 78 vgepcpvcggTLEPEEVDFWNLSDklrrrIRKRIAIMLQRTFALYGddTVLDNVLEALEEIGYEGKEAVGRAV---DLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 461 NNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHF--EGKTVIFITHRLIGLES 538
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIED 234
|
250 260
....*....|....*....|....
gi 2020526634 539 M-DSIVLIEQGEIVENGSHEKLLN 561
Cdd:TIGR03269 235 LsDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
339-559 |
1.47e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.61 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPAtNKV-AIVGQTGSGKSTLIQLLTRYWD--PK---KGYISIAGIEL--TQWNES 410
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPE-NKVtALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 411 QLRESISVVSQRVDILNGTLRDNLL-------IARPEATDDHLANILKDVGLekllennaldsW------LGDGGRQLSG 477
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAyglrlhgIKSKSELDEIVEESLRKAAL-----------WdevkdrLKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 478 GEKRRIGIARAILHDAPILLLDEPTEGLD----KQTEHSIMTLFEKHfegkTVIFITHrligleSM-------DSIVLIE 546
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILELKKDY----TIVIVTH------NMqqaarvsDYTAFFY 227
|
250
....*....|...
gi 2020526634 547 QGEIVENGSHEKL 559
Cdd:COG1117 228 LGELVEFGPTEQI 240
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
358-558 |
2.38e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.61 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 358 AVDLTIPATNKVAIVGQTGSGKSTLIQL---LTRywdPKKGYISIAGIELtqwNESQLRESISVVSQRVdilnG------ 428
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAisgLTR---PQKGRIVLNGRVL---FDAEKGICLPPEKRRI----Gyvfqda 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 429 ------TLRDNLLIARPEATDDHLANILKDVGLEKLLENNALDswlgdggrqLSGGEKRRIGIARAILHDAPILLLDEPT 502
Cdd:PRK11144 86 rlfphyKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGS---------LSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 503 EGLDKQTEHSIMTLFEKHfeGKTV----IFITHrligleSMDSI-------VLIEQGEIVENGSHEK 558
Cdd:PRK11144 157 ASLDLPRKRELLPYLERL--AREInipiLYVSH------SLDEIlrladrvVVLEQGKVKAFGPLEE 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
345-573 |
3.37e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.82 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 345 TFNypdsERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKgyISIAGIEL---TQWNESQL-------RE 414
Cdd:PRK09984 13 TFN----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK--SAGSHIELlgrTVQREGRLardirksRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 415 SISVVSQRVDILNG-TLRDNLLIARPEAT--------------DDHLANILKDVGLEKLLENNAldswlgdggRQLSGGE 479
Cdd:PRK09984 87 NTGYIFQQFNLVNRlSVLENVLIGALGSTpfwrtcfswftreqKQRALQALTRVGMVHFAHQRV---------STLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 480 KRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIM-TLFE-KHFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSH 556
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMdTLRDiNQNDGITVVVTLHQVdYALRYCERIVALRQGHVFYDGSS 237
|
250
....*....|....*..
gi 2020526634 557 EKLLNEagRYFQLRQAI 573
Cdd:PRK09984 238 QQFDNE--RFDHLYRSI 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
337-561 |
5.59e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 5.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 337 LDITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKS-TLIQLLTRYWDPK----KGYISIAGIELTQWNESQ 411
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 412 LR----ESISVVSQR-------VDILNGTLRDNLLI---ARPEATDDHLANILKDVGLEKLLENnaldswLGDGGRQLSG 477
Cdd:PRK15134 86 LRgvrgNKIAMIFQEpmvslnpLHTLEKQLYEVLSLhrgMRREAARGEILNCLDRVGIRQAAKR------LTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 478 GEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFE--KHFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENG 554
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLsIVRKLADRVAVMQNGRCVEQN 239
|
....*..
gi 2020526634 555 SHEKLLN 561
Cdd:PRK15134 240 RAATLFS 246
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
348-531 |
7.79e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.98 E-value: 7.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 348 YPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILN 427
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 428 GTLRDNLLIA---RPEATD-DHLANILKDVGL-EKLLENNALDswlgdggrqLSGGEKRRIGIARAILHDAPILLLDEPT 502
Cdd:PRK10247 95 DTVYDNLIFPwqiRNQQPDpAIFLDDLERFALpDTILTKNIAE---------LSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190
....*....|....*....|....*....|.
gi 2020526634 503 EGLDKQTEHSIMTLFEKHFEGK--TVIFITH 531
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQniAVLWVTH 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-561 |
9.16e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 9.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpDSERnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYwDPKKGYISIAG--------IELTQWNES 410
Cdd:PRK14258 8 IKVNNLSFYY-DTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrveffnqnIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 411 QLRESISVVSQRVDILNGTLRDNLLIA------RPEAT-DDHLANILKDVGLEKLLENNALDSWLgdggrQLSGGEKRRI 483
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEiDDIVESALKDADLWDEIKHKIHKSAL-----DLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 484 GIARAILHDAPILLLDEPTEGLDK----QTEHSIMTLFEKhfEGKTVIFITHRLIGLESMDSIVLIEQG------EIVEN 553
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSLRLR--SELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEF 237
|
....*...
gi 2020526634 554 GSHEKLLN 561
Cdd:PRK14258 238 GLTKKIFN 245
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
342-561 |
1.08e-14 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 73.86 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 342 SNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL-RESISVVS 420
Cdd:COG0410 7 ENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 421 QRVDILNG-TLRDNLLI-ARPEATDDHLANILKDVgLE---KLLENnaldswLGDGGRQLSGGEKRRIGIARAILHDAPI 495
Cdd:COG0410 85 EGRRIFPSlTVEENLLLgAYARRDRAEVRADLERV-YElfpRLKER------RRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 496 LLLDEPTEGLD----KQTEHSIMTLFEkhfEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLN 561
Cdd:COG0410 158 LLLDEPSLGLAplivEEIFEIIRRLNR---EGVTILLVEQNArFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
355-533 |
1.11e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.60 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPAtNKV-AIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWN--ESQlRESISVVSQRVDILNG-TL 430
Cdd:COG1129 19 ALDGVSLELRP-GEVhALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprDAQ-AAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 RDNLLIARP--------------EATDdhlanILKDVGLEkllennaLDSW--LGDggrqLSGGEKRRIGIARAILHDAP 494
Cdd:COG1129 97 AENIFLGREprrgglidwramrrRARE-----LLARLGLD-------IDPDtpVGD----LSVAQQQLVEIARALSRDAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2020526634 495 ILLLDEPTEGL-DKQTEHsimtLFE--KHF--EGKTVIFITHRL 533
Cdd:COG1129 161 VLILDEPTASLtEREVER----LFRiiRRLkaQGVAIIYISHRL 200
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
343-540 |
1.12e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.06 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLRESISVVSQR 422
Cdd:PRK13540 6 ELDFDYHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 423 VDI-LNGTLRDNLLIarpeatDDHLANilKDVGLEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEP 501
Cdd:PRK13540 83 SGInPYLTLRENCLY------DIHFSP--GAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2020526634 502 TEGLDKQTEHSIMTLFEKH-FEGKTVIFITHRLIGLESMD 540
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHrAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
353-561 |
1.22e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 73.35 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ-LRESISVVSQRVDILNG-TL 430
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 RDNLLIARPEATDDH------LANILKDVGLEKLLENNALdswlgdggrQLSGGEKRRIGIARAILHDAPILLLDEPTEG 504
Cdd:cd03218 93 EENILAVLEIRGLSKkereekLEELLEEFHITHLRKSKAS---------SLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 505 LDKQTEHSIMTLFEKHFEGKTVIFIT-H--RLIgLESMDSIVLIEQGEIVENGSHEKLLN 561
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLITdHnvRET-LSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
356-554 |
1.30e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIE---LTQWNESQLreSISVVSQRVDILNG-TLR 431
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQL--GIGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 432 DNLLIARP-------------EATDDHLANILKDVGLEKllennALDSWLGDggrqLSGGEKRRIGIARAILHDAPILLL 498
Cdd:PRK09700 99 ENLYIGRHltkkvcgvniidwREMRVRAAMMLLRVGLKV-----DLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 499 DEPTEGL-DKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENG 554
Cdd:PRK09700 170 DEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSG 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
334-555 |
1.81e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 75.37 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 334 NKPLdITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQlR 413
Cdd:PRK09452 11 LSPL-VELRGISKSFDGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 414 ESISVVSQRVDILNGTLRDNLLIA-----RPEA-TDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIAR 487
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGlrmqkTPAAeITPRVMEALRMVQLEEFAQRKP---------HQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 488 AILHDAPILLLDEPTEGLD----KQTEHSIMTLFEKhfEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGS 555
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDyklrKQMQNELKALQRK--LGITFVFVTHDQEEALTMsDRIVVMRDGRIEQDGT 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
356-561 |
2.64e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 74.23 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWN---ESQLRESISVVSQ----------R 422
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQnpygslnprkK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 423 V-DILNGTLRDNLLIARPEATDDHLAnILKDVGLEKllENNaldswlgdgGR---QLSGGEKRRIGIARAILHDAPILLL 498
Cdd:PRK11308 111 VgQILEEPLLINTSLSAAERREKALA-MMAKVGLRP--EHY---------DRyphMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 499 DEPTEGLDKQTEHSIMTLF---EKHFeGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLLN 561
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMmdlQQEL-GLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFN 244
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-560 |
2.81e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.16 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 351 SERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRY---WDPK---KGYISIAGIELTQWNESQLRESISVVSQRVD 424
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 425 IL-NGTLRDNLL-------IARPEATDDHLANILKDVGLEKLLENNaldswLGDGGRQLSGGEKRRIGIARAILHDAPIL 496
Cdd:PRK14246 101 PFpHLSIYDNIAyplkshgIKEKREIKKIVEECLRKVGLWKEVYDR-----LNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 497 LLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLL 560
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
356-531 |
3.28e-14 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 72.11 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLresisVVSQRVDILNG-TLRDNL 434
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 435 LIA------------RPEATDDHLANilkdVGLEKllennALDSWLGdggrQLSGGEKRRIGIARAILHDAPILLLDEPT 502
Cdd:TIGR01184 76 ALAvdrvlpdlskseRRAIVEEHIAL----VGLTE-----AADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190
....*....|....*....|....*....|...
gi 2020526634 503 EGLDKQT----EHSIMTLFEKHfeGKTVIFITH 531
Cdd:TIGR01184 143 GALDALTrgnlQEELMQIWEEH--RVTVLMVTH 173
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
339-552 |
4.04e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.01 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERNVlNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISV 418
Cdd:PRK10522 323 LELRNVTFAYQDNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDilngtLRDNLLIARPEATDDHLAnilkDVGLEKLLENNALDSwlgDGGR----QLSGGEKRRIGIARAILHDAP 494
Cdd:PRK10522 402 VFTDFH-----LFDQLLGPEGKPANPALV----EKWLERLKMAHKLEL---EDGRisnlKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 495 ILLLDEPTEGLDKQtehsimtlFEKHF----------EGKTVIFITHRLIGLESMDSIVLIEQGEIVE 552
Cdd:PRK10522 470 ILLLDEWAADQDPH--------FRREFyqvllpllqeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
356-548 |
5.76e-14 |
|
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: 71.21 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYI----SIAGIELTQWNESQLRESISVVSQRVDILNGTLR 431
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 432 DNLLIARPEATDDHLA-----NILKDVGLEKLLENNALdswlGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLD 506
Cdd:cd03290 97 ENITFGSPFNKQRYKAvtdacSLQPDIDLLPFGDQTEI----GERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2020526634 507 KQTEHSIMTLFEKHF---EGKTVIFITHRLIGLESMDSIVLIEQG 548
Cdd:cd03290 173 IHLSDHLMQEGILKFlqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
342-559 |
5.89e-14 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 71.40 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 342 SNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL-RESISVVS 420
Cdd:TIGR03410 4 SNLNVYYGQSH--ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 421 QRVDILNG-TLRDNLLI------ARPEATDDH---LANILKDVglekllennaldswLGDGGRQLSGGEKRRIGIARAIL 490
Cdd:TIGR03410 82 QGREIFPRlTVEENLLTglaalpRRSRKIPDEiyeLFPVLKEM--------------LGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 491 HDAPILLLDEPTEGLD----KQTEHSIMTLFEKHfeGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKL 559
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQpsiiKDIGRVIRRLRAEG--GMAILLVEQYLdFARELADRYYVMERGRVVASGAGDEL 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
352-561 |
6.41e-14 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 71.54 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWN-ESQLRESISVVSQRVDILNG-T 429
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmHERARLGIGYLPQEASIFRKlT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 430 LRDNLLIA-------RPEATDDHLANILKDVGLEKLLENNALDswlgdggrqLSGGEKRRIGIARAILHDAPILLLDEPT 502
Cdd:TIGR04406 93 VEENIMAVleirkdlDRAEREERLEALLEEFQISHLRDNKAMS---------LSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 503 EGLDKQTEHSIMTLFEKHFEGKTVIFITHRLI--GLESMDSIVLIEQGEIVENGSHEKLLN 561
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHLKERGIGVLITDHNVreTLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
339-531 |
6.45e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.04 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTqwNESQLResiSV 418
Cdd:PRK11248 2 LQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER---GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILN-GTLRDNL-----LIARPEATDDHLA-NILKDVGLEkllennaldswlGDGGR---QLSGGEKRRIGIARA 488
Cdd:PRK11248 75 VFQNEGLLPwRNVQDNVafglqLAGVEKMQRLEIAhQMLKKVGLE------------GAEKRyiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2020526634 489 ILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITH 531
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
339-570 |
6.47e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.19 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAG--IELTQWNESQLRESI 416
Cdd:PRK13636 6 LKVEELNYNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 417 SVVSQR-----------VDILNGTLrdNLLIARPEaTDDHLANILKDVGLEKLleNNALDSWLgdggrqlSGGEKRRIGI 485
Cdd:PRK13636 85 GMVFQDpdnqlfsasvyQDVSFGAV--NLKLPEDE-VRKRVDNALKRTGIEHL--KDKPTHCL-------SFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 486 ARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE--GKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLL-- 560
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIdIVPLYCDNVFVMKEGRVILQGNPKEVFae 232
|
250
....*....|
gi 2020526634 561 NEAGRYFQLR 570
Cdd:PRK13636 233 KEMLRKVNLR 242
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
352-538 |
7.09e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 7.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISiagieltqWNESQLREsisvvsQRVDI------ 425
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL--------WQGEPIRR------QRDEYhqdlly 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 426 ---LNG-----TLRDNLLIARP---EATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAP 494
Cdd:PRK13538 79 lghQPGiktelTALENLRFYQRlhgPGDDEALWEALAQVGLAGFEDVPV---------RQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEKHFE-GKTVIFITHRLIGLES 538
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQHAEqGGMVILTTHQDLPVAS 194
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
352-538 |
7.36e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTqwnESQLRESISVVSQRvDILNGTL- 430
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLGHR-NAMKPALt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 -RDNLLI-ARPEATDD-HLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDK 507
Cdd:PRK13539 90 vAENLEFwAAFLGGEElDIAAALEAVGLAPLAHLPF---------GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180 190
....*....|....*....|....*....|..
gi 2020526634 508 QTEHSIMTLFEKHFE-GKTVIFITHRLIGLES 538
Cdd:PRK13539 161 AAVALFAELIRAHLAqGGIVIAATHIPLGLPG 192
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
354-533 |
9.20e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 354 NVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQW---NESQLR-ESISVVSQRVDIL-NG 428
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRnQKLGFIYQFHHLLpDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 429 TLRDN----LLI--ARPEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPT 502
Cdd:PRK11629 103 TALENvampLLIgkKKPAEINSRALEMLAAVGLEHRANHRP---------SELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|...
gi 2020526634 503 EGLDKQTEHSIMTLFEK--HFEGKTVIFITHRL 533
Cdd:PRK11629 174 GNLDARNADSIFQLLGElnRLQGTAFLVVTHDL 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
339-562 |
2.72e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.50 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERN----VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQ----WNes 410
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeenlWD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 411 qLRESISVVSQRVD--ILNGTLRD-------NLLIArPEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKR 481
Cdd:PRK13633 83 -IRNKAGMVFQNPDnqIVATIVEEdvafgpeNLGIP-PEEIRERVDESLKKVGMYEYRRHAP---------HLLSGGQKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 482 RIGIARAILHDAPILLLDEPTEGLD----KQTEHSIMTLFEKHfeGKTVIFITHRLIGLESMDSIVLIEQGEIVENGSHE 557
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKY--GITIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*
gi 2020526634 558 KLLNE 562
Cdd:PRK13633 230 EIFKE 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
320-562 |
8.64e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.99 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 320 SEPEvqfAEEKLDINKPLdITFSNVTFNYPDSERNVLNAVD---LTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGY 396
Cdd:TIGR03269 265 SEVE---KECEVEVGEPI-IKVRNVSKRYISVDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 397 ISI----AGIELTQ---WNESQLRESISVVSQRVDIL-NGTLRDNLLIARPEATDDHLAN-----ILKDVGLEKLLENNA 463
Cdd:TIGR03269 341 VNVrvgdEWVDMTKpgpDGRGRAKRYIGILHQEYDLYpHRTVLDNLTEAIGLELPDELARmkaviTLKMVGFDEEKAEEI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 464 LDSWlgdgGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTE----HSIMTLFEKHfeGKTVIFITHRL-IGLES 538
Cdd:TIGR03269 421 LDKY----PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKvdvtHSILKAREEM--EQTFIIVSHDMdFVLDV 494
|
250 260
....*....|....*....|....
gi 2020526634 539 MDSIVLIEQGEIVENGSHEKLLNE 562
Cdd:TIGR03269 495 CDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
359-560 |
8.83e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.66 E-value: 8.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 359 VDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVV----------SQRV-DILN 427
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIfqdpstslnpRQRIsQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 428 GTLRDNLLIArPEATDDHLANILKDVGlekLLENNAldswlGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDK 507
Cdd:PRK15112 112 FPLRLNTDLE-PEQREKQIIETLRQVG---LLPDHA-----SYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 508 QTEHSIMTLF----EKHfeGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLL 560
Cdd:PRK15112 183 SMRSQLINLMlelqEKQ--GISYIYVTQHLGMMKHIsDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
302-534 |
9.29e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 70.43 E-value: 9.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 302 QHLGQTLSSARRLNEVILSEPEVQFAEEKLDINKPLdITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKST 381
Cdd:PRK10938 225 QALVAQLAHSEQLEGVQLPEPDEPSARHALPANEPR-IVLNNGVVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKST 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 382 LIQLLT----------------------RYWDPKK--GYISiagieltqwneSQL----RESISVvsqRVDILNGTLrDN 433
Cdd:PRK10938 302 LLSLITgdhpqgysndltlfgrrrgsgeTIWDIKKhiGYVS-----------SSLhldyRVSTSV---RNVILSGFF-DS 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 434 LLIARpeATDDHLaNILKDVGLEKLlennALDSWLGDGG-RQLSGGEKRRIGIARAILHDAPILLLDEPTEGLD---KQ- 508
Cdd:PRK10938 367 IGIYQ--AVSDRQ-QKLAQQWLDIL----GIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnRQl 439
|
250 260 270
....*....|....*....|....*....|....*
gi 2020526634 509 ---------TEHSIMTLFEKHFEGKTVIFITHRLI 534
Cdd:PRK10938 440 vrrfvdvliSEGETQLLFVSHHAEDAPACITHRLE 474
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
343-560 |
9.65e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.47 E-value: 9.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQR 422
Cdd:PRK10253 12 QLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 423 VDIlNGTLRDNLLIAR------PEAT------DDHLANILKDVGLEKlLENNALDSwlgdggrqLSGGEKRRIGIARAIL 490
Cdd:PRK10253 90 ATT-PGDITVQELVARgryphqPLFTrwrkedEEAVTKAMQATGITH-LADQSVDT--------LSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 491 HDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLL 560
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSElnREKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
369-554 |
1.14e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 67.82 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 369 VAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAgieltqwnesqlRESISVVSQRVDI-LNGTLRDNLLiarpEATDDHLA 447
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE------------LDTVSYKPQYIKAdYEGTVRDLLS----SITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 448 N------ILKDVGLEKLLENNALDswlgdggrqLSGGEKRRIGIARAILHDAPILLLDEPTEGLDkqTEHSIM-TLFEKH 520
Cdd:cd03237 92 HpyfkteIAKPLQIEQILDREVPE---------LSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMaSKVIRR 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 2020526634 521 F---EGKTVIFITHRLIGLESMDSIVLIEQGEIVENG 554
Cdd:cd03237 161 FaenNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNG 197
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
361-549 |
1.41e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 67.78 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 361 LTIPATNKV-AIVGQTGSGKSTLIQLLTRYWDPKKGYIS-----------IAGIELTQWNESQLRESISVV--SQRVDIL 426
Cdd:cd03236 20 LPVPREGQVlGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNYFTKLLEGDVKVIvkPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 427 ----NGTLRDNLliarpEATDDH--LANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDE 500
Cdd:cd03236 100 pkavKGKVGELL-----KKKDERgkLDELVDQLELRHVLDRNI---------DQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2020526634 501 PTEGLD-KQTEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVLIEQGE 549
Cdd:cd03236 166 PSSYLDiKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGE 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
352-557 |
7.20e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.86 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPK--KGYISIAGIELTQWN-ESQLRESISVVSQRvdilng 428
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPpEERARLGIFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 429 tlrdnlliarPEAtddhlaniLKDVGLEKLLENnaldswLGDGgrqLSGGEKRRIGIARAILHDAPILLLDEPTEGLD-- 506
Cdd:cd03217 86 ----------PPE--------IPGVKNADFLRY------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDid 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 507 --KQTEHSIMTLFEkhfEGKTVIFITH--RLIGLESMDSIVLIEQGEIVENGSHE 557
Cdd:cd03217 139 alRLVAEVINKLRE---EGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
352-564 |
7.88e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.47 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLT---RYwDPKKGYISIAGIELTQWN-ESQLRESISVVSQR-VDIL 426
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghpKY-EVTSGSILLDGEDILELSpDERARAGIFLAFQYpVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 427 NGTLRDNLLIA---------RPEATDDHLANILKDVGLEKllenNALDSWLGDGgrqLSGGEKRRIGIARAILHDAPILL 497
Cdd:COG0396 91 GVSVSNFLRTAlnarrgeelSAREFLKLLKEKMKELGLDE----DFLDRYVNEG---FSGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 498 LDEPTEGLD----KQTEHSIMTLfekHFEGKTVIFITH--RLIGLESMDSIVLIEQGEIVENGSHE--KLLNEAG 564
Cdd:COG0396 164 LDETDSGLDidalRIVAEGVNKL---RSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElaLELEEEG 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
319-531 |
8.48e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.89 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 319 LSEPEVQFAEEKL--DINKPLDITFSNVTFNYPDSERNvLNAVDLTIPATN-----KVAIVGQTGSGKSTLIQLLTRYWD 391
Cdd:COG1245 313 LPEENVRIRDEPIefEVHAPRREKEEETLVEYPDLTKS-YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 392 PKKGYIsiagieltqwnESQLResISVVSQRVDI-LNGTLRDNLLIARPEATDDHLAN--ILKDVGLEKLLENNAldswl 468
Cdd:COG1245 392 PDEGEV-----------DEDLK--ISYKPQYISPdYDGTVEEFLRSANTDDFGSSYYKteIIKPLGLEKLLDKNV----- 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 469 gdggRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQtEHSIMTLFEKHF---EGKTVIFITH 531
Cdd:COG1245 454 ----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-QRLAVAKAIRRFaenRGKTAMVVDH 514
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
339-532 |
1.17e-11 |
|
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: 67.47 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSERnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieltqwnesqlRESISV 418
Cdd:TIGR00954 452 IKFENIPLVTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFY 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDNllIARPEATDDHLANILKDVGLEKLLENNALDSWLGDGG---------RQLSGGEKRRIGIARAI 489
Cdd:TIGR00954 520 VPQRPYMTLGTLRDQ--IIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLF 597
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMTLFEKHfeGKTVIFITHR 532
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
353-559 |
1.23e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.40 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQlrESISVVSQRVDIL-NGTLR 431
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 432 DNLLIARPEatdDHLANILKDVGLEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQ--- 508
Cdd:PRK11607 110 QNIAFGLKQ---DKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrd 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 509 -TEHSIMTLFEKhfEGKTVIFITHRLIGLESMDS-IVLIEQGEIVENGSHEKL 559
Cdd:PRK11607 187 rMQLEVVDILER--VGVTCVMVTHDQEEAMTMAGrIAIMNRGKFVQIGEPEEI 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
354-533 |
1.23e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 354 NVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRE-SISVVSQRVDIL-NGTLR 431
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 432 DNLL--IARPEATDDHLANILKDVGLEKLLENNAldSWLGDGGRQLsggekrrIGIARAILHDAPILLLDEPTEGLdkqT 509
Cdd:PRK15439 105 ENILfgLPKRQASMQKMKQLLAALGCQLDLDSSA--GSLEVADRQI-------VEILRGLMRDSRILILDEPTASL---T 172
|
170 180
....*....|....*....|....*...
gi 2020526634 510 EHSIMTLFEK----HFEGKTVIFITHRL 533
Cdd:PRK15439 173 PAETERLFSRirelLAQGVGIVFISHKL 200
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
339-506 |
1.46e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.75 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISiagieltqwNESQLResISV 418
Cdd:PRK09544 5 VSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDiLNGTLR---DNLLIARPEATDDHLANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPI 495
Cdd:PRK09544 72 VPQKLY-LDTTLPltvNRFLRLRPGTKKEDILPALKRVQAGHLIDAPM---------QKLSGGETQRVLLARALLNRPQL 141
|
170
....*....|.
gi 2020526634 496 LLLDEPTEGLD 506
Cdd:PRK09544 142 LVLDEPTQGVD 152
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
359-533 |
1.47e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.19 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 359 VDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWD-----PKKGYISIAGIEL--TQWNESQLRESISVVSQRVDILNGTLR 431
Cdd:PRK14243 29 VWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 432 DNllIARPEATDDHLANIlkDVGLEKLLENNALdsW------LGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGL 505
Cdd:PRK14243 109 DN--IAYGARINGYKGDM--DELVERSLRQAAL--WdevkdkLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180
....*....|....*....|....*...
gi 2020526634 506 DKQTEHSIMTLFEKHFEGKTVIFITHRL 533
Cdd:PRK14243 183 DPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-555 |
1.55e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 342 SNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAG--IELTQWNESQLRESISVV 419
Cdd:PRK13638 5 SDLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 420 SQRVD--ILNGTLrdnlliarpeatDDHLANILKDVGLEKLLENNALDSWL----GDGGRQ-----LSGGEKRRIGIARA 488
Cdd:PRK13638 83 FQDPEqqIFYTDI------------DSDIAFSLRNLGVPEAEITRRVDEALtlvdAQHFRHqpiqcLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 489 ILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHF-EGKTVIFITHRL-IGLESMDSIVLIEQGEIVENGS 555
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIdLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-560 |
2.16e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.48 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 351 SERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPK-----KGYISIAG--IELTQWNESQLRESISVVSQ-- 421
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGrnIYSPDVDPIEVRREVGMVFQyp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 422 ----RVDILNGT---LRDNLLIARPEATDDHLANILKDVGLEKLLENNaldswLGDGGRQLSGGEKRRIGIARAILHDAP 494
Cdd:PRK14267 95 npfpHLTIYDNVaigVKLNGLVKSKKELDERVEWALKKAALWDEVKDR-----LNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKLL 560
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVF 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
339-565 |
3.68e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ-LRESIS 417
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQ-RVDILNGTLRDNLLIARPEATDDHLANILKDVG--LEKLLENNALDSwlgdggRQLSGGEKRRIGIARAILHDAP 494
Cdd:PRK11614 84 IVPEgRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYelFPRLHERRIQRA------GTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 495 ILLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLI--GLESMDSIVLIEQGEIV-ENGSHEKLLNEAGR 565
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVlEDTGDALLANEAVR 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
352-532 |
4.29e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTR--YWDPKKGYISIAGIELtqWNESQLRESISV---VSQRVDIL 426
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQF--GREASLIDAIGRkgdFKDAVELL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 427 NGT-LRDN-LLIARPeatddhlanilkdvglekllennaldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPTEG 504
Cdd:COG2401 120 NAVgLSDAvLWLRRF---------------------------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|..
gi 2020526634 505 LDKQT----EHSIMTLFEKHfeGKTVIFITHR 532
Cdd:COG2401 167 LDRQTakrvARNLQKLARRA--GITLVVATHH 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
356-533 |
4.91e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRES-ISVVSQR---VDILngTLR 431
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQHfmlVPNL--TVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 432 DNLLIARP---------EATDDHLANILKDVGLEklLENNALDSwlgdggrQLSGGEKRRIGIARAILHDAPILLLDEPT 502
Cdd:COG3845 99 ENIVLGLEptkggrldrKAARARIRELSERYGLD--VDPDAKVE-------DLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 2020526634 503 EGLDKQ-TEHsimtLFE--KHF--EGKTVIFITHRL 533
Cdd:COG3845 170 AVLTPQeADE----LFEilRRLaaEGKSIIFITHKL 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
339-533 |
6.39e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.87 E-value: 6.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWD--PK---KGYISIAG--IELTQWNESQ 411
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGhnIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 412 LRESISVVSQRVDILNGTLRDNLL-------IARPEATDDHLANILKDVGLEKLLENNALDSWLGdggrqLSGGEKRRIG 484
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVyglrlkgIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALG-----LSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 485 IARAILHDAPILLLDEPTEGLD----KQTEHSIMTLFEKHfegkTVIFITHRL 533
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDpisaGKIEETLLGLKDDY----TMLLVTRSM 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
357-561 |
8.66e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.70 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 357 NAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL-RESISVVSQRVDILNG-TLRDNL 434
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFREmTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 435 LIARPEatddHL-ANILKdvGLEKL-----LENNALDS---WLGDGG------RQ---LSGGEKRRIGIARAILHDAPIL 496
Cdd:PRK11300 102 LVAQHQ----QLkTGLFS--GLLKTpafrrAESEALDRaatWLERVGllehanRQagnLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 497 LLDEPTEGLD-KQTE---HSIMTLFEKHfeGKTVIFITH--RLIgLESMDSIVLIEQGEIVENGSHEKLLN 561
Cdd:PRK11300 176 MLDEPAAGLNpKETKeldELIAELRNEH--NVTVLLIEHdmKLV-MGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
340-531 |
1.09e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 340 TFSNVTFNYPdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLltrywdpkkgyisIAGIE---------------- 403
Cdd:TIGR03719 6 TMNRVSKVVP-PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI-------------MAGVDkdfngearpqpgikvg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 404 -LTQwnESQLRESISV-------VSQRVDILNGTLRDNLLIARPEATDDHLANilKDVGLEKLLEnnALDSWlgDGGRQ- 474
Cdd:TIGR03719 72 yLPQ--EPQLDPTKTVrenveegVAEIKDALDRFNEISAKYAEPDADFDKLAA--EQAELQEIID--AADAW--DLDSQl 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 475 ------------------LSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQT----EHsimtlFEKHFEGkTVIFITH 531
Cdd:TIGR03719 144 eiamdalrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlER-----HLQEYPG-TVVAVTH 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
353-562 |
1.26e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.83 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISI--AGIELTQWNEsQLRESISVVSQRVDILNG-T 429
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddEDISLLPLHA-RARRGIGYLPQEASIFRRlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 430 LRDNLLiARPEATDDHLANILKDVGlEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQT 509
Cdd:PRK10895 95 VYDNLM-AVLQIRDDLSAEQREDRA-NELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 510 EHSIMTLFEKHFEGKTVIFITHRLI--GLESMDSIVLIEQGEIVENGSHEKLLNE 562
Cdd:PRK10895 173 VIDIKRIIEHLRDSGLGVLITDHNVreTLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
329-559 |
1.73e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 329 EKLDINKPLDITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAG------- 401
Cdd:PRK10261 5 DELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 402 ---IELTQWNESQLRE----SISVVSQR-------VDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLENNALdsw 467
Cdd:PRK10261 85 rqvIELSEQSAAQMRHvrgaDMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTI--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 468 LGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFE--KHFEGKTVIFITHRL-IGLESMDSIVL 544
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMgVVAEIADRVLV 241
|
250
....*....|....*
gi 2020526634 545 IEQGEIVENGSHEKL 559
Cdd:PRK10261 242 MYQGEAVETGSVEQI 256
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
361-545 |
1.80e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.65 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 361 LTIPATNKV-AIVGQTGSGKSTLIQLLT--------RY-----WDPKKGYISiaGIELTQWNESQLRESISVV--SQRVD 424
Cdd:COG1245 93 LPVPKKGKVtGILGPNGIGKSTALKILSgelkpnlgDYdeepsWDEVLKRFR--GTELQDYFKKLANGEIKVAhkPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 425 ----ILNGTLRDnLLiarpEATDDH--LANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPILLL 498
Cdd:COG1245 171 lipkVFKGTVRE-LL----EKVDERgkLDELAEKLGLENILDRDI---------SELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 499 DEPTEGLD-KQ---TEHSIMTLFEkhfEGKTVIFITHRLIGLESM-DSIVLI 545
Cdd:COG1245 237 DEPSSYLDiYQrlnVARLIRELAE---EGKYVLVVEHDLAILDYLaDYVHIL 285
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
359-550 |
2.07e-10 |
|
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: 60.14 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 359 VDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRES-ISVVSQ-RVD---ILNGTLRDN 433
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEdRKReglVLDLSVAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 434 LLIarpeatddhlanilkdvglekllennaldswlgdgGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLD---KQTE 510
Cdd:cd03215 99 IAL-----------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDvgaKAEI 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2020526634 511 HSIMTLFEKhfEGKTVIFIT---HRLIGLesMDSIVLIEQGEI 550
Cdd:cd03215 144 YRLIRELAD--AGKAVLLISselDELLGL--CDRILVMYEGRI 182
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
339-554 |
2.50e-10 |
|
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: 60.62 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDS--------------------ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYIS 398
Cdd:cd03220 1 IELENVSKSYPTYkggssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 399 IAG-----IELTQWNESQL--RESIsvvsqrvdILNGTlrdnLLIARPEATDDHLANILKDVGLEKllennALDSWLgdg 471
Cdd:cd03220 81 VRGrvsslLGLGGGFNPELtgRENI--------YLNGR----LLGLSRKEIDEKIDEIIEFSELGD-----FIDLPV--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 472 gRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQT-EHSIMTLFEKHFEGKTVIFITHRLIGLESM-DSIVLIEQGE 549
Cdd:cd03220 141 -KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFqEKCQRRLRELLKQGKTVILVSHDPSSIKRLcDRALVLEKGK 219
|
....*
gi 2020526634 550 IVENG 554
Cdd:cd03220 220 IRFDG 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
369-563 |
2.71e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.01 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 369 VAIVGQTGSGKSTLIQL---LTRYwdpkKGYISIAGIELTQWNESQLRESISVVSQRVDILNGTLRDNLL------IARP 439
Cdd:COG4138 25 IHLIGPNGAGKSTLLARmagLLPG----QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLalhqpaGASS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 440 EATDDHLANILKDVGLEKLLennaldswlgdgGR---QLSGGEKRRIGIARAILH-------DAPILLLDEPTEGLDKQT 509
Cdd:COG4138 101 EAVEQLLAQLAEALGLEDKL------------SRpltQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 510 EHSIMTLFEKHFE-GKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLNEA 563
Cdd:COG4138 169 QAALDRLLRELCQqGITVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVMTPE 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
337-533 |
3.33e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.66 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 337 LDITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKS----TLIQLLTrywdpKKGYIS----IAGIELTQWN 408
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLA-----ANGRIGgsatFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 409 ESQLR----ESISVVSQR-VDILNGTLRdnlliarpeaTDDHLANIL---KDVGLEKLLENNA--LDSWLGDGGRQ---- 474
Cdd:PRK09473 88 EKELNklraEQISMIFQDpMTSLNPYMR----------VGEQLMEVLmlhKGMSKAEAFEESVrmLDAVKMPEARKrmkm 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 475 ----LSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFE--KHFEGKTVIFITHRL 533
Cdd:PRK09473 158 ypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDL 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
361-545 |
3.47e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 361 LTIPATNKV-AIVGQTGSGKSTLIQLLT--------RY-----WDP--KKgyisIAGIELTQWNEsQLRE-SISVV--SQ 421
Cdd:PRK13409 93 LPIPKEGKVtGILGPNGIGKTTAVKILSgelipnlgDYeeepsWDEvlKR----FRGTELQNYFK-KLYNgEIKVVhkPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 422 RVDI----LNGTLRDnLLiarpEATDDH--LANILKDVGLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAPI 495
Cdd:PRK13409 168 YVDLipkvFKGKVRE-LL----KKVDERgkLDEVVERLGLENILDRDI---------SELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 496 LLLDEPTEGLDKQTEHSIMTLFEKHFEGKTVIFITHRLIGLESM-DSIVLI 545
Cdd:PRK13409 234 YFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYLaDNVHIA 284
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
359-561 |
5.26e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 359 VDLTIPATNKVAIVGQTGSGKS----TLIQLLTRYWDPKKGYISIAGIELTqwnESQLR-ESISVVSQR-------VDIL 426
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRgRKIATIMQNprsafnpLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 427 NGTLRDNLLIARPEATDDHLANILKDVGLE---KLLENNALdswlgdggrQLSGGEKRRIGIARAILHDAPILLLDEPTE 503
Cdd:PRK10418 99 HTHARETCLALGKPADDATLTAALEAVGLEnaaRVLKLYPF---------EMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 504 GLDKQTEHSIMTLFEKHFE--GKTVIFITH------RLiglesMDSIVLIEQGEIVENGSHEKLLN 561
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQkrALGMLLVTHdmgvvaRL-----ADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
369-531 |
6.60e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 369 VAIVGQTGSGKSTLIQLLTRYWDPKKGYISIagiELTqwnesqlresISVVSQRVDI-LNGTLRDNLLIARPEATDDHL- 446
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK----------ISYKPQYIKPdYDGTVEDLLRSITDDLGSSYYk 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 447 ANILKDVGLEKLLENNaldswLGDggrqLSGGEKRRIGIARAILHDAPILLLDEPTEGLDkqTEHSIMT------LFEKH 520
Cdd:PRK13409 435 SEIIKPLQLERLLDKN-----VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLAVakairrIAEER 503
|
170
....*....|.
gi 2020526634 521 feGKTVIFITH 531
Cdd:PRK13409 504 --EATALVVDH 512
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
356-559 |
1.22e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.11 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVD---LTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESisvvsqRVDI------- 425
Cdd:PRK15079 34 LKAVDgvtLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAV------RSDIqmifqdp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 426 ---LNGTLRDNLLIARP----------EATDDHLANILKDVGLEKLLENNAldswlgdgGRQLSGGEKRRIGIARAILHD 492
Cdd:PRK15079 108 lasLNPRMTIGEIIAEPlrtyhpklsrQEVKDRVKAMMLKVGLLPNLINRY--------PHEFSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 493 APILLLDEPTEGLDKQTEHSIMTLFEK-HFE-GKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKL 559
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQlQREmGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
306-531 |
1.49e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 306 QTLSSARRLNEVILSE--------PEVQFAEEKLDINKPLDITfsNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGS 377
Cdd:PRK15064 281 QATSRAKQIDKIKLEEvkpssrqnPFIRFEQDKKLHRNALEVE--NLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 378 GKSTLIQLLTRYWDPKKGYIsiagieltQWNESQlreSISVVSQRV--DILNG-TLRDNLLIARPEATDDHLANILkdvg 454
Cdd:PRK15064 357 GKTTLLRTLVGELEPDSGTV--------KWSENA---NIGYYAQDHayDFENDlTLFDWMSQWRQEGDDEQAVRGT---- 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 455 LEKLL--ENNALDSwlgdgGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKhFEGkTVIFITH 531
Cdd:PRK15064 422 LGRLLfsQDDIKKS-----VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEK-YEG-TLIFVSH 493
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
338-554 |
1.52e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.04 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 338 DITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQlrESIS 417
Cdd:PRK11000 3 SVTLRNVTKAYGDVV--ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQRVDI---LNgtLRDN----LLIARPEATD-----DHLANILKdvgLEKLLEnnaldswlgdggRQ---LSGGEKRR 482
Cdd:PRK11000 79 MVFQSYALyphLS--VAENmsfgLKLAGAKKEEinqrvNQVAEVLQ---LAHLLD------------RKpkaLSGGQRQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 483 IGIARAILHDAPILLLDEPTEGLDK----QTEHSIMTLFEKHfeGKTVIFITHRLIglESM---DSIVLIEQGEIVENG 554
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDAalrvQMRIEISRLHKRL--GRTMIYVTHDQV--EAMtlaDKIVVLDAGRVAQVG 216
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
336-548 |
1.65e-09 |
|
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: 57.64 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 336 PLDITFSNVTF--NYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPK--KGYISIAGIELTQwnesQ 411
Cdd:cd03232 1 GSVLTWKNLNYtvPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 412 LRESISVVSQrVDILNG--TLRDNLLIArpeatddhlANIlkdvglekllennaldswlgdggRQLSGGEKRRIGIARAI 489
Cdd:cd03232 77 FQRSTGYVEQ-QDVHSPnlTVREALRFS---------ALL-----------------------RGLSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHR---LIgLESMDSIVLIEQG 548
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQpsaSI-FEKFDRLLLLKRG 185
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
352-550 |
1.72e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.57 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIA-GIELTQWNESQLResisvvSQRVDilNGTL 430
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLE------FLRAD--ESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 RDNLLIArPEATDDHLANILKDVGL--EKLLENNAldswlgdggrQLSGGEKRRIGIARAILHDAPILLLDEPTEGLD-- 506
Cdd:PRK10636 396 QHLARLA-PQELEQKLRDYLGGFGFqgDKVTEETR----------RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDld 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2020526634 507 -KQ--TEHSImtlfekHFEGKTVIFITHRLIGLESMDSIVLIEQGEI 550
Cdd:PRK10636 465 mRQalTEALI------DFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
352-568 |
1.82e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPK--KGYISIAGIELTQwnesQLRESISVVSQRvDIL--N 427
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK----QILKRTGFVTQD-DILypH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 428 GTLRDNLL------IARPEATDDHLA---NILKDVGLEKLlENNAL-DSWLgdggRQLSGGEKRRIGIARAILHDAPILL 497
Cdd:PLN03211 155 LTVRETLVfcsllrLPKSLTKQEKILvaeSVISELGLTKC-ENTIIgNSFI----RGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 498 LDEPTEGLDKQTEHS-IMTLFEKHFEGKTVIFITHRLIG--LESMDSIVLIEQGEIVENGSheklLNEAGRYFQ 568
Cdd:PLN03211 230 LDEPTSGLDATAAYRlVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGK----GSDAMAYFE 299
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
339-531 |
1.99e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTR--------------------YWDPKKG--- 395
Cdd:PRK11147 4 ISIHGAWLSFSDAP--LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlQQDPPRNveg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 396 ----YISiAGIEltqwNESQLRESISVVSQRVDIlngTLRDNLL--IARPEATDDH-----LANILKDVgLEKL-LENNA 463
Cdd:PRK11147 82 tvydFVA-EGIE----EQAEYLKRYHDISHLVET---DPSEKNLneLAKLQEQLDHhnlwqLENRINEV-LAQLgLDPDA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 464 LDSwlgdggrQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTehsIMTL--FEKHFEGkTVIFITH 531
Cdd:PRK11147 153 ALS-------SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLegFLKTFQG-SIIFISH 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
352-555 |
2.66e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.78 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAG-----IELTQwnesqlresisvvsqrvdIL 426
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsalLELGA------------------GF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 427 NG--TLRDNL-LIAR-----PEATDDHLANILKDVGLEKllennALDSWLgdggRQLSGGEKRRIGIARAILHDAPILLL 498
Cdd:COG1134 100 HPelTGRENIyLNGRllglsRKEIDEKFDEIVEFAELGD-----FIDQPV----KTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 499 DEPTEGLDKQ-TEHSIMTLFEKHFEGKTVIFITHrligleSMDSI-------VLIEQGEIVENGS 555
Cdd:COG1134 171 DEVLAVGDAAfQKKCLARIRELRESGRTVIFVSH------SMGAVrrlcdraIWLEKGRLVMDGD 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
355-559 |
2.69e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.96 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 355 VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQwNESQLREsISVVSQRVDIL-NGTLRDN 433
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQQRD-ICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 434 L-----LIARP-EATDDHLANILKDVGLEKLlENNALDswlgdggrQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDK 507
Cdd:PRK11432 99 VgyglkMLGVPkEERKQRVKEALELVDLAGF-EDRYVD--------QISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 508 QTEHSIMtlfEKHFE-----GKTVIFITH-RLIGLESMDSIVLIEQGEIVENGSHEKL 559
Cdd:PRK11432 170 NLRRSMR---EKIRElqqqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
347-554 |
2.89e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.56 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 347 NYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQlltrywdpkkgyisiAGIEltqwnESQLRESISVVSqrvdil 426
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------EGLY-----ASGKARLISFLP------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 427 ngTLRDNLLIARpeatdDHLANILkDVGLEKLLENNALDSwlgdggrqLSGGEKRRIGIARAI-LHDAPIL-LLDEPTEG 504
Cdd:cd03238 56 --KFSRNKLIFI-----DQLQFLI-DVGLGYLTLGQKLST--------LSGGELQRVKLASELfSEPPGTLfILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 505 LDKQTEHSIMTLFEKHF-EGKTVIFITHRLIGLESMDSIVLI------EQGEIVENG 554
Cdd:cd03238 120 LHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
353-506 |
2.90e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 57.73 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKST-------LIQlltrywdPKKGYISIAGIELTQWNESQ-LRESISVVSQRVD 424
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVK-------PDSGRIFLDGEDITHLPMHKrARLGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 425 ILNG-TLRDNLLIAR------PEATDDHLANILKDVGLEKLLENNALdswlgdggrQLSGGEKRRIGIARAILHDAPILL 497
Cdd:COG1137 89 IFRKlTVEDNILAVLelrklsKKEREERLEELLEEFGITHLRKSKAY---------SLSGGERRRVEIARALATNPKFIL 159
|
....*....
gi 2020526634 498 LDEPTEGLD 506
Cdd:COG1137 160 LDEPFAGVD 168
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
356-551 |
5.73e-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: 58.68 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRY-----WDpkkGYISIAGIELTQWNESQL-RESISVVSQRVDIL-NG 428
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtWD---GEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 429 TLRDNLL----IARPEATDDHLANILKDVGLEKLLENNALDSWLGDGgrQLSGGEKRRIGIARAILHDAPILLLDEPTEG 504
Cdd:TIGR02633 94 SVAENIFlgneITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVG--DYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2020526634 505 LDKQtEHSIMTLFEKHFEGKTV--IFITHRLIGLESM-DSIVLIEQGEIV 551
Cdd:TIGR02633 172 LTEK-ETEILLDIIRDLKAHGVacVYISHKLNEVKAVcDTICVIRDGQHV 220
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
352-564 |
7.81e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRY--WDPKKGYISIAGIELTQWN-ESQLRESISVVSQR-VDILN 427
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpEERAHLGIFLAFQYpIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 428 GTLRDNLLIA---------RPEATD----DHLANILKDVGL-EKLLENNaldswLGDGgrqLSGGEKRRIGIARAILHDA 493
Cdd:CHL00131 99 VSNADFLRLAynskrkfqgLPELDPleflEIINEKLKLVGMdPSFLSRN-----VNEG---FSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020526634 494 PILLLDEPTEGLD----KQTEHSIMTLFEKhfeGKTVIFITH--RLIGLESMDSIVLIEQGEIVENGSHE--KLLNEAG 564
Cdd:CHL00131 171 ELAILDETDSGLDidalKIIAEGINKLMTS---ENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKG 246
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
352-559 |
1.02e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.70 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 352 ERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL---RESISVVSQRVDILNG 428
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 429 -TLRDNllIARPEATDDHL-ANILKDVGLEKLlENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLD 506
Cdd:PRK11831 99 mNVFDN--VAYPLREHTQLpAPLLHSTVMMKL-EAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 507 KQTEHSIMTLFEK--HFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVENGSHEKL 559
Cdd:PRK11831 176 PITMGVLVKLISElnSALGVTCVVVSHDVPEVLSIaDHAYIVADKKIVAHGSAQAL 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
456-572 |
1.03e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.44 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 456 EKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHF-EGKTVIFITHRLI 534
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYME 205
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2020526634 535 GLESM-DSIVLIEQGEIVENGSHEKLLNE-AGRYFQLRQA 572
Cdd:NF000106 206 EAEQLaHELTVIDRGRVIADGKVDELKTKvGGRTLQIRPA 245
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
368-531 |
1.25e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 368 KVAIVGQTGSGKSTLIQLltrywdpkkgyisIAGIE-----------------LTQwnESQLRESISV-------VSQRV 423
Cdd:PRK11819 35 KIGVLGLNGAGKSTLLRI-------------MAGVDkefegearpapgikvgyLPQ--EPQLDPEKTVrenveegVAEVK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 424 DILNGTLRDNLLIARPEATDDHLAnilKDVG-LEKLLEnnALDSWlgDGGRQ-------------------LSGGEKRRI 483
Cdd:PRK11819 100 AALDRFNEIYAAYAEPDADFDALA---AEQGeLQEIID--AADAW--DLDSQleiamdalrcppwdakvtkLSGGERRRV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 484 GIARAILHDAPILLLDEPTEGLDKQT----EHsimtlFEKHFEGkTVIFITH 531
Cdd:PRK11819 173 ALCRLLLEKPDMLLLDEPTNHLDAESvawlEQ-----FLHDYPG-TVVAVTH 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
339-506 |
1.26e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYPDSE---RNVLNAVDLTipatNKVAIVGQTGSGKSTLIQLLTRYWDPKKGyisiagielTQWNESQLRes 415
Cdd:PLN03073 509 ISFSDASFGYPGGPllfKNLNFGIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSG---------TVFRSAKVR-- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 416 ISVVSQR-VDILNGTLRDNLLIAR--PEATDDHLANILKDVGLEKlleNNALDSWLgdggrQLSGGEKRRIGIARAILHD 492
Cdd:PLN03073 574 MAVFSQHhVDGLDLSSNPLLYMMRcfPGVPEQKLRAHLGSFGVTG---NLALQPMY-----TLSGGQKSRVAFAKITFKK 645
|
170
....*....|....
gi 2020526634 493 APILLLDEPTEGLD 506
Cdd:PLN03073 646 PHILLLDEPSNHLD 659
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
356-549 |
1.58e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTR-Y----WDpkkGYISIAGIELTQWN--ESQlRESISVVSQRVDIL-N 427
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYphgtYE---GEIIFEGEELQASNirDTE-RAGIAIIHQELALVkE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 428 GTLRDNLLIARpEATDDHLANILK-DVGLEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGL- 505
Cdd:PRK13549 97 LSVLENIFLGN-EITPGGIMDYDAmYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLt 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2020526634 506 DKQTEH--SIMTLFEKHfeGKTVIFITHRLIGLESM-DSIVLIEQGE 549
Cdd:PRK13549 176 ESETAVllDIIRDLKAH--GIACIYISHKLNEVKAIsDTICVIRDGR 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
367-539 |
3.96e-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: 52.76 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 367 NKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVvsqrvdilngtlrdnlliarpeatddhl 446
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV---------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 447 anilkdvglekllennaldswlGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFE-------K 519
Cdd:smart00382 55 ----------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllllK 112
|
170 180
....*....|....*....|
gi 2020526634 520 HFEGKTVIFITHRLIGLESM 539
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPA 132
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
370-533 |
4.38e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 370 AIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRES-ISVVSQRVDIL-NGTLRDNLLIARpEATdDHLA 447
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIpQLTIAENIFLGR-EFV-NRFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 448 NIL-------KDVGLEKLLENNALDSWLGDggrqLSGGEKRRIGIARAILHDAPILLLDEPTEGL-DKQTEhsimTLF-- 517
Cdd:PRK10762 112 RIDwkkmyaeADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETE----SLFrv 183
|
170
....*....|....*...
gi 2020526634 518 --EKHFEGKTVIFITHRL 533
Cdd:PRK10762 184 irELKSQGRGIVYISHRL 201
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
474-543 |
1.19e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.59 E-value: 1.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020526634 474 QLSGGEKRRIGIArAILH-----DAPILLLDEPTEGLDKQTEHSIMTLFEKHF-EGKTVIFITHRLIGLESMDSIV 543
Cdd:cd03227 77 QLSGGEKELSALA-LILAlaslkPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
351-562 |
1.50e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 351 SERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQ----LLtrywdPKKGYISIAGIELTQWNESQLRESISVVSQR---- 422
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtpp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 423 --VDI---LNGTLRDNLLIARPEATDDHLANILKdvgLEKLLENNAldswlgdggRQLSGGEKRRIGIARAILHDAP--- 494
Cdd:PRK03695 82 faMPVfqyLTLHQPDKTRTEAVASALNEVAEALG---LDDKLGRSV---------NQLSGGEWQRVRLAAVVLQVWPdin 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 495 ----ILLLDEPTEGLDKQTEHSIMTLFEKHFE-GKTVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLNE 562
Cdd:PRK03695 150 pagqLLLLDEPMNSLDVAQQAALDRLLSELCQqGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
356-533 |
2.78e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 356 LNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ-LRESISVVSQRVD-ILNGTLRDN 433
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNlVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 434 LLIARPEATD---DHlANILKDVglEKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGL-DKQT 509
Cdd:PRK10982 94 MWLGRYPTKGmfvDQ-DKMYRDT--KAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtEKEV 170
|
170 180
....*....|....*....|....*
gi 2020526634 510 EHsIMTLFEKHFE-GKTVIFITHRL 533
Cdd:PRK10982 171 NH-LFTIIRKLKErGCGIVYISHKM 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
339-554 |
2.90e-07 |
|
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: 51.11 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYP--DSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPK---KGYISIAGIELTQWNESQLR 413
Cdd:cd03233 4 LSWRNISFTTGkgRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 414 ESISVVSQRVDILNGTLRDNLLIARpeatddhlanilkdvgleKLLENNALdswlgdggRQLSGGEKRRIGIARAILHDA 493
Cdd:cd03233 84 EIIYVSEEDVHFPTLTVRETLDFAL------------------RCKGNEFV--------RGISGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 494 PILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHR--LIGLESMDSIVLIEQGEIVENG 554
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEILKCIRTmaDVLKTTTFVSLYQasDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
370-546 |
3.56e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.07 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 370 AIVGQTGSGKSTLIQLLT-------------RYWDPK---KGYiSIAGIELTQWNESQLResiSVVSQRVDILngtlrDN 433
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltgelppnskgGAHDPKlirEGE-VRAQVKLAFENANGKK---YTITRSLAIL-----EN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 434 LLIARPEATDdhlanilkdvgleKLLENNAldswlgdgGRqLSGGEKR------RIGIARAILHDAPILLLDEPTEGLDK 507
Cdd:cd03240 97 VIFCHQGESN-------------WPLLDMR--------GR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2020526634 508 -QTEHSIMTLFE--KHFEGKTVIFITH--RLigLESMDSIVLIE 546
Cdd:cd03240 155 eNIEESLAEIIEerKSQKNFQLIVITHdeEL--VDAADHIYRVE 196
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
327-539 |
3.77e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.48 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 327 AEEKLDI----NKPLDITFSNVTFNYPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGI 402
Cdd:TIGR01257 1922 AEERQRIisggNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK 2001
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 403 ELTQwNESQLRESISVVSQRV---DILNGtlRDNL-LIAR----PEATDDHLANI-LKDVGLEKLLENNAldswlgdggR 473
Cdd:TIGR01257 2002 SILT-NISDVHQNMGYCPQFDaidDLLTG--REHLyLYARlrgvPAEEIEKVANWsIQSLGLSLYADRLA---------G 2069
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 474 QLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTE----HSIMTLFEkhfEGKTVIFITHRLIGLESM 539
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARrmlwNTIVSIIR---EGRAVVLTSHSMEECEAL 2136
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
369-554 |
3.83e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.47 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 369 VAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAG-----IELTQWNESQ----LRESISVVSQRVdilngtlRDNLliaRP 439
Cdd:PRK11701 35 LGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAErrrlLRTEWGFVHQHP-------RDGL---RM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 440 EATDDhlANI---LKDVGLEKL--LENNALDsWLG----------DGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEG 504
Cdd:PRK11701 105 QVSAG--GNIgerLMAVGARHYgdIRATAGD-WLErveidaaridDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGG 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2020526634 505 LDKQTEHSIMTLFEK--HFEGKTVIFITH-----RLIGlesmDSIVLIEQGEIVENG 554
Cdd:PRK11701 182 LDVSVQARLLDLLRGlvRELGLAVVIVTHdlavaRLLA----HRLLVMKQGRVVESG 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
306-531 |
3.93e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.02 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 306 QTLSSAR--RLNEviLSEPEVQFAEEKLDINKP-------LDITFSNVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTG 376
Cdd:TIGR03719 283 QAKSKARlaRYEE--LLSQEFQKRNETAEIYIPpgprlgdKVIEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNG 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 377 SGKSTLIQLLTRYWDPKKGYISIAgiELTQwnesqlresISVVSQRvdilngtlRDNLliarpeatdDHLANILKDV--G 454
Cdd:TIGR03719 359 AGKSTLFRMITGQEQPDSGTIEIG--ETVK---------LAYVDQS--------RDAL---------DPNKTVWEEIsgG 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 455 LEKLLENN------ALDSWLGDGGR-------QLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQT----EHSIMTlf 517
Cdd:TIGR03719 411 LDIIKLGKreipsrAYVGRFNFKGSdqqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETlralEEALLN-- 488
|
250
....*....|....
gi 2020526634 518 ekhFEGKTVIfITH 531
Cdd:TIGR03719 489 ---FAGCAVV-ISH 498
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
474-559 |
6.90e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 474 QLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLF--EKHFEGKTVIFITHRL-IGLESMDSIVLIEQGEI 550
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLleLQQKENMALVLITHDLaLVAEAAHKIIVMYAGQV 232
|
....*....
gi 2020526634 551 VENGSHEKL 559
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
334-568 |
8.76e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 334 NKPLDiTFSNVTFNYPDSERN-VLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGieltqwNESQL 412
Cdd:PRK13545 18 NKPFD-KLKDLFFRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 413 RESISVVSQRVDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLLeNNALDSWlgdggrqlSGGEKRRIGIARAILHD 492
Cdd:PRK13545 91 AISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFI-YQPVKTY--------SSGMKSRLGFAISVHIN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 493 APILLLDEPTEGLDKQ-TEHSIMTLFEKHFEGKTVIFITHRLIGLESMDSIVL-IEQGEIVENGSHEKLLNEAGRYFQ 568
Cdd:PRK13545 162 PDILVIDEALSVGDQTfTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVDHYDEFLK 239
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
343-568 |
1.01e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYPDS--ERNVLNAVD-LTIPATnKVAIVGQTGSGKSTLIQLLTRYWDpkKGYISiAGIELTQWNE--SQLRESIS 417
Cdd:TIGR00956 764 NLTYEVKIKkeKRVILNNVDgWVKPGT-LTALMGASGAGKTTLLNVLAERVT--TGVIT-GGDRLVNGRPldSSFQRSIG 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVSQR-VDILNGTLRDNLLIA----RP-----EATDDHLANILKDVGLEKLLennalDSWLGDGGRQLSGGEKRRIGIAR 487
Cdd:TIGR00956 840 YVQQQdLHLPTSTVRESLRFSaylrQPksvskSEKMEYVEEVIKLLEMESYA-----DAVVGVPGEGLNVEQRKRLTIGV 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 488 AILHDAPILL-LDEPTEGLDKQTEHSIMTLFEKHFE-GKTVIFITHR--LIGLESMDSIVLIEQ-------GEIVENgSH 556
Cdd:TIGR00956 915 ELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQpsAILFEEFDRLLLLQKggqtvyfGDLGEN-SH 993
|
250
....*....|..
gi 2020526634 557 eKLLNeagrYFQ 568
Cdd:TIGR00956 994 -TIIN----YFE 1000
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
358-509 |
1.39e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 49.40 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 358 AVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPK---KGYISIAGIELTqwnesqlreSISVVSQRVDIL-------- 426
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT---------ALPAEQRRIGILfqddllfp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 427 NGTLRDNLLIARPEAT-----DDHLANILKDVGLEKLlennaldswlgdGGR---QLSGGEKRRIGIARAILHDAPILLL 498
Cdd:COG4136 90 HLSVGENLAFALPPTIgraqrRARVEQALEEAGLAGF------------ADRdpaTLSGGQRARVALLRALLAEPRALLL 157
|
170
....*....|.
gi 2020526634 499 DEPTEGLDKQT 509
Cdd:COG4136 158 DEPFSKLDAAL 168
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
341-533 |
2.03e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 341 FSNVTFNYPDSErnVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWN-ESQLRESISVV 419
Cdd:PRK11288 7 FDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 420 SQRVDIL-NGTLRDNLLIAR-PEA---TDDHLANilKDVG--LEKLLENNALDSWLGDggrqLSGGEKRRIGIARAILHD 492
Cdd:PRK11288 85 YQELHLVpEMTVAENLYLGQlPHKggiVNRRLLN--YEAReqLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKALARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2020526634 493 APILLLDEPTEGLD-KQTEHsimtLF----EKHFEGKTVIFITHRL 533
Cdd:PRK11288 159 ARVIAFDEPTSSLSaREIEQ----LFrvirELRAEGRVILYVSHRM 200
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
348-506 |
2.12e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 348 YPDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQ----------LRESIS 417
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRfmaylghlpgLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 418 VVsQRVDILNGtlrdnLLIARPEATDDHLANILKDVGLEKLLEnnaldswlgdggRQLSGGEKRRIGIARAILHDAPILL 497
Cdd:PRK13543 99 TL-ENLHFLCG-----LHGRRAKQMPGSALAIVGLAGYEDTLV------------RQLSAGQKKRLALARLWLSPAPLWL 160
|
....*....
gi 2020526634 498 LDEPTEGLD 506
Cdd:PRK13543 161 LDEPYANLD 169
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
339-550 |
2.14e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.84 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpDSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQlltrywdpkkgyiSIAGIELTQWNEsqlresISV 418
Cdd:PRK11650 4 LKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR-------------MVAGLERITSGE------IWI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 VSQRVDILNGTLRDnllIAR--------PEAT-DDHLANILKDVGLEK------------LLEnnaLDSWLGDGGRQLSG 477
Cdd:PRK11650 64 GGRVVNELEPADRD---IAMvfqnyalyPHMSvRENMAYGLKIRGMPKaeieervaeaarILE---LEPLLDRKPRELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 478 GEKRRIGIARAILHDAPILLLDEPTEGLDK----QTEHSIMTLfekHFE-GKTVIFITHRliGLESM---DSIVLIEQGE 549
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvQMRLEIQRL---HRRlKTTSLYVTHD--QVEAMtlaDRVVVMNGGV 212
|
.
gi 2020526634 550 I 550
Cdd:PRK11650 213 A 213
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
354-533 |
2.81e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.15 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 354 NVLNAVDLTIPATNKVAIVGQTGSGKSTLI---------QLLTRYWDPKKGYISIAGIE----LTQWNES---------- 410
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQPGNHDRIEGLEhidkVIVIDQSpigrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 411 --------QLRE-----------------------SISvvsqrvDILNGTLRDNLLIARPEATDDHLANILKDVGLEKLL 459
Cdd:cd03271 89 atytgvfdEIRElfcevckgkrynretlevrykgkSIA------DVLDMTVEEALEFFENIPKIARKLQTLCDVGLGYIK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2020526634 460 ennaldswLGDGGRQLSGGEKRRIGIARAILHDAP---ILLLDEPTEGLDKQTEHSIMTLFEKHFE-GKTVIFITHRL 533
Cdd:cd03271 163 --------LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNL 232
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
343-509 |
4.90e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 343 NVTFNYPDseRNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIaGIELTQWNESQLRESISvvsqr 422
Cdd:PRK11147 324 NVNYQIDG--KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAELD----- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 423 vdiLNGTLRDNLLIARPEAT----DDHLANILKD-----------VglekllennaldswlgdggRQLSGGEKRRIGIAR 487
Cdd:PRK11147 396 ---PEKTVMDNLAEGKQEVMvngrPRHVLGYLQDflfhpkramtpV-------------------KALSGGERNRLLLAR 453
|
170 180
....*....|....*....|..
gi 2020526634 488 AILHDAPILLLDEPTEGLDKQT 509
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVET 475
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
22-314 |
5.81e-06 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 48.32 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 22 MLLAFATLSASIGLLTLSGWFISAsAVAGLTIARETFNYMLPGGGVRGLAMSRTAGRWGERVVSHNATFKLLTDLRIFFF 101
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKL-LIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 102 KKLAPLIPGRISNLRDADLLNRLVADVDAMDHVYLRLVSPVTVGVFGIFFLTLFLMWFDsslglilGSILLIMLLVWPIL 181
Cdd:cd07346 80 RHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLN-------WKLTLVALLLLPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 182 F---YKLGKRnggeltqnkadLRVTTLDWIEGYSELT--------------LFGAEERYRNAILETQRKLMANQFVNANL 244
Cdd:cd07346 153 VlilRYFRRR-----------IRKASREVRESLAELSaflqeslsgirvvkAFAAEEREIERFREANRDLRDANLRAARL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 245 TGMASAALMLFNGLTLVLMLWLAADGVGGNAPDP--FIALMAFATMASFEL--LMPIAGAFQhlgQTLSSARRL 314
Cdd:cd07346 222 SALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIgeLVAFLAYLGMLFGPIqrLANLYNQLQ---QALASLERI 292
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
449-573 |
6.32e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 449 ILKDVGLEKLLENNALDSwlgdggrqLSGGEKRRIGIARailHDAPIL-----LLDEPTEGLDKQTEHSIMTLFEK-HFE 522
Cdd:PRK00635 459 ILIDLGLPYLTPERALAT--------LSGGEQERTALAK---HLGAELigityILDEPSIGLHPQDTHKLINVIKKlRDQ 527
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 523 GKTVIFITH--RLIGLesMDSIVLIEQ------GEIVENGSHEKLLNEA----GRYFQLRQAI 573
Cdd:PRK00635 528 GNTVLLVEHdeQMISL--ADRIIDIGPgagifgGEVLFNGSPREFLAKSdsltAKYLRQELTI 588
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
353-563 |
6.89e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQL----LTRYWDPK----KGYISIAGIELTQWNESQLRESISVVSQRVD 424
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 425 -ILNGTLRDNLLIARPEATDDHLANILKDVGL-EKLLENNALDSWLGDGGRQLSGGEKRRIGIARAIL-----HDAPI-- 495
Cdd:PRK13547 94 pAFAFSAREIVLLGRYPHARRAGALTHRDGEIaWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwppHDAAQpp 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020526634 496 --LLLDEPTEGLDKQTEHSIM----TLFEKHFEGktVIFITHRL-IGLESMDSIVLIEQGEIVENGSHEKLLNEA 563
Cdd:PRK13547 174 ryLLLDEPTAALDLAHQHRLLdtvrRLARDWNLG--VLAIVHDPnLAARHADRIAMLADGAIVAHGAPADVLTPA 246
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
449-573 |
8.01e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.86 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 449 ILKDVGLEKLLENNALDSwlgdggrqLSGGEKRRIGIARAI-------LHdapilLLDEPTEGL-DKQTEHSIMTLFEKH 520
Cdd:TIGR00630 471 FLIDVGLDYLSLSRAAGT--------LSGGEAQRIRLATQIgsgltgvLY-----VLDEPSIGLhQRDNRRLINTLKRLR 537
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 521 FEGKTVIFITHRLIGLESMDSIVLI------EQGEIVENGSHEKLLNE----AGRYFQLRQAI 573
Cdd:TIGR00630 538 DLGNTLIVVEHDEDTIRAADYVIDIgpgageHGGEVVASGTPEEILANpdslTGQYLSGRKKI 600
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
475-554 |
8.03e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.41 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 475 LSGGEKRRIGIARAILHDAPILLLDEPTEGLD-KQTEHS---IMTLFEKHfeGKTVIFITHRLIGLESMDSIVLIEQGEI 550
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDiEQRLNAaraIRRLSEEG--KKTALVVEHDLAVLDYLSDRIHVFEGEP 149
|
....
gi 2020526634 551 VENG 554
Cdd:cd03222 150 GVYG 153
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
351-563 |
8.15e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 351 SERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRvdilNGTl 430
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQR----NNT- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 rdNLLIARPEATDDHLANIL----KDVGL-EKLLENNALDSWLGDGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGL 505
Cdd:PRK10938 89 --DMLSPGEDDTGRTTAEIIqdevKDPARcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 506 DKQTEHSIMTLFEK-HFEGKTVIFITHRLIGL-ESMDSIVLIEQGEIVENGSHEKLLNEA 563
Cdd:PRK10938 167 DVASRQQLAELLASlHQSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQA 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
369-554 |
1.30e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 369 VAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQL---RESISVVSQR------------VDILNGTLRDN 433
Cdd:PRK10261 353 LSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQDpyasldprqtvgDSIMEPLRVHG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 434 LLiaRPEATDDHLANILKDVGLeklLENNALDSwlgdgGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSI 513
Cdd:PRK10261 433 LL--PGKAAAARVAWLLERVGL---LPEHAWRY-----PHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2020526634 514 MTL---FEKHFeGKTVIFITHRLIGLESMD-SIVLIEQGEIVENG 554
Cdd:PRK10261 503 INLlldLQRDF-GIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
353-552 |
1.90e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLtrywdpkKGYISIAGIELTQWNESQL----RESISVVSQRVD-ILN 427
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNWQLawvnQETPALPQPALEyVID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 428 G-----TLRDNLLIARpEATDDHLANILKDvgleKLlenNALDSW------------LGDGGRQL-------SGGEKRRI 483
Cdd:PRK10636 87 GdreyrQLEAQLHDAN-ERNDGHAIATIHG----KL---DAIDAWtirsraasllhgLGFSNEQLerpvsdfSGGWRMRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2020526634 484 GIARAILHDAPILLLDEPTEGLDKQtehSIMTL--FEKHFEGkTVIFITHRLIGLESM-DSIVLIEQGEIVE 552
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDLD---AVIWLekWLKSYQG-TLILISHDRDFLDPIvDKIIHIEQQSLFE 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
473-557 |
1.59e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 473 RQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTL-FEKHFEGKTVIFITHRL---IGLEsmDSIVLIEQG 548
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNViYELAAQGVAVLFVSSDLpevLGVA--DRIVVMREG 472
|
....*....
gi 2020526634 549 EIVENGSHE 557
Cdd:PRK11288 473 RIAGELARE 481
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
473-530 |
1.82e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.24 E-value: 1.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 473 RQLSGGEKRRIGIARAILHDAPILLLDEPTEGLD---KQTEHSIMTLFEKhfEGKTVIFIT 530
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgaKAEIYRLIRELAA--EGKAVIVIS 451
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
449-559 |
1.84e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 449 ILKDVGLEKLLennaldswLGDGGRQLSGGEKRRIGIARAILHDA---PILLLDEPTEGLD----KQTEHSIMTLFEKhf 521
Cdd:TIGR00630 812 TLCDVGLGYIR--------LGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHfddiKKLLEVLQRLVDK-- 881
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2020526634 522 eGKTVIFITHRLIGLESMDSIVLI------EQGEIVENGSHEKL 559
Cdd:TIGR00630 882 -GNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
475-572 |
1.88e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 475 LSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTL---FEKhfEGKTVIFITHRLIGLESM-DSIVLIEQGEI 550
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLinqFKA--EGLSIILVSSEMPEVLGMsDRILVMHEGRI 473
|
90 100
....*....|....*....|....*...
gi 2020526634 551 -----VENGSHEKLLNEA-GRYFQLRQA 572
Cdd:PRK10762 474 sgeftREQATQEKLMAAAvGKLNRVNQE 501
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
371-560 |
2.07e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.45 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 371 IVGQTGSGKSTLIQLLTRYWDPK---KGYISIAGIELtqwNESQLRESISVVSQRvDILNGTL----------------- 430
Cdd:PLN03140 196 LLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRL---NEFVPRKTSAYISQN-DVHVGVMtvketldfsarcqgvgt 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 431 RDNLL--IAR--------PEATDDHL----------ANILKDVGLEKLLENNALDSWLGDGG-RQLSGGEKRRIGIARAI 489
Cdd:PLN03140 272 RYDLLseLARrekdagifPEAEVDLFmkatamegvkSSLITDYTLKILGLDICKDTIVGDEMiRGISGGQKKRVTTGEMI 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 490 LHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVifithrLIGL--------ESMDSIVLIEQGEIVENGSHEKL 559
Cdd:PLN03140 352 VGPTKTLFMDEISTGLDSSTTYQIVKCLQQivHLTEATV------LMSLlqpapetfDLFDDIILLSEGQIVYQGPRDHI 425
|
.
gi 2020526634 560 L 560
Cdd:PLN03140 426 L 426
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
350-568 |
3.31e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 350 DSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLLT----RYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDI 425
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 426 LNGTLRDNLLIA--------RPEATD-DHLANILKDVGLEKLLENNALDSWLG-DGGRQLSGGEKRRIGIARAILHDAPI 495
Cdd:TIGR00956 151 PHLTVGETLDFAarcktpqnRPDGVSrEEYAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 496 LLLDEPTEGLDKQTEHSimtlFEKHFEGKTVIFITHRLIGL--------ESMDSIVLIEQGEIVENGSHEKllneAGRYF 567
Cdd:TIGR00956 231 QCWDNATRGLDSATALE----FIRALKTSANILDTTPLVAIyqcsqdayELFDKVIVLYEGYQIYFGPADK----AKQYF 302
|
.
gi 2020526634 568 Q 568
Cdd:TIGR00956 303 E 303
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
446-566 |
3.33e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 446 LANILKDVGLEKLLENNALDS---WLGDGGR-----------QLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEH 511
Cdd:PRK10982 349 ISNIRNYKNKVGLLDNSRMKSdtqWVIDSMRvktpghrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKF 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 512 SIMTLF-EKHFEGKTVIFITH---RLIGLesMDSIVLIEQGE---IVE--NGSHEKLLNEAGRY 566
Cdd:PRK10982 429 EIYQLIaELAKKDKGIIIISSempELLGI--TDRILVMSNGLvagIVDtkTTTQNEILRLASLH 490
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
474-550 |
3.34e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 474 QLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTL-FEKHFEGKTVIFITHRL---IGLEsmDSIVLIEQGE 549
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLiNQLVQQGVAIIVISSELpevLGLS--DRVLVMHEGK 482
|
.
gi 2020526634 550 I 550
Cdd:PRK13549 483 L 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
475-562 |
3.83e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 43.27 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 475 LSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTL-FEKHFEGKTVIFITHRL---IGLEsmDSIVLIEQGEI 550
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLiNQLAQEGVAIIVVSSELaevLGLS--DRVLVIGEGKL 481
|
90
....*....|..
gi 2020526634 551 VENGSHEKLLNE 562
Cdd:TIGR02633 482 KGDFVNHALTQE 493
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
474-552 |
4.81e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.85 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 474 QLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRLIGLESM-DSIVLIEQGEIV 551
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
|
.
gi 2020526634 552 E 552
Cdd:PRK09700 489 Q 489
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
473-531 |
7.27e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 7.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2020526634 473 RQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKqteHSIMTLfEKHFEG--KTVIFITH 531
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWL-ETYLLKwpKTFIVVSH 399
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
473-550 |
7.71e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 473 RQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEKHFE-GKTVIFITHRLIGLESM-DSIVLIEQGEI 550
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqNVAVLFISSDLEEIEQMaDRVLVMHQGEI 481
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
376-531 |
8.85e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 376 GSGKSTLIQLLTRYWDPKKGYISIAGIELTQWNESQLRESISVVSQRVDILNGtlrdNLLIARPEATDDHLANILKDVGL 455
Cdd:pfam13304 148 ISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLS----DLGEGIEKSLLVDDRLRERGLIL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 456 EKLLENNALDSWlgdggrQLSGGEKRRIGIARAILHDAP---ILLLDEPTEGLDKQTEHSIMTLFE-KHFEGKTVIFITH 531
Cdd:pfam13304 224 LENGGGGELPAF------ELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKeLSRNGAQLILTTH 297
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
339-506 |
1.27e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.65 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 339 ITFSNVTFNYpdSERNVLNAVDLTIPATNKVAIVGQTGSGKSTLIQLltrywdpkkgyisIAGIELTQwnesqlresisv 418
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSL-------------IAGARKIQ------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 419 vSQRVDILNGTLRD--------------------NL-----------LIAR-----PEATDDHLANILKDVGLEKLLENN 462
Cdd:NF033858 55 -QGRVEVLGGDMADarhrravcpriaympqglgkNLyptlsvfenldFFGRlfgqdAAERRRRIDELLRATGLAPFADRP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2020526634 463 AldswlgdggRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLD 506
Cdd:NF033858 134 A---------GKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
370-548 |
2.58e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 370 AIVGQTGSGKSTLIQLLTrywdPKK--GYIS----IAGIELTQwnESQLResISVVSQRVDILNG--TLRDNLLIAR--- 438
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLA----GRKtgGYIEgdirISGFPKKQ--ETFAR--ISGYCEQNDIHSPqvTVRESLIYSAflr 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 439 -PEATDDHLANILKDVGLEKLLENNALDSWLG-DGGRQLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTL 516
Cdd:PLN03140 982 lPKEVSKEEKMMFVDEVMELVELDNLKDAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1061
|
170 180 190
....*....|....*....|....*....|....*
gi 2020526634 517 FEKHFE-GKTVIFITHR--LIGLESMDSIVLIEQG 548
Cdd:PLN03140 1062 VRNTVDtGRTVVCTIHQpsIDIFEAFDELLLMKRG 1096
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
368-420 |
3.12e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 38.93 E-value: 3.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 368 KVAIVGQTGSGKSTLIQLLTRYWDPKKGYISIAGIElTQWNESQLRESISVVS 420
Cdd:PRK07261 2 KIAIIGYSGSGKSTLARKLSQHYNCPVLHLDTLHFQ-PNWQERDDDDMIADIS 53
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
474-561 |
3.13e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 474 QLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK--HFEGKTVIFITHRLIGLESM-DSIVLIEQGEI 550
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISHDLQMLSQWaDKINVLYCGQT 237
|
90
....*....|.
gi 2020526634 551 VENGSHEKLLN 561
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
440-552 |
3.56e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 440 EATDDHLANILKDVGLEkllEN-NALDSWLGDGGRQLsggekrrIGIARAILHDAPILLLDEPTEGL-DKQTEHSIMTLF 517
Cdd:NF040905 114 NETNRRARELLAKVGLD---ESpDTLVTDIGVGKQQL-------VEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLL 183
|
90 100 110
....*....|....*....|....*....|....*.
gi 2020526634 518 EKHFEGKTVIFITHRLIGLESM-DSIVLIEQGEIVE 552
Cdd:NF040905 184 ELKAQGITSIIISHKLNEIRRVaDSITVLRDGRTIE 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
475-560 |
3.59e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 475 LSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQTEHSIMTLFEK-HFEGKTVIFITHRLIGLESM-DSIVLIEQGEIV- 551
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVISSELPELLGMcDRIYVMNEGRITg 484
|
90
....*....|...
gi 2020526634 552 ----ENGSHEKLL 560
Cdd:NF040905 485 elprEEASQERIM 497
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
353-403 |
5.79e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 5.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020526634 353 RNVLNAVDLTIPATNKVAIVGQTGSGKSTLI---------QLLTRYWDPKKGYISIAGIE 403
Cdd:PRK00349 622 ENNLKNVDVEIPLGKFTCVTGVSGSGKSTLInetlykalaRKLNGAKKVPGKHKEIEGLE 681
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
475-533 |
5.99e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 5.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2020526634 475 LSGGEKRRIGIARAILHDAP---ILLLDEPTEGLDKQTEHS-IMTLFEKHFEGKTVIFITHRL 533
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKAlIYVLQSLTHQGHTVVIIEHNM 872
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
474-542 |
7.18e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.27 E-value: 7.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020526634 474 QLSGGEKRRIGIAR--AILH--DAPILLLDEPTEGLDKQTEHSIMTLFeKHFEGKT-VIFITHRLIGLESMDSI 542
Cdd:TIGR02168 1089 LLSGGEKALTALALlfAIFKvkPAPFCILDEVDAPLDDANVERFANLL-KEFSKNTqFIVITHNKGTMEVADQL 1161
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
474-509 |
7.81e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 7.81e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2020526634 474 QLSGGEKRRIGIARAILHDAPILLLDEPTEGLDKQT 509
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| |
