|
Name |
Accession |
Description |
Interval |
E-value |
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-579 |
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: 678.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 13 KNDQWVRPFLKRYKKTLYFALLLGFLTFFSAGALMFTSGYLISRAASLPEnILLIYIPIVLTRAFGIGRPVFRYVERLTS 92
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPP-ILNLFVPIVGVRAFAIGRTVFRYLERLVS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 93 HNWVLKMTSDLRLKLYNVLEKDAIFFKTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFAL 172
Cdd:COG4987 80 HDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 173 CMLLMLGVVVFLLPLVSVLVNGARQEKHKYAKNELYQTLTDNILGVSDWVFSQRGSEFVARYETDEANVRALDEKMKQFN 252
Cdd:COG4987 160 VLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 253 RGRDFVLQLLFGVIAIAVLAWtSVRFPGNHGGAANWIGAFVLTVFPLIDAFAPLPAAAQETTIYKDSIRRFNELPEGEDD 332
Cdd:COG4987 240 ALAQALLQLAAGLAVVAVLWL-AAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 333 STE---APVQPNGTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIP 409
Cdd:COG4987 319 VTEpaePAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 410 TEAF-GETMTEYIGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERH 488
Cdd:COG4987 399 LRDLdEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 489 RLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
570
....*....|.
gi 256953159 569 TNAHYQKLYRI 579
Cdd:COG4987 559 QNGRYRQLYQR 569
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-540 |
5.95e-161 |
|
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: 470.30 E-value: 5.95e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 17 WVRPFLKRYKKTLYFALLLGFLTFFSAGALMFTSGYLISRAASLPEnILLIYIPIVLTRAFGIGRPVFRYVERLTSHNWV 96
Cdd:TIGR02868 3 RILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPP-VLYLSVAAVAVRAFGIGRAVFRYLERLVGHDAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 97 LKMTSDLRLKLYNVLEKDAIFFKTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFALCMLL 176
Cdd:TIGR02868 82 LRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 177 MLGVVVFLLPLVSVLVNGARQEKHKYAKNELYQTLTDNILGVSDWVFSQRGSEFVARYETDEANVRALDEKMKQFNRGRD 256
Cdd:TIGR02868 162 GLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 257 fVLQLLFGVIAIAVLAWTSVRFPGNHGGAANWIGAFVLTVFPLIDAFAPLPAAAQETTIYKDSIRRFNELPEGE------ 330
Cdd:TIGR02868 242 -ALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAgpvaeg 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 331 DDSTEAPVQPNGTSLSIEHLSFAYENQEkKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPT 410
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 411 EAFGET-MTEYIGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHR 489
Cdd:TIGR02868 400 SSLDQDeVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQR 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 256953159 490 LALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHL 540
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-578 |
2.06e-115 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 355.24 E-value: 2.06e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 8 TKDVWKNDQWVRPFLKRYKKTLYFALLLGFLTFFSAGALMFTSGYLISRAASLPENILLIYIPIVLTrAFGIGRPVFRYV 87
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLL-GLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 88 ERLTSHNWVLKMTSDLRLKLYN-VLEKDAIFFkTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFF 166
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEhLLRLPLSFF-DRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 167 SWWFALCMLLMLGVVVFLLPLVSVLVNgARQEKHKYAKNELYQTLTDNILGVSDwV--FSQRGSEFvARYetDEANVRAL 244
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLR-KLFRRVQEALAELNGRLQESLSGIRV-VkaFGREEREL-ERF--REANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 245 DEKMKQFNRGR--DFVLQLLFGVIAIAVLAWTSVRFpgnHGGAANwIGAFVLTVFPLIDAFAPLPAAAQETTIYKD---S 319
Cdd:COG1132 235 RANLRAARLSAlfFPLMELLGNLGLALVLLVGGLLV---LSGSLT-VGDLVAFILYLLRLFGPLRQLANVLNQLQRalaS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 320 IRRFNEL----PEGEDDSTEAPVQPNGTSLSIEHLSFAYENqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGD 395
Cdd:COG1132 311 AERIFELldepPEIPDPPGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 396 LRPTSGEILLGNIPTEAFgeTMTEY---IGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQ 472
Cdd:COG1132 390 YDPTSGRILIDGVDIRDL--TLESLrrqIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 473 TMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFI 552
Cdd:COG1132 468 TVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVL 547
|
570 580
....*....|....*....|....*.
gi 256953159 553 EDGQLEMSGTPEELLATNAHYQKLYR 578
Cdd:COG1132 548 DDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-578 |
8.22e-100 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 314.46 E-value: 8.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 19 RPFLKRYKK---TLYFALLLGFLTFFSAGALMFTSGYLISRAASLPENILLIY---IPIVLTRAFGIGRPVFRYVERLTS 92
Cdd:PRK11160 5 LPFLKLYKRhwfMLSLGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSFnymLPAAGVRGAAIGRTAGRYGERLVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 93 HNWVLKMTSDLRLKLYNVLEKDAIFFKTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFAL 172
Cdd:PRK11160 85 HDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 173 CMLLMLGVVVFLLPLVSVLVNGARQEKHKYAKNELYQTLTDNILGVSD-WVFsqrGSEFVARYETDEANVRALD--EKMK 249
Cdd:PRK11160 165 TLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAElTLF---GAEDRYRQQLEQTEQQWLAaqRRQA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 250 QFNRGRDFVLQLLFGVIAIAVLaWTSVRFPGNHGGAANWIGAFVLTVFPLIDAFAPLPAAAQE--TTIykDSIRRFNELP 327
Cdd:PRK11160 242 NLTGLSQALMILANGLTVVLML-WLAAGGVGGNAQPGALIALFVFAALAAFEALMPVAGAFQHlgQVI--ASARRINEIT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 328 EGEDD---STEAPVQPNGTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEIL 404
Cdd:PRK11160 319 EQKPEvtfPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 405 LGNIPTEAFGE-TMTEYIGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQlPEGLQTMVDEAGLRFS 483
Cdd:PRK11160 399 LNGQPIADYSEaALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 484 GGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTP 563
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTH 557
|
570
....*....|....*
gi 256953159 564 EELLATNAHYQKLYR 578
Cdd:PRK11160 558 QELLAQQGRYYQLKQ 572
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-570 |
1.36e-99 |
|
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: 313.62 E-value: 1.36e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 15 DQWVRPFLKRYKKTLYFALLLGFLTFFSAGALMFTSGYLISRAASLPENILLIYIPIVLTRAFGIGRPVFRYVERLTSHN 94
Cdd:COG4988 5 DKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 95 WVLKMTSDLRLKLYNVLEKDAIFFKTKYRTGDILGLLSEDINHIQNlYLRTIFPTVIAWILY-IFLVIALGFFSWWFALC 173
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDG-YFARYLPQLFLAALVpLLILVAVFPLDWLSGLI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 174 MLlmlgVVVFLLPLVSVLVN-GARQEKHKYAknELYQTLT----DNILGVSDWVFSQRgsefvARYETDEanVRALDEK- 247
Cdd:COG4988 164 LL----VTAPLIPLFMILVGkGAAKASRRQW--RALARLSghflDRLRGLTTLKLFGR-----AKAEAER--IAEASEDf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 248 ----MK----QFNRGrdFVLQLLF--GVIAIAVLAWTSVRfpgnHGGAANWIGAFVLTVFPliDAFAPLP-------AAA 310
Cdd:COG4988 231 rkrtMKvlrvAFLSS--AVLEFFAslSIALVAVYIGFRLL----GGSLTLFAALFVLLLAP--EFFLPLRdlgsfyhARA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 311 QETTIYkDSIRRFNELPEGE-DDSTEAPVQPNGTSLSIEHLSFAYEnQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLA 389
Cdd:COG4988 303 NGIAAA-EKIFALLDAPEPAaPAGTAPLPAAGPPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 390 SLIRGDLRPTSGEILLGNIPTEAF-GETMTEYIGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLP 468
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLdPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 469 EGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQ 548
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADR 540
|
570 580
....*....|....*....|..
gi 256953159 549 VIFIEDGQLEMSGTPEELLATN 570
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAKN 562
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-578 |
3.40e-92 |
|
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: 298.29 E-value: 3.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 16 QWVRPFLKRYKKTLYFALLLGFLTFFSAGALMFTSGYLISRAasLPENI--LLIYIPIVLTrAFGIGRPVFRY-----VE 88
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRV--LPNQDlsTLWVLAIGLL-LALLFEGLLRLlrsylLL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 89 RLTShnwvlKMTSDLRLKLYNVLEKDAIFFKTKYRTGDILGLLSeDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSW 168
Cdd:COG2274 222 RLGQ-----RIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 169 WFALCMLLMLGVVVFLLPLVS-VLVNGARQEKHKYAKNE--LYQTLTdnilGVSDWVFSQRGSEFVARYETDEANVRALD 245
Cdd:COG2274 296 PLALVVLLLIPLYVLLGLLFQpRLRRLSREESEASAKRQslLVETLR----GIETIKALGAESRFRRRWENLLAKYLNAR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 246 EKMKQFNRGRDFVLQLLFGVIAIAVLAWTSVRFPGNH-------------GGAANWIGAFVLTVFPLIDAFAplpaaaqe 312
Cdd:COG2274 372 FKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQltlgqliafnilsGRFLAPVAQLIGLLQRFQDAKI-------- 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 313 ttiykdSIRRFNEL----PEGEDDSTEAPVQPNGTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTL 388
Cdd:COG2274 444 ------ALERLDDIldlpPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTL 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 389 ASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQL 467
Cdd:COG2274 518 LKLLLGLYEPTSGRILIDGIDLRQIDpASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEAL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 468 PEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMD 547
Cdd:COG2274 598 PMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLAD 677
|
570 580 590
....*....|....*....|....*....|.
gi 256953159 548 QVIFIEDGQLEMSGTPEELLATNAHYQKLYR 578
Cdd:COG2274 678 RIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
345-561 |
4.10e-87 |
|
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: 268.03 E-value: 4.10e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGVM 424
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFRTTILNNIrigreeaseaevwavlekvglkemvnqlpeglqtmvdeaGLRFSGGERHRLALARILLQDTPIVL 504
Cdd:cd03247 81 NQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 505 LDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSG 561
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
25-550 |
4.38e-68 |
|
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: 229.87 E-value: 4.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 25 YKKTLYFALLLGFLTFFSAGALMFTSGYLISRAASLPENILLIYIPIVLTRAFGIGRPVFRYVERLTSHNWVLKMTSDLR 104
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 105 LKLYNVLEKDAIFFKTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFALCMLLmlgvVVFL 184
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLL----TAPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 185 LPLVSVLVN---GARQEKHKYAKNELYQTLTDNILGVSDWVFSQRGSEFVARYETDEANVRalDEKMK----QFNRGrdF 257
Cdd:TIGR02857 157 IPIFMILIGwaaQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYR--ERTMRvlriAFLSS--A 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 258 VLQLlFGVIAIAVLAwTSVRFPGNHGGAANWIGAFVLTVFPliDAFAPL-------------PAAAQETTIYKDSirrfN 324
Cdd:TIGR02857 233 VLEL-FATLSVALVA-VYIGFRLLAGDLDLATGLFVLLLAP--EFYLPLrqlgaqyharadgVAAAEALFAVLDA----A 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 325 ELPEGED-DSTEAPVqpngTSLSIEHLSFAYENqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEI 403
Cdd:TIGR02857 305 PRPLAGKaPVTAAPA----SSLEFSGVSVAYPG-RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 404 LLGNIPTEAFGE-TMTEYIGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRF 482
Cdd:TIGR02857 380 AVNGVPLADADAdSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGL 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 483 SGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVI 550
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIV 527
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
348-579 |
8.58e-65 |
|
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: 212.09 E-value: 8.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 348 EHLSFAYeNQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIrgdLR---PTSGEILLGNIP-TEAFGETMTEYIGV 423
Cdd:cd03253 4 ENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL---FRfydVSSGSILIDGQDiREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIV 503
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 504 LLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLATNAHYQKLYRI 579
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-579 |
5.43e-63 |
|
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: 217.28 E-value: 5.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 20 PFLKRYKKTLYFALLLGFLTFFSAGALMFTSGYLISRAASLPENILLIYIPIVLtrafgIGRPVFRYVERLTSH---NWV 96
Cdd:TIGR02203 7 SYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVV-----IGLAVLRGICSFVSTyllSWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 97 -LKMTSDLRLKLYN-VLEKDAIFFKtKYRTGDILGLLSEDINHIQNlYLRTIFPTVIAWIL-YIFLVIALGFFSWWFALC 173
Cdd:TIGR02203 82 sNKVVRDIRVRMFEkLLGLPVSFFD-RQPTGTLLSRITFDSEQVAS-AATDAFIVLVRETLtVIGLFIVLLYYSWQLTLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 174 MLLMLgvvvfllPLVSVLVNGARQ------EKHKYAKNELYQTLTDNILGVSDwVFSQRGSEFVA-RYETDEANVRALDE 246
Cdd:TIGR02203 160 VVVML-------PVLSILMRRVSKrlrrisKEIQNSMGQVTTVAEETLQGYRV-VKLFGGQAYETrRFDAVSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 247 KMKQFNRGRDFVLQLLfGVIAIAVLAWTSVrFPGNHGgaANWIGAFVLTVFPLIDAFAPLPAAA------QETTIYKDSI 320
Cdd:TIGR02203 232 KMTSAGSISSPITQLI-ASLALAVVLFIAL-FQAQAG--SLTAGDFTAFITAMIALIRPLKSLTnvnapmQRGLAAAESL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 321 RRFNELPEGEDDSTEAPVQPNGtSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTS 400
Cdd:TIGR02203 308 FTLLDSPPEKDTGTRAIERARG-DVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 401 GEILLGNIPTEAFG-ETMTEYIGVMHQAPYLFRTTILNNIRIGR-EEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEA 478
Cdd:TIGR02203 387 GQILLDGHDLADYTlASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGEN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 479 GLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLE 558
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
570 580
....*....|....*....|.
gi 256953159 559 MSGTPEELLATNAHYQKLYRI 579
Cdd:TIGR02203 547 ERGTHNELLARNGLYAQLHNM 567
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-579 |
1.40e-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: 214.30 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 1 MMEKQPTTKDVWKNDQWVRPFLKRYKKTLYFALLLGFLTFFSA-GALMFTSGYLISRAASLPENILLIYIPIVLTRAFGI 79
Cdd:COG5265 7 MSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAaLALVVPPLLKDAIDALLSGAAALLVVPVGLLLAYGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 80 GRpvfryverLTShnwvlKMTSDLRlklynvlekDAIFFKTKYRTGDILGLlsEDINHIQNLYLR--------------- 144
Cdd:COG5265 87 LR--------LLS-----VLFGELR---------DALFARVTQRAVRRLAL--EVFRHLHALSLRfhlerqtgglsrdie 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 145 ---------------TIFPTviawILYIFLVIA--LGFFSWWFALCMLLMLGVVVfllpLVSVLVNGARQeKHKYAKNEL 207
Cdd:COG5265 143 rgtkgiefllrfllfNILPT----LLEIALVAGilLVKYDWWFALITLVTVVLYI----AFTVVVTEWRT-KFRREMNEA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 208 Y----QTLTDNIL--------GVSDWVfSQRGSEFVARYEtdEANVRaldekmkqfNRGRDFVLQllFG---VIAIAVLA 272
Cdd:COG5265 214 DseanTRAVDSLLnyetvkyfGNEARE-ARRYDEALARYE--RAAVK---------SQTSLALLN--FGqalIIALGLTA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 273 --WTSVRfpGNHGGAANwIGAFVLTVFPLIDAFAPLPAAAqetTIYKDsIRR-----------FNELPEGEDDSTEAPVQ 339
Cdd:COG5265 280 mmLMAAQ--GVVAGTMT-VGDFVLVNAYLIQLYIPLNFLG---FVYRE-IRQaladmermfdlLDQPPEVADAPDAPPLV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 340 PNGTSLSIEHLSFAYEnQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIrgdLR---PTSGEILLGnipteafGET 416
Cdd:COG5265 353 VGGGEVRFENVSFGYD-PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL---FRfydVTSGRILID-------GQD 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 MTEY--------IGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERH 488
Cdd:COG5265 422 IRDVtqaslraaIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQ 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 489 RLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLA 581
|
650
....*....|.
gi 256953159 569 TNAHYQKLYRI 579
Cdd:COG5265 582 QGGLYAQMWAR 592
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
345-556 |
3.21e-61 |
|
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: 200.30 E-value: 3.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIGV 423
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDlESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYLFRTTILNNIrigreeaseaevwavlekvglkemvnqlpeglqtmvdeaglrFSGGERHRLALARILLQDTPIV 503
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 256953159 504 LLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQ 556
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
345-577 |
7.41e-60 |
|
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: 198.99 E-value: 7.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIGV 423
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIV 503
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 504 LLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLATNAHYQKLY 577
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
347-570 |
1.11e-58 |
|
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: 195.52 E-value: 1.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 347 IEHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGE-TMTEYIGVMH 425
Cdd:cd03254 5 FENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRkSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 426 QAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLL 505
Cdd:cd03254 84 QDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 506 DEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLATN 570
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
344-563 |
3.42e-57 |
|
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: 191.55 E-value: 3.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIG 422
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 VMHQAPYLFRTTILNNIRIgREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPI 502
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDP-FGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256953159 503 VLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTP 563
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
347-578 |
9.73e-57 |
|
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: 190.83 E-value: 9.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 347 IEHLSFAYENQ-EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIrgdLR---PTSGEILLGNIPTEAFG-ETMTEYI 421
Cdd:cd03249 3 FKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIRDLNlRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTP 501
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 502 IVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLATNAHYQKLYR 578
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
351-561 |
1.22e-55 |
|
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: 187.41 E-value: 1.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 351 SFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNI------PTEafgetMTEYIGVM 424
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdirqldPAD-----LRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVL 504
Cdd:cd03245 84 PQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 505 LDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSG 561
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
345-568 |
1.39e-53 |
|
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: 182.15 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPT-EAFGETMTEYIGV 423
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAP--YLFRTTI-------LNNIRIGREEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALAR 494
Cdd:COG1122 80 VFQNPddQLFAPTVeedvafgPENLGLPREEI-RERVEEALELVGLEHLADRPPHEL-----------SGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 495 ILLQDTPIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAeLADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
346-556 |
1.19e-50 |
|
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: 173.81 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 346 SIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIGVM 424
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAP--YLFRTTI-------LNNIRIGREEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARI 495
Cdd:cd03225 81 FQNPddQFFGPTVeeevafgLENLGLPEEEI-EERVEEALELVGLEGLRDRSPFTL-----------SGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 496 LLQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKD--KTVIWITHHLQGV-TLMDQVIFIEDGQ 556
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLE-LLKKLKAegKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-577 |
6.09e-48 |
|
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: 178.39 E-value: 6.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 20 PFLKRYKKtlyfallLGFLTFFSAGALMftsgyLISRAASL-PENILLIYIPIVLTRAFGI----------GRPVFRYVE 88
Cdd:TIGR01193 149 PLITRQKK-------LIVNIVIAAIIVT-----LISIAGSYyLQKIIDTYIPHKMMGTLGIisigliiayiIQQILSYIQ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 89 RLTSHNWVLKMTSDLRLKLYN-VLEKDAIFFKTKyRTGDILGLLSeDINHIqnlyLRTIFPTVIAWILYIFLVIALGFFs 167
Cdd:TIGR01193 217 IFLLNVLGQRLSIDIILSYIKhLFELPMSFFSTR-RTGEIVSRFT-DASSI----IDALASTILSLFLDMWILVIVGLF- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 168 wwfalcmLLMLGVVVFLLPLVSVLV------------NGARQEKHKyAKNELYQTLTDNI--------LGVSDWVFSQRG 227
Cdd:TIGR01193 290 -------LVRQNMLLFLLSLLSIPVyaviiilfkrtfNKLNHDAMQ-ANAVLNSSIIEDLngietiksLTSEAERYSKID 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 228 SEFVARYETDEANVRAldEKMKQfnrgrdfVLQLLFGVIAIAVLAWTSVRFPGNHGGAANWIGAF--VLTVF--PLIDAF 303
Cdd:TIGR01193 362 SEFGDYLNKSFKYQKA--DQGQQ-------AIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFnaLLSYFltPLENII 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 304 APLPAAAQETTIYKdsirRFNE--LPEGEDD---STEAPVQPNGtSLSIEHLSFAYeNQEKKVLNDLSLTIPEKQKLAIL 378
Cdd:TIGR01193 433 NLQPKLQAARVANN----RLNEvyLVDSEFInkkKRTELNNLNG-DIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIV 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 379 GRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGE-TMTEYIGVMHQAPYLFRTTILNNIRIG-REEASEAEVWAVLE 456
Cdd:TIGR01193 507 GMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRhTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 457 KVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKDKTVIWI 536
Cdd:TIGR01193 587 IAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFV 665
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 256953159 537 THHLQGVTLMDQVIFIEDGQLEMSGTPEELLATNAHYQKLY 577
Cdd:TIGR01193 666 AHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
321-568 |
4.42e-46 |
|
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: 170.70 E-value: 4.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 321 RRFNEL---PEGEDDSTEAPVqPNGtSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLR 397
Cdd:COG4618 306 RRLNELlaaVPAEPERMPLPR-PKG-RLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 398 PTSGEILLGNIPT-----EAFGEtmteYIGVMHQAPYLFRTTILNNI-RIGreEASEAEVWAVLEKVGLKEMVNQLPEGL 471
Cdd:COG4618 384 PTAGSVRLDGADLsqwdrEELGR----HIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGY 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 472 QTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETfFEALKD--KTVIWITHHLQGVTLMDQV 549
Cdd:COG4618 458 DTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAA-IRALKArgATVVVITHRPSLLAAVDKL 536
|
250
....*....|....*....
gi 256953159 550 IFIEDGQLEMSGTPEELLA 568
Cdd:COG4618 537 LVLRDGRVQAFGPRDEVLA 555
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
335-579 |
6.12e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 171.05 E-value: 6.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 335 EAPVQPNGT--------SLSIEHLSFAYENqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG 406
Cdd:PRK10790 323 DGPRQQYGNddrplqsgRIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 407 NIPTEAFG-ETMTEYIGVMHQAPYLFRTTILNNIRIGREeASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGG 485
Cdd:PRK10790 402 GRPLSSLShSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 486 ERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEE 565
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQ 560
|
250
....*....|....
gi 256953159 566 LLATNAHYQKLYRI 579
Cdd:PRK10790 561 LLAAQGRYWQMYQL 574
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
328-579 |
6.68e-46 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 170.58 E-value: 6.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 328 EGEDDSTEAPVQPNGTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGN 407
Cdd:PRK11176 325 EQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 408 IPTEAFG-ETMTEYIGVMHQAPYLFRTTILNNIRIGREEA-SEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGG 485
Cdd:PRK11176 405 HDLRDYTlASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 486 ERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEE 565
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
250
....*....|....
gi 256953159 566 LLATNAHYQKLYRI 579
Cdd:PRK11176 565 LLAQNGVYAQLHKM 578
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
345-577 |
9.94e-46 |
|
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: 161.50 E-value: 9.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILL-GNIPTEAFGETMTEYIGV 423
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIV 503
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 504 LLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLATNAHYQKLY 577
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
345-557 |
1.52e-44 |
|
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: 157.65 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKV--LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMT---- 418
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 -EYIGVMHQAPYLFRT-TILNNI----RIGREEASEAEVWA--VLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRL 490
Cdd:cd03255 81 rRHIGFVFQSFNLLPDlTALENVelplLLAGVPKKERRERAeeLLERVGLGDRLNHYPSEL-----------SGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 491 ALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFE--ALKDKTVIWITHHLQGVTLMDQVIFIEDGQL 557
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
318-578 |
2.09e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 166.56 E-value: 2.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 318 DSIRRFNELPEGEDDSTEAPVQPNGT-SLSIEHLSfAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDL 396
Cdd:PRK11174 322 ESLVTFLETPLAHPQQGEKELASNDPvTIEAEDLE-ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 397 rPTSGEILLGNIP-TEAFGETMTEYIGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMV 475
Cdd:PRK11174 401 -PYQGSLKINGIElRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPI 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 476 DEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDG 555
Cdd:PRK11174 480 GDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
250 260
....*....|....*....|...
gi 256953159 556 QLEMSGTPEELLATNAHYQKLYR 578
Cdd:PRK11174 560 QIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
345-556 |
2.21e-44 |
|
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: 156.48 E-value: 2.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAY---ENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGniPTEAFGEtmteyi 421
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--GSIAYVS------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 gvmhQAPYLFRTTILNNIRIGREEaSEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTP 501
Cdd:cd03250 73 ----QEPWIQNGTIRENILFGKPF-DEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 502 IVLLDEPTTGLDPITEQQLLET-FFEALKD-KTVIWITHHLQGVTLMDQVIFIEDGQ 556
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFENcILGLLLNnKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
345-568 |
4.19e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.07 E-value: 4.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGVM 424
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFRT-TILNNIR-------IGREEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARIL 496
Cdd:COG1131 79 PQEPALYPDlTVRENLRffarlygLPRKEA-RERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 497 LQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKD--KTVIWITHHLQGVTLM-DQVIFIEDGQLEMSGTPEELLA 568
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWE-LLRELAAegKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKA 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
345-568 |
1.46e-42 |
|
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: 153.74 E-value: 1.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIpteafgETMTE----- 419
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL------DTLDEenlwe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 ---YIGVMHQAP--YLFRTTI-------LNNIRIGREEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGER 487
Cdd:TIGR04520 75 irkKVGMVFQNPdnQFVGATVeddvafgLENLGVPREEM-RKRVDEALKLVGMEDFRDREPHLL-----------SGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 488 HRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETfFEALKD---KTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPE 564
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLET-IRKLNKeegITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
....
gi 256953159 565 ELLA 568
Cdd:TIGR04520 222 EIFS 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
345-580 |
1.63e-42 |
|
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: 153.28 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIGV 423
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSrRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYL-FRTTILNNIRIGR----------EEASEAEVWAVLEKVGLKEMVNQLpeglqtmVDEaglrFSGGERHRLAL 492
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRyphlglfgrpSAEDREAVEEALERTGLEHLADRP-------VDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 493 ARILLQDTPIVLLDEPTTGLDPITEQQLLETFFE--ALKDKTVIWITHHL-QGVTLMDQVIFIEDGQLEMSGTPEELLaT 569
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL-T 227
|
250
....*....|.
gi 256953159 570 NAHYQKLYRID 580
Cdd:COG1120 228 PELLEEVYGVE 238
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
348-578 |
2.34e-42 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 160.90 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 348 EHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIGVMHQ 426
Cdd:PRK13657 338 DDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTrASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 427 APYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLD 506
Cdd:PRK13657 417 DAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256953159 507 EPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLATNAHYQKLYR 578
Cdd:PRK13657 497 EATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
345-568 |
6.05e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 151.16 E-value: 6.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGVM 424
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLF-RTTILNNIRI------GREEASEAEVWAVLEKVGLKEMVNQLPEGlqtmvdeaglrFSGGERHRLALARILL 497
Cdd:COG4555 80 PDERGLYdRLTVRENIRYfaelygLFDEELKKRIEELIELLGLEEFLDRRVGE-----------LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 498 QDTPIVLLDEPTTGLDPITEQQLLEtFFEALKD--KTVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLRE-ILRALKKegKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELRE 221
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
345-570 |
6.53e-42 |
|
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: 150.90 E-value: 6.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLgnipteaFGETMTEY---- 420
Cdd:COG1127 6 IEVRNLTKSFG--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV-------DGQDITGLseke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 -------IGVMHQAPYLFRT-TILNNI--------RIGREEASEAeVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSG 484
Cdd:COG1127 77 lyelrrrIGMLFQGGALFDSlTVFENVafplrehtDLSEAEIREL-VLEKLELVGLPGAADKMPSEL-----------SG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 485 GERHRLALARILLQDTPIVLLDEPTTGLDPIT----EQQLLEtffeaLKDK---TVIWITHHLQGV-TLMDQVIFIEDGQ 556
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDPITsaviDELIRE-----LRDElglTSVVVTHDLDSAfAIADRVAVLADGK 219
|
250
....*....|....
gi 256953159 557 LEMSGTPEELLATN 570
Cdd:COG1127 220 IIAEGTPEELLASD 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
345-572 |
7.30e-42 |
|
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: 158.14 E-value: 7.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYE---NQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIP-TEAFGETMTEY 420
Cdd:COG1123 261 LEVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDlTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 ---IGVMHQAPY--LF-RTTI-------LNNIRIGREEASEAEVWAVLEKVGL-KEMVNQLPeglqtmvdeagLRFSGGE 486
Cdd:COG1123 341 rrrVQMVFQDPYssLNpRMTVgdiiaepLRLHGLLSRAERRERVAELLERVGLpPDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 487 RHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKDK---TVIWITHHLQGVTLM-DQVIFIEDGQLEMSGT 562
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILN-LLRDLQRElglTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGP 488
|
250
....*....|
gi 256953159 563 PEELLATNAH 572
Cdd:COG1123 489 TEEVFANPQH 498
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
345-558 |
1.42e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.81 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYE--NQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGET-MT--- 418
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEReLArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 -EYIGVMHQAPYLF-RTTILNNI----RIGREEASEAEVWA--VLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRL 490
Cdd:COG1136 85 rRHIGFVFQFFNLLpELTALENValplLLAGVSRKERRERAreLLERVGLGDRLDHRPSQL-----------SGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 491 ALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHLQGVTLMDQVIFIEDGQLE 558
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
345-569 |
1.57e-41 |
|
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: 149.96 E-value: 1.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGET----MTEY 420
Cdd:cd03261 1 IELRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 IGVMHQAPYLFRT-TILNNI-------RIGREEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLAL 492
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafplrehTRLSEEEIREIVLEKLEAVGLRGAEDLYPAEL-----------SGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 493 ARILLQDTPIVLLDEPTTGLDPITE---QQLLETFFEALkDKTVIWITHHLQGVTLM-DQVIFIEDGQLEMSGTPEELLA 568
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASgviDDLIRSLKKEL-GLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
.
gi 256953159 569 T 569
Cdd:cd03261 227 S 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
345-557 |
6.83e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 147.27 E-value: 6.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFgeTMTEY---I 421
Cdd:COG4619 1 LELEGLSFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM--PPPEWrrqV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAPYLFRTTILNNI----RIGREEASEAEVWAVLEKVGLKEMVnqlpegLQTMVDeaglRFSGGERHRLALARILL 497
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDI------LDKPVE----RLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 498 QDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITH-HLQGVTLMDQVIFIEDGQL 557
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
345-579 |
1.11e-40 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 148.75 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYE---NQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG--NIPTEAfGETMTE 419
Cdd:TIGR04521 1 IKLKNVSYIYQpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDgrDITAKK-KKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 Y---IGVMHQAP--YLFRTTILNNIRIG-------REEASEAEVWAvLEKVGLKEmvnqlpeglqTMVDEAGLRFSGGER 487
Cdd:TIGR04521 80 LrkkVGLVFQFPehQLFEETVYKDIAFGpknlglsEEEAEERVKEA-LELVGLDE----------EYLERSPFELSGGQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 488 HRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETF--FEALKDKTVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPE 564
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFkrLHKEKGLTVILVTHSMEDVaEYADRVIVMHKGKIVLDGTPR 228
|
250
....*....|....*
gi 256953159 565 ELLatnAHYQKLYRI 579
Cdd:TIGR04521 229 EVF---SDVDELEKI 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
345-579 |
6.29e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 147.08 E-value: 6.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIP-TEAFGETMTEYIGV 423
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAP--YLFRTTI-------LNNIRIGREEASEAEVWAvLEKVGLKEMVNQLPEglqtmvdeaglRFSGGERHRLALAR 494
Cdd:PRK13635 86 VFQNPdnQFVGATVqddvafgLENIGVPREEMVERVDQA-LRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 495 ILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKDK---TVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLatnA 571
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQ-LKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF---K 229
|
....*...
gi 256953159 572 HYQKLYRI 579
Cdd:PRK13635 230 SGHMLQEI 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
348-557 |
1.74e-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: 144.15 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 348 EHLSFAYENQ-EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIGVMH 425
Cdd:cd03248 15 QNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEhKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 426 QAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLL 505
Cdd:cd03248 95 QEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 256953159 506 DEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQL 557
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
345-566 |
1.82e-39 |
|
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: 143.86 E-value: 1.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRG--DL---RPTSGEILLGNIPTEAFGETMTE 419
Cdd:cd03260 1 IELRDLNVYYG--DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLipgAPDEGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 Y---IGVMHQAPYLFRTTILNNIRIG-------REEASEAEVWAVLEKVGLKEMVNQlpeglqtmvDEAGLRFSGGERHR 489
Cdd:cd03260 79 LrrrVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKD---------RLHALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 490 LALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEEL 566
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
345-568 |
2.35e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 150.82 E-value: 2.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPT---SGEILLGNIPTEAFGET-MTEY 420
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAlRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 IGVMHQAPY--LFRTTI-------LNNIRIGREEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLA 491
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVgdqiaeaLENLGLSRAEA-RARVLELLEAVGLERRLDRYPHQL-----------SGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHLQGVTLM-DQVIFIEDGQLEMSGTPEELLA 568
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILA 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
345-572 |
6.35e-39 |
|
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: 143.02 E-value: 6.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYE--NQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIP-TEAFGETMTEYI 421
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAPYL-------FRTTILNNIRIGREEASEAEVWAVLEKVGL-KEMVNQLPEGLqtmvdeaglrfSGGERHRLALA 493
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQL-----------SGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 494 RILLQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKDK---TVIWITHHLQGVTLM-DQVIFIEDGQLEMSGTPEELLAT 569
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILN-LLKDLREErglTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADLLAG 229
|
...
gi 256953159 570 NAH 572
Cdd:COG1124 230 PKH 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
345-572 |
7.63e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.59 E-value: 7.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKvlndLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTeyigvm 424
Cdd:COG3840 2 LRLDDLTYRYGDFPLR----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-------GQDLT------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPY------LFRT-------TILNNIRIGRE------EASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGG 485
Cdd:COG3840 65 ALPPAerpvsmLFQEnnlfphlTVAQNIGLGLRpglkltAEQRAQVEQALERVGLAGLLDRLPGQL-----------SGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 486 ERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGV-TLMDQVIFIEDGQLEMSGT 562
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAaRIADRVLLVADGRIAADGP 213
|
250
....*....|
gi 256953159 563 PEELLATNAH 572
Cdd:COG3840 214 TAALLDGEPP 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
340-578 |
1.42e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 340 PNGTSLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETmte 419
Cdd:COG1121 2 MMMPAIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 yIG-V--MHQAPYLFRTTILNNIRIGR----------EEASEAEVWAVLEKVGLKEM----VNQLpeglqtmvdeaglrf 482
Cdd:COG1121 77 -IGyVpqRAEVDWDFPITVRDVVLMGRygrrglfrrpSRADREAVDEALERVGLEDLadrpIGEL--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 483 SGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETfFEALKD--KTVIWITHHLQGV-TLMDQVIFIEDGQLEm 559
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEL-LRELRRegKTILVVTHDLGAVrEYFDRVLLLNRGLVA- 218
|
250
....*....|....*....
gi 256953159 560 SGTPEELLaTNAHYQKLYR 578
Cdd:COG1121 219 HGPPEEVL-TPENLSRAYG 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
345-557 |
1.70e-38 |
|
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: 141.49 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQ--EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY-- 420
Cdd:cd03257 2 LEVKNLSVSFPTGggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 --IGVMHQAPY-----------LFRTTILNNIRIGREEASEAEVWAVLEKVGL-KEMVNQLPEglqtmvdeaglRFSGGE 486
Cdd:cd03257 82 keIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 487 RHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKDK---TVIWITHHLQGV-TLMDQVIFIEDGQL 557
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKK-LQEElglTLLFITHDLGVVaKIADRVAVMYAGKI 224
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
36-311 |
3.16e-38 |
|
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: 142.62 E-value: 3.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 36 GFLTFFSAGALMFTSGYLISRAASLPENILLI--YIPIVLTRAFGIGRPVFRYVERLTSHNWVLKMTSDLRLKLYNVLEK 113
Cdd:cd18585 1 GLLTLLASIGLLALSGWFISAAALAGLAAPTFnyFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 114 --DAIFfkTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFALCMLLMLGVVVFLLPLVSVL 191
Cdd:cd18585 81 laPARL--QKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 192 VNGARQEKHKYAKNELYQTLTDNILGVSDWVFSQRGSEFVARYETDEANVRALDEKMKQFNRGRDFVLQLLFGVIAIAVL 271
Cdd:cd18585 159 LGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 256953159 272 aWTSVRFPGNHGGAANWIGAFVLTVFPLIDAFAPLPAAAQ 311
Cdd:cd18585 239 -WLGAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAFQ 277
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
345-550 |
4.77e-38 |
|
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: 139.91 E-value: 4.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEN--QEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLgnipteaFGETMTEY-- 420
Cdd:cd03293 1 LEVRNVSKTYGGggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV-------DGEPVTGPgp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 -IGVMHQAPYLF--RtTILNNIRIG-------REEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRL 490
Cdd:cd03293 74 dRGYVFQQDALLpwL-TVLDNVALGlelqgvpKAEA-RERAEELLELVGLSGFENAYPHQL-----------SGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 491 ALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHL-QGVTLMDQVI 550
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWREtgKTVLLVTHDIdEAVFLADRVV 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
345-557 |
2.34e-37 |
|
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: 136.37 E-value: 2.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGVM 424
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFRT-TILNNirigreeaseaevwavlekvglkemvnqlpeglqtmvdeagLRFSGGERHRLALARILLQDTPIV 503
Cdd:cd03230 79 PEEPSLYENlTVREN-----------------------------------------LKLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 504 LLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITHHLQGV-TLMDQVIFIEDGQL 557
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
346-556 |
3.72e-37 |
|
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: 135.06 E-value: 3.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 346 SIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTeafgetmteyigvmh 425
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 426 qapylfrttilnnirigreeaSEAEVWAVLEKVGlkeMVNQLpeglqtmvdeaglrfSGGERHRLALARILLQDTPIVLL 505
Cdd:cd00267 64 ---------------------AKLPLEELRRRIG---YVPQL---------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 256953159 506 DEPTTGLDPITEQQLLETFFEALKD-KTVIWITHHLQGVT-LMDQVIFIEDGQ 556
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
346-561 |
8.31e-37 |
|
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: 134.87 E-value: 8.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 346 SIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGET-MTEYIGVM 424
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKeLARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQApylfrttilnnirigreeaseaevwavLEKVGLKEMVNQlpeGLQTMvdeaglrfSGGERHRLALARILLQDTPIVL 504
Cdd:cd03214 79 PQA---------------------------LELLGLAHLADR---PFNEL--------SGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256953159 505 LDEPTTGLDPITEQQLLETFFE--ALKDKTVIWITHHLqGVTLM--DQVIFIEDGQLEMSG 561
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDL-NLAARyaDRVILLKDGRIVAQG 180
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
327-576 |
1.05e-36 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 145.64 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 327 PEGEDDSTEAPVQPNGTsLSIEHLSFAYENQ-EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILL 405
Cdd:TIGR00958 462 PNIPLTGTLAPLNLEGL-IEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 406 GNIPTEAFG-ETMTEYIGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSG 484
Cdd:TIGR00958 541 DGVPLVQYDhHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSG 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 485 GERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETffEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPE 564
Cdd:TIGR00958 621 GQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
250
....*....|..
gi 256953159 565 ELLATNAHYQKL 576
Cdd:TIGR00958 699 QLMEDQGCYKHL 710
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
340-538 |
1.51e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.14 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 340 PNGTSLSIEHLSFAY--ENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETm 417
Cdd:COG1116 3 AAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 418 teyIGVMHQAPYLF--RTtILNNIRIG-------REEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERH 488
Cdd:COG1116 82 ---RGVVFQEPALLpwLT-VLDNVALGlelrgvpKAER-RERARELLELVGLAGFEDAYPHQL-----------SGGMRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 256953159 489 RLALARILLQDTPIVLLDEPTTGLDPITE---QQLLETFFEALKdKTVIWITH 538
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRerlQDELLRLWQETG-KTVLFVTH 197
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
335-578 |
2.87e-36 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 142.93 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 335 EAPVQPNGT--------SLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG 406
Cdd:PRK10789 296 EAPVVKDGSepvpegrgELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 407 NIPTEAFG-ETMTEYIGVMHQAPYLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGG 485
Cdd:PRK10789 376 DIPLTKLQlDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 486 ERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEE 565
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQ 535
|
250
....*....|...
gi 256953159 566 LLATNAHYQKLYR 578
Cdd:PRK10789 536 LAQQSGWYRDMYR 548
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
345-578 |
1.07e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.41 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNI-PTEAFGETMTEY--- 420
Cdd:COG3638 3 LELRNLSKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdVTALRGRALRRLrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 IGVMHQAPYLF-RTTILNNIRIGR----------------EEASEAEvwAVLEKVGLKEMVNQlpeglqtMVDEagLrfS 483
Cdd:COG3638 82 IGMIFQQFNLVpRLSVLTNVLAGRlgrtstwrsllglfppEDRERAL--EALERVGLADKAYQ-------RADQ--L--S 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 484 GGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQ-GVTLMDQVIFIEDGQLEMS 560
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDlARRYADRIIGLRDGRVVFD 228
|
250
....*....|....*...
gi 256953159 561 GTPEELlaTNAHYQKLYR 578
Cdd:COG3638 229 GPPAEL--TDAVLREIYG 244
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
362-510 |
4.40e-35 |
|
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: 129.30 E-value: 4.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTeaFGETMTEY---IGVMHQAPYLF-RTTILN 437
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL--TDDERKSLrkeIGYVFQDPQLFpRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 438 NIRIGRE------EASEAEVWAVLEKVGLKEMVNQLpeglqtmVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTT 510
Cdd:pfam00005 79 NLRLGLLlkglskREKDARAEEALEKLGLGDLADRP-------VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
346-580 |
9.26e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.42 E-value: 9.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 346 SIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLgnipteaFGETMT------- 418
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-------DGITISkenlkei 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 -EYIGVMHQAP--YLFRTTI-------LNNIRIGREEASEAeVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERH 488
Cdd:PRK13632 82 rKKIGIIFQNPdnQFIGATVeddiafgLENKKVPPKKMKDI-IDDLAKKVGMEDYLDKEPQNL-----------SGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 489 RLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFE--ALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
250
....*....|....
gi 256953159 567 LaTNAHYQKLYRID 580
Cdd:PRK13632 230 L-NNKEILEKAKID 242
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
345-557 |
9.38e-35 |
|
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: 129.26 E-value: 9.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGET-MTEYIGV 423
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNeLGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYLFRTTILNNIrigreeaseaevwavlekvglkemvnqlpeglqtmvdeaglrFSGGERHRLALARILLQDTPIV 503
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 504 LLDEPTTGLDPITEQQLLETfFEALK--DKTVIWITHHLQGVTLMDQVIFIEDGQL 557
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQA-IAALKaaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
346-557 |
9.74e-35 |
|
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: 130.07 E-value: 9.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 346 SIEHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIgVMh 425
Cdd:cd03226 1 RIENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGY-VM- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 426 QAP--YLFRTTILNNIRIGREEASE--AEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTP 501
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHPLSL-----------SGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 502 IVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITHHLQGVTLM-DQVIFIEDGQL 557
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
345-566 |
1.07e-34 |
|
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: 130.70 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGVM 424
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFRT-TILNNIRI------GREEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILL 497
Cdd:cd03263 81 PQFDALFDElTVREHLRFyarlkgLPKSEIKEEVELLLRVLGLTDKANKRARTL-----------SGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 498 QDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
345-561 |
4.60e-34 |
|
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: 128.79 E-value: 4.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEY---- 420
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-------GRDVTGVpper 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 --IGVMHQAPYLFRT-TILNNIRIG------REEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLA 491
Cdd:cd03259 72 rnIGMVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALK--DKTVIWITHHLQ-GVTLMDQVIFIEDGQLEMSG 561
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
345-577 |
7.34e-34 |
|
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: 128.84 E-value: 7.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGE----TMTEY 420
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 IGVMHQAPYLF-RTTILNNIRIGR-------------------EEASEAevwavLEKVGLKEMVNQlpeglqtMVDEagl 480
Cdd:cd03256 80 IGMIFQQFNLIeRLSVLENVLSGRlgrrstwrslfglfpkeekQRALAA-----LERVGLLDKAYQ-------RADQ--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 481 rFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQ-GVTLMDQVIFIEDGQL 557
Cdd:cd03256 145 -LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDlAREYADRIVGLKDGRI 223
|
250 260
....*....|....*....|
gi 256953159 558 EMSGTPEELlaTNAHYQKLY 577
Cdd:cd03256 224 VFDGPPAEL--TDEVLDEIY 241
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
345-571 |
9.45e-34 |
|
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: 128.57 E-value: 9.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGET-MTEYIGV 423
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVeLRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYLF-RTTILNNIRI------GREEASEAEVWAVLEKVGL--KEMVNQLPEGLqtmvdeaglrfSGGERHRLALAR 494
Cdd:cd03295 80 VIQQIGLFpHMTVEENIALvpkllkWPKEKIRERADELLALVGLdpAEFADRYPHEL-----------SGGQQQRVGVAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 495 ILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHLQ-GVTLMDQVIFIEDGQLEMSGTPEELLATNA 571
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
340-557 |
3.08e-33 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 127.87 E-value: 3.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 340 PNGTSLSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAfgetMTE 419
Cdd:PRK11247 8 NQGTPLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE----ARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 YIGVMHQ-APYLFRTTILNNIRIG-----REEASEAevwavLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALA 493
Cdd:PRK11247 82 DTRLMFQdARLLPWKKVIDNVGLGlkgqwRDAALQA-----LAAVGLADRANEWPAAL-----------SGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 494 RILLQDTPIVLLDEPTTGLDPITE---QQLLETFFEAlKDKTVIWITHHL-QGVTLMDQVIFIEDGQL 557
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRiemQDLIESLWQQ-HGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
343-567 |
8.84e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 126.28 E-value: 8.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYI 421
Cdd:PRK11231 1 MTLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQ------------------APYLfrttilnNI--RIGREEasEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglr 481
Cdd:PRK11231 79 ALLPQhhltpegitvrelvaygrSPWL-------SLwgRLSAED--NARVNQAMEQTRINHLADRRLTDL---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 482 fSGGERHRLALARILLQDTPIVLLDEPTTGLDpITEQQLLETFFEALKD--KTVIWITHHL-QGVTLMDQVIFIEDGQLE 558
Cdd:PRK11231 140 -SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD-INHQVELMRLMRELNTqgKTVVTVLHDLnQASRYCDHLVVLANGHVM 217
|
....*....
gi 256953159 559 MSGTPEELL 567
Cdd:PRK11231 218 AQGTPEEVM 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
346-544 |
1.05e-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: 124.95 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 346 SIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGEtmteYIGVMH 425
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK----RIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 426 Q---APYLFRTTILNNIRIGRE----------EASEAEVWAVLEKVGLKEMVNQLpeglqtmVDEAglrfSGGERHRLAL 492
Cdd:cd03235 75 QrrsIDRDFPISVRDVVLMGLYghkglfrrlsKADKAKVDEALERVGLSELADRQ-------IGEL----SGGQQQRVLL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 256953159 493 ARILLQDTPIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITHHLQGVT 544
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVL 196
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
345-554 |
1.84e-32 |
|
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: 123.74 E-value: 1.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIG-V 423
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAyL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYLFRTTILNNI----RIGREEASEAEVWAVLEKVGLkemvnqlpEGLQtmvDEAGLRFSGGERHRLALARILLQD 499
Cdd:COG4133 81 GHADGLKPELTVRENLrfwaALYGLRADREAIDEALEAVGL--------AGLA---DLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 500 TPIVLLDEPTTGLDPiTEQQLLETFFEALKDK--TVIWITHHLQGVTLmDQVIFIED 554
Cdd:COG4133 150 APLWLLDEPFTALDA-AGVALLAELIAAHLARggAVLLTTHQPLELAA-ARVLDLGD 204
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
364-561 |
2.84e-32 |
|
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: 123.76 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 364 DLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTeAFGETMTEYIGVMHQAPYLF-RTTILNNIRIG 442
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 443 R-------EEASEAeVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDEPTTGLDPI 515
Cdd:cd03298 95 LspglkltAEDRQA-IEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 256953159 516 TEQQLLETFFEALKDK--TVIWITHHLQGVT-LMDQVIFIEDGQLEMSG 561
Cdd:cd03298 163 LRAEMLDLVLDLHAETkmTVLMVTHQPEDAKrLAQRVVFLDNGRIAAQG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
345-557 |
3.51e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 123.62 E-value: 3.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY---- 420
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 IGVMHQ-APYLFRTTILNNIR-----IGREEAS-EAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALA 493
Cdd:COG2884 81 IGVVFQdFRLLPDRTVYENVAlplrvTGKSRKEiRRRVREVLDLVGLSDKAKALPHEL-----------SGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 494 RILLQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKD--KTVIWITHHLQgvtLMDQ----VIFIEDGQL 557
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIME-LLEEINRrgTTVLIATHDLE---LVDRmpkrVLELEDGRL 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
341-566 |
9.04e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 125.98 E-value: 9.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 341 NGTSLSIEHLSFAYENQekKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTE- 419
Cdd:COG3842 2 AMPALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD-------GRDVTGl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 -----YIGVMHQAPYLF-RTTILNNI-------RIGREEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGE 486
Cdd:COG3842 73 ppekrNVGMVFQDYALFpHLTVAENVafglrmrGVPKAEI-RARVAELLELVGLEGLADRYPHQL-----------SGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 487 RHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHlQG--VTLMDQVIFIEDGQLEMSGT 562
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElgITFIYVTHD-QEeaLALADRIAVMNDGRIEQVGT 219
|
....
gi 256953159 563 PEEL 566
Cdd:COG3842 220 PEEI 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-575 |
1.28e-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: 131.19 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 340 PNGTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLAS-LIRgdLRPTSGEILLGNIPTEAFG-ETM 417
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSaLLR--LLSTEGEIQIDGVSWNSVTlQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 418 TEYIGVMHQAPYLFRTTILNNIRiGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILL 497
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSIL 1369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 498 QDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLATNAHYQK 575
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
342-581 |
1.73e-31 |
|
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: 122.71 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 342 GTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEY 420
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPlHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 IGVMHQAPYLFRTTILNNIRIGREeASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDT 500
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 501 PIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLA-TNAHYQKLYRI 579
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGVFASLVRT 255
|
..
gi 256953159 580 DR 581
Cdd:cd03288 256 DK 257
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
345-556 |
6.41e-31 |
|
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: 118.83 E-value: 6.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY---I 421
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrrI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAPYLFRT-TILNNIrigreeaseaevwavlekvglkemvnqlpeglqtmvdeaGLRFSGGERHRLALARILLQDT 500
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI---------------------------------------ALGLSGGQQQRVALARALAMDP 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 501 PIVLLDEPTTGLDPITE---QQLLETFFEALKdKTVIWITHHL-QGVTLMDQVIFIEDGQ 556
Cdd:cd03229 120 DVLLLDEPTSALDPITRrevRALLKSLQAQLG-ITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
347-568 |
9.06e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 121.38 E-value: 9.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 347 IEHLSFAY-ENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILL-GNIPTEAFGETMTEYIGVM 424
Cdd:PRK13650 7 VKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENVWDIRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPylfrttilNNIRIGreEASEAEVWAVLEKVGL--KEMVNQLPE-----GLQTMVDEAGLRFSGGERHRLALARILL 497
Cdd:PRK13650 87 FQNP--------DNQFVG--ATVEDDVAFGLENKGIphEEMKERVNEalelvGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 498 QDTPIVLLDEPTTGLDPITEQQLLETfFEALKDK---TVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKT-IKGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
344-565 |
2.08e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.54 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENQ---EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY 420
Cdd:PRK13637 2 SIKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 ---IGVMHQAP--YLFRTTILNNIRIG------REEASEAEVWAVLEKVGLKemvnqlpegLQTMVDEAGLRFSGGERHR 489
Cdd:PRK13637 82 rkkVGLVFQYPeyQLFEETIEKDIAFGpinlglSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 490 LALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEE 565
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAkLADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
340-566 |
2.46e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 120.29 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 340 PNGTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGE----ILLGNIPTEAFGE 415
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskiTVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 416 TMTEYIGVMHQAP--YLFRTTI-------LNNIRIGREEASEAeVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGE 486
Cdd:PRK13640 81 DIREKVGIVFQNPdnQFVGATVgddvafgLENRAVPRPEMIKI-VRDVLADVGMLDYIDSEPANL-----------SGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 487 RHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPE 564
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPV 228
|
..
gi 256953159 565 EL 566
Cdd:PRK13640 229 EI 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
343-580 |
4.13e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.72 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAF-GETMTEYI 421
Cdd:PRK13548 1 AMLEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWsPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAPYL-FRTTILNNIRIGR------EEASEAEVWAVLEKVGLkemvnqlpEGLqtmvdeAGLRF---SGGERHRLA 491
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGRaphglsRAEDDALVAAALAQVDL--------AHL------AGRDYpqlSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 492 LARILLQ------DTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHL-QGVTLMDQVIFIEDGQLEMSGT 562
Cdd:PRK13548 145 LARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLnLAARYADRIVLLHQGRLVADGT 224
|
250
....*....|....*...
gi 256953159 563 PEELLaTNAHYQKLYRID 580
Cdd:PRK13548 225 PAEVL-TPETLRRVYGAD 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
347-568 |
5.05e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 119.74 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 347 IEHLSFAYENQ---EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-----ETMT 418
Cdd:PRK13634 5 FQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkklKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 EYIGVMHQAP--YLFRTTILNNIRIG------REEASEAEVWAVLEKVGLKEMVnqlpeglqtmVDEAGLRFSGGERHRL 490
Cdd:PRK13634 85 KKVGIVFQFPehQLFEETVEKDICFGpmnfgvSEEDAKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 491 ALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELL 567
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAArYADQIVVMHKGTVFLQGTPREIF 234
|
.
gi 256953159 568 A 568
Cdd:PRK13634 235 A 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
337-566 |
8.37e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 125.66 E-value: 8.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 337 PVQPNgtSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-E 415
Cdd:PTZ00243 1303 PVQAG--SLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGlR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 416 TMTEYIGVMHQAPYLFRTTILNNIRiGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARI 495
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARA 1459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256953159 496 LLQ-DTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:PTZ00243 1460 LLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
362-571 |
8.98e-30 |
|
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: 118.13 E-value: 8.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGN-----IPTEAFGETMTEYIGVMHQAPYLF-RTTI 435
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaaMSRKELRELRRKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 436 LNNIRIGRE------EASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDEPT 509
Cdd:cd03294 120 LENVAFGLEvqgvprAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 510 TGLDPITEQQLLETFFEALKD--KTVIWITHHL-QGVTLMDQVIFIEDGQLEMSGTPEELLATNA 571
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNPA 253
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
345-580 |
1.04e-29 |
|
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: 117.49 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGE--ILLGNiptEAFGETMTE--- 419
Cdd:COG1119 4 LELRNVTVRRG--GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGE---RRGGEDVWElrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 YIGV----MHQApYLFRTTILNNIR------IGR----EEASEAEVWAVLEKVGLKEMVNQLpegLQTMvdeaglrfSGG 485
Cdd:COG1119 79 RIGLvspaLQLR-FPRDETVLDVVLsgffdsIGLyrepTDEQRERARELLELLGLAHLADRP---FGTL--------SQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 486 ERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETfFEAL---KDKTVIWITHHLQ-GVTLMDQVIFIEDGQLEMSG 561
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLAL-LDKLaaeGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAG 225
|
250
....*....|....*....
gi 256953159 562 TPEELLaTNAHYQKLYRID 580
Cdd:COG1119 226 PKEEVL-TSENLSEAFGLP 243
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
345-557 |
1.11e-29 |
|
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: 116.48 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTE---YI 421
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAPYLF-RTTILNNIRIG--------REEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLAL 492
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENITLApikvkgmsKAEA-EERALELLEKVGLADKADAYPAQL-----------SGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 493 ARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK-TVIWITHHL---QGVTlmDQVIFIEDGQL 557
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEMgfaREVA--DRVIFMDDGRI 213
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
341-575 |
1.15e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 119.18 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 341 NGTSLSIEHLSFAY-ENQEK--KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEA--FGE 415
Cdd:PRK13631 18 DDIILRVKNLYCVFdEKQENelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkkNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 416 TMTEY---------------IGVMHQAP--YLFRTTILNNIRIG-------REEASEAEVWaVLEKVGLKEmvnqlpegl 471
Cdd:PRK13631 98 ELITNpyskkiknfkelrrrVSMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKF-YLNKMGLDD--------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 472 qTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD-KTVIWITHHLQGV-TLMDQV 549
Cdd:PRK13631 168 -SYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVlEVADEV 246
|
250 260
....*....|....*....|....*.
gi 256953159 550 IFIEDGQLEMSGTPEELLATNAHYQK 575
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIFTDQHIINS 272
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
281-568 |
1.47e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 124.70 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 281 NHGGAANWIG---AFVLTVFPLIDAFAPLPAAAQETTIYKDSIRRFNELP-EGED-DSTEAPVQ--PNGTSLSIEHLSFA 353
Cdd:PLN03232 1164 NQAGFASTMGlllSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPsEATAiIENNRPVSgwPSRGSIKFEDVHLR 1243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 354 YENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGET-MTEYIGVMHQAPYLFR 432
Cdd:PLN03232 1244 YRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdLRRVLSIIPQSPVLFS 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 433 TTILNNIRiGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGL 512
Cdd:PLN03232 1324 GTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 513 DPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
360-568 |
1.69e-29 |
|
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: 116.38 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGE---TMTEY------IGVMHQAPYL 430
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-------GEditGLPPHeiarlgIGRTFQIPRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 431 FRT-TILNNIRIG----------------REEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALA 493
Cdd:cd03219 87 FPElTVLENVMVAaqartgsglllararrEEREARERAEELLERVGLADLADRPAGEL-----------SYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 494 RILLQDTPIVLLDEPTTGLDPiTEQQLLETFFEALKDK--TVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNP-EETEELAELIRELRERgiTVLLVEHDMDVVMsLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
340-563 |
1.74e-29 |
|
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: 115.59 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 340 PNGTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMT 418
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 EYIGVMHQAPYLFRTTILNNIRIgREEASEAEVWAVLEkvglkemvnqlpeglqtmVDEAGLRFSGGERHRLALARILLQ 498
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLDP-FDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 499 DTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTP 563
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
345-558 |
1.86e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.10 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEIllgnipteAFGETMTeyIGVM 424
Cdd:COG0488 316 LELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGETVK--IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFRT--TILNNIRIGREEASEAEVWAVLEKVGLKemvnqlPEGLQTMVDeaglRFSGGERHRLALARILLQDTPI 502
Cdd:COG0488 384 DQHQEELDPdkTVLDELRDGAPGGTEQEVRGYLGRFLFS------GDDAFKPVG----VLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256953159 503 VLLDEPTTGLDPITeQQLLEtffEALKD--KTVIWITHH---LQGVTlmDQVIFIEDGQLE 558
Cdd:COG0488 454 LLLDEPTNHLDIET-LEALE---EALDDfpGTVLLVSHDryfLDRVA--TRILEFEDGGVR 508
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
345-568 |
3.08e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 115.86 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY---I 421
Cdd:COG1126 2 IEIENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLrrkV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAPYLF-RTTILNNI--------RIGREEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLAL 492
Cdd:COG1126 80 GMVFQQFNLFpHLTVLENVtlapikvkKMSKAEA-EERAMELLERVGLADKADAYPAQL-----------SGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 493 ARILLQDTPIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITHHlqgvtlM-------DQVIFIEDGQLEMSGTPE 564
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlAKEGMTMVVVTHE------MgfarevaDRVVFMDGGRIVEEGPPE 221
|
....
gi 256953159 565 ELLA 568
Cdd:COG1126 222 EFFE 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
337-568 |
3.11e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 123.69 E-value: 3.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 337 PVQPNGTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGET 416
Cdd:PLN03130 1230 PGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLM 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 -MTEYIGVMHQAPYLFRTTILNNIRIGREEaSEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARI 495
Cdd:PLN03130 1310 dLRKVLGIIPQAPVLFSGTVRFNLDPFNEH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 496 LLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
345-580 |
9.07e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.21 E-value: 9.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAF-GETMTEYIGV 423
Cdd:COG4559 2 LEAENLSVRL--GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWsPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYL-FRTTILNNIRIGRE------EASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARIL 496
Cdd:COG4559 80 LPQHSSLaFPFTVEEVVALGRAphgssaAQDRQIVREALALVGLAHLAGRSYQTL-----------SGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 497 LQ------DTP-IVLLDEPTTGLDPITEQQLLetffEALKDKT-----VIWITHHLQgVTLM--DQVIFIEDGQLEMSGT 562
Cdd:COG4559 149 AQlwepvdGGPrWLFLDEPTSALDLAHQHAVL----RLARQLArrgggVVAVLHDLN-LAAQyaDRILLLHQGRLVAQGT 223
|
250
....*....|....*...
gi 256953159 563 PEELLaTNAHYQKLYRID 580
Cdd:COG4559 224 PEEVL-TDELLERVYGAD 240
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
107-568 |
1.42e-28 |
|
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: 121.59 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 107 LYNVLEKDAIFFKTKyRTGDILGLLSEDINHIQNLYLRTI------FPTVIAWILYIFLVIALgffswwfALCMLLMLGV 180
Cdd:TIGR00957 1045 LHNKLRSPMSFFERT-PSGNLVNRFSKELDTVDSMIPPVIkmfmgsLFNVIGALIVILLATPI-------AAVIIPPLGL 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 181 VVFLLPlvSVLVNGARQEK--HKYAKNELYQTLTDNILGVSDWVFSQRGSEFVARYETDeanvraLDEKMKQF------N 252
Cdd:TIGR00957 1117 LYFFVQ--RFYVASSRQLKrlESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLK------VDENQKAYypsivaN 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 253 R----GRDFV------LQLLFGVIA----IAVLAWTSVRFPGNHGGAANWigafvltvfpLIDAFAPLpaaaqETTIYkd 318
Cdd:TIGR00957 1189 RwlavRLECVgncivlFAALFAVISrhslSAGLVGLSVSYSLQVTFYLNW----------LVRMSSEM-----ETNIV-- 1251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 319 SIRRFNELPEGEddsTEAPVQPNGTS----------LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTL 388
Cdd:TIGR00957 1252 AVERLKEYSETE---KEAPWQIQETAppsgwpprgrVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSL 1328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 389 ASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIGVMHQAPYLFRTTILNNIRiGREEASEAEVWAVLEKVGLKEMVNQL 467
Cdd:TIGR00957 1329 TLGLFRINESAEGEIIIDGLNIAKIGlHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSAL 1407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 468 PEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQgvTLMD 547
Cdd:TIGR00957 1408 PDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLN--TIMD 1485
|
490 500
....*....|....*....|...
gi 256953159 548 --QVIFIEDGQLEMSGTPEELLA 568
Cdd:TIGR00957 1486 ytRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
345-575 |
2.13e-28 |
|
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: 114.57 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLAS-LIRgdLRPTSGEILLGNIPTEAFgeTMTEY--- 420
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaFLR--LLNTEGDIQIDGVSWNSV--PLQKWrka 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 IGVMHQAPYLFRTTILNNIRiGREEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDT 500
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 501 PIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLATNAHYQK 575
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
348-566 |
5.20e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.31 E-value: 5.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 348 EHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIGVMHQ 426
Cdd:PRK13648 11 KNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLRKHIGIVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 427 AP-YLFRTTI--------LNNIRIGREEASEaEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILL 497
Cdd:PRK13648 91 NPdNQFVGSIvkydvafgLENHAVPYDEMHR-RVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256953159 498 QDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
344-567 |
9.89e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 114.47 E-value: 9.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMT----- 418
Cdd:COG1118 2 SIEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLN-------GRDLFtnlpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 --EYIGVMHQAPYLFR-TTILNNIRIG------REEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHR 489
Cdd:COG1118 73 reRRVGFVFQHYALFPhMTVAENIAFGlrvrppSKAEIRARVEELLELVQLEGLADRYPSQL-----------SGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 490 LALARILLQDTPIVLLDEPTTGLDPITEQQL---LETFFEALKdKTVIWITH-HLQGVTLMDQVIFIEDGQLEMSGTPEE 565
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKVRKELrrwLRRLHDELG-GTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDE 220
|
..
gi 256953159 566 LL 567
Cdd:COG1118 221 VY 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-566 |
9.90e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.05 E-value: 9.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 335 EAPVQPNGTSLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKST-LASLIR-GDLRP---TSGEILLGNIP 409
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGD--KQALKDINLDIPENKVTALIGPSGCGKSTlLRCLNRmNDLIPgarVEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 410 TEAFGETMTE---YIGVMHQAPYLFRTTILNNI----RI----GREEASEAEVWAvLEKVGL-KEMVNQLpeglqtmvDE 477
Cdd:COG1117 80 IYDPDVDVVElrrRVGMVFQKPNPFPKSIYDNVayglRLhgikSKSELDEIVEES-LRKAALwDEVKDRL--------KK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 478 AGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKDK-TVIWITHHLQGVT-LMDQVIFIEDG 555
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILE-LKKDyTIVIVTHNMQQAArVSDYTAFFYLG 229
|
250
....*....|.
gi 256953159 556 QLEMSGTPEEL 566
Cdd:COG1117 230 ELVEFGPTEQI 240
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
345-561 |
1.11e-27 |
|
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: 110.75 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqeKKVLNDLSLTIPEKQkLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGVM 424
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAP----------YLFRTTILNNIRIGREEAseaEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALAR 494
Cdd:cd03264 78 PQEFgvypnftvreFLDYIAWLKGIPSKEVKA---RVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 495 ILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLM-DQVIFIEDGQLEMSG 561
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
345-556 |
2.73e-27 |
|
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: 107.15 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNipteafgetmTEYIGVM 424
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQapylfrttilnnirigreeaseaevwavlekvglkemvnqlpeglqtmvdeaglrFSGGERHRLALARILLQDTPIVL 504
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 505 LDEPTTGLDpITEQQLLETFFEALKdKTVIWITH---HLQGVTlmDQVIFIEDGQ 556
Cdd:cd03221 94 LDEPTNHLD-LESIEALEEALKEYP-GTVILVSHdryFLDQVA--TKIIELEDGK 144
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
350-566 |
4.43e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.05 E-value: 4.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 350 LSFAYENqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIP-TEAFGETMTEYIGVMHQAP 428
Cdd:PRK13652 9 LCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPiTKENIREVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 429 --YLFRTTILNNIRIG------REEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDT 500
Cdd:PRK13652 88 ddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 501 PIVLLDEPTTGLDPITEQQLLEtFFEALKDK---TVIWITHHLQGVTLMDQVIFI-EDGQLEMSGTPEEL 566
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELID-FLNDLPETygmTVIFSTHQLDLVPEMADYIYVmDKGRIVAYGTVEEI 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
345-568 |
4.90e-27 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 109.59 E-value: 4.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKV--LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILL-GNIPTEAFGETMTEY- 420
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 --IGVMHQAPYLF-RTTILNNI----RIGREEASEAE--VWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLA 491
Cdd:cd03258 82 rrIGMIFQHFNLLsSRTVFENValplEIAGVPKAEIEerVLELLELVGLEDKADAYPAQL-----------SGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQLLETffeaLKDK------TVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPE 564
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILAL----LRDInrelglTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVE 226
|
....
gi 256953159 565 ELLA 568
Cdd:cd03258 227 EVFA 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
319-576 |
5.23e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 117.00 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 319 SIRRFNELPEGEDD--STEAPVQPNGTSLSIEHLSFAYENQ-EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGD 395
Cdd:PLN03232 587 SLQRIEELLLSEERilAQNPPLQPGAPAISIKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 396 LRP--TSGEILLGNIpteafgetmteyiGVMHQAPYLFRTTILNNIRIGREEASEaEVWAVLEKVGLKEMVNQLPEGLQT 473
Cdd:PLN03232 667 LSHaeTSSVVIRGSV-------------AYVPQVSWIFNATVRENILFGSDFESE-RYWRAIDVTALQHDLDLLPGRDLT 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 474 MVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFF-EALKDKTVIWITHHLQGVTLMDQVIFI 552
Cdd:PLN03232 733 EIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMkDELKGKTRVLVTNQLHFLPLMDRIILV 812
|
250 260
....*....|....*....|....
gi 256953159 553 EDGQLEMSGTPEELLATNAHYQKL 576
Cdd:PLN03232 813 SEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
345-578 |
7.28e-27 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 109.31 E-value: 7.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILL-GNIPTEAFGE---TMTEY 420
Cdd:TIGR02315 2 LEVENLSKVYPNG-KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLeGTDITKLRGKklrKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 IGVMHQAPYLF-RTTILNNIRIGR--------------EEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGG 485
Cdd:TIGR02315 81 IGMIFQHYNLIeRLTVLENVLHGRlgykptwrsllgrfSEEDKERALSALERVGLADKAYQRADQL-----------SGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 486 ERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVT-LMDQVIFIEDGQLEMSGT 562
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKkYADRIVGLKAGEIVFDGA 229
|
250
....*....|....*.
gi 256953159 563 PEELlaTNAHYQKLYR 578
Cdd:TIGR02315 230 PSEL--DDEVLRHIYG 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
345-567 |
8.11e-27 |
|
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: 108.96 E-value: 8.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEkkvLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG-----NIPTEAFGetmte 419
Cdd:cd03299 1 LKVENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditNLPPEKRD----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 yIGVMHQAPYLF-RTTILNNIRIG-------REEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLA 491
Cdd:cd03299 73 -ISYVPQNYALFpHMTVYKNIAYGlkkrkvdKKEI-ERKVLEIAEMLGIDHLLNRKPETL-----------SGGEQQRVA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALK--DKTVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPEELL 567
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
345-540 |
1.02e-26 |
|
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: 110.91 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLS--FAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRP---TSGEILLGNIP-TEAFGETMT 418
Cdd:COG0444 2 LEVRNLKvyFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDlLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 EY----IGVMHQAPYlfrtTILN-NIRIGR---------EEASEAEVWA----VLEKVGL---KEMVNQLP-Eglqtmvd 476
Cdd:COG0444 82 KIrgreIQMIFQDPM----TSLNpVMTVGDqiaeplrihGGLSKAEAREraieLLERVGLpdpERRLDRYPhE------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 477 eaglrFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKDK---TVIWITHHL 540
Cdd:COG0444 151 -----LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKD-LQRElglAILFITHDL 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
360-568 |
1.30e-26 |
|
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: 108.97 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIP--------------------TEAFGEtMT- 418
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitglpphriarlgiartfqnPRLFPE-LTv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 -E--YIGVMHQAPYLFRTTILNNIRIGREE-ASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALAR 494
Cdd:COG0411 97 lEnvLVAAHARLGRGLLAALLRLPRARREErEARERAEELLERVGLADRADEPAGNL-----------SYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 495 ILLQDTPIVLLDEPTTGLDPiTEQQLLETFFEALKDK---TVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNP-EETEELAELIRRLRDErgiTILLIEHDMDLVMgLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
362-555 |
1.51e-26 |
|
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: 107.80 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY-----IGVMHQAPYLFRTTIL 436
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSrnrysVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 437 NNIRIGrEEASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLD-PI 515
Cdd:cd03290 97 ENITFG-SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 256953159 516 TEQQLLETFFEALKD--KTVIWITHHLQGVTLMDQVIFIEDG 555
Cdd:cd03290 176 SDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
345-571 |
1.85e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 107.75 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKvlndLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEY---- 420
Cdd:PRK10771 2 LKLTDITWLYHHLPMR----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN-------GQDHTTTppsr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 --IGVMHQAPYLF-RTTILNNIRIGRE------EASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLA 491
Cdd:PRK10771 71 rpVSMLFQENNLFsHLTVAQNIGLGLNpglklnAAQREKLHAIARQMGIEDLLARLPGQL-----------SGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQ-GVTLMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
...
gi 256953159 569 TNA 571
Cdd:PRK10771 220 GKA 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
360-568 |
2.09e-26 |
|
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: 112.97 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGE--ILLG----NIPTEAFGET--MTEYIGVMHQAPYLF 431
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGdewvDMTKPGPDGRgrAKRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 432 -RTTILNNIR--IGREEASE-AEVWAV--LEKVGLKEmvNQLPEGLQTMVDEaglrFSGGERHRLALARILLQDTPIVLL 505
Cdd:TIGR03269 378 pHRTVLDNLTeaIGLELPDElARMKAVitLKMVGFDE--EKAEEILDKYPDE----LSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 506 DEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
350-561 |
2.31e-26 |
|
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: 107.36 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 350 LSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRP---TSGEILLGNIPTEAfgETMTEYIGVMHQ 426
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP--DQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 427 ----APYL-FRTTIL--NNIRIGREEASE--AEVWAV--LEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARI 495
Cdd:cd03234 89 ddilLPGLtVRETLTytAILRLPRKSSDAirKKRVEDvlLRDLALTRIGGNLVKGI-----------SGGERRRVSIAVQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 496 LLQDTPIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIwITHHLQG---VTLMDQVIFIEDGQLEMSG 561
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVI-LTIHQPRsdlFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
348-566 |
2.65e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 348 EHLSFAY----ENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGET--MTEYI 421
Cdd:PRK13633 8 KNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAP--YLFRTTILNNIRIGRE----EASE--AEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALA 493
Cdd:PRK13633 88 GMVFQNPdnQIVATIVEEDVAFGPEnlgiPPEEirERVDESLKKVGMYEYRRHAPHLL-----------SGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 494 RILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
345-568 |
3.53e-26 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 106.75 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG-----NIPTE---AFGet 416
Cdd:cd03224 1 LEVENLNAGYG--KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditGLPPHeraRAG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 mteyIGVMHQAPYLFRT-TILNNIRIGREEASEAEVWAVLEKV-----GLKEMVNQLpeglqtmvdeAGLrFSGGERHRL 490
Cdd:cd03224 77 ----IGYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERVyelfpRLKERRKQL----------AGT-LSGGEQQML 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 491 ALARILLQDTPIVLLDEPTTGLDPITEQQLLETfFEALKDK--TVIWITHHLQGVTLM-DQVIFIEDGQLEMSGTPEELL 567
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEA-IRELRDEgvTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELL 220
|
.
gi 256953159 568 A 568
Cdd:cd03224 221 A 221
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
344-577 |
4.36e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.38 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYE---NQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG--NIPTEAFGETMT 418
Cdd:PRK13641 2 SIKFENVDYIYSpgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyHITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 EY---IGVMHQAP--YLFRTTILNNIRIG-------REEASEAEV-WavLEKVGLKEmvnqlpeglqTMVDEAGLRFSGG 485
Cdd:PRK13641 82 KLrkkVSLVFQFPeaQLFENTVLKDVEFGpknfgfsEDEAKEKALkW--LKKVGLSE----------DLISKSPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 486 ERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD-KTVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTP 563
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAeYADDVLVLEHGKLIKHASP 229
|
250
....*....|....
gi 256953159 564 EELLATNAHYQKLY 577
Cdd:PRK13641 230 KEIFSDKEWLKKHY 243
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
339-558 |
8.79e-26 |
|
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: 105.98 E-value: 8.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 339 QPNGTSLSIEHLSFAYENQEKKV--LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLgnipteaFGET 416
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL-------AGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 MT------------EYIGVMHQAPYLFRT-TILNNIRIGREEASEAEVW----AVLEKVGLKEMVNQLPEGLqtmvdeag 479
Cdd:COG4181 76 LFaldedararlraRHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARararALLERVGLGHRLDHYPAQL-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 480 lrfSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVTLMDQVIFIEDGQL 557
Cdd:COG4181 148 ---SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRL 224
|
.
gi 256953159 558 E 558
Cdd:COG4181 225 V 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
344-566 |
2.05e-25 |
|
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: 105.11 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNipTEAFGETMTEY-IG 422
Cdd:cd03296 2 SIEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG--EDATDVPVQERnVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 VMHQAPYLFR-TTILNNIRIG------REEASEAE----VWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLA 491
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFGlrvkprSERPPEAEirakVHELLKLVQLDWLADRYPAQL-----------SGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQlLETFFEALKDK---TVIWITH-HLQGVTLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKE-LRRWLRRLHDElhvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
347-559 |
3.03e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.77 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 347 IEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNipteafGETmteyIGVMHQ 426
Cdd:COG0488 1 LENLSKSFG--GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR----IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 427 APYLF-RTTILNNIRIGREE--ASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEA--------------GLRF------- 482
Cdd:COG0488 69 EPPLDdDLTVLDTVLDGDAElrALEAELEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsGLGFpeedldr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 483 -----SGGERHRLALARILLQDTPIVLLDEPTTGLDpITEQQLLETFfeaLKD--KTVIWITH--H-LQGVTlmDQVIFI 552
Cdd:COG0488 149 pvselSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LESIEWLEEF---LKNypGTVLVVSHdrYfLDRVA--TRILEL 222
|
....*..
gi 256953159 553 EDGQLEM 559
Cdd:COG0488 223 DRGKLTL 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
343-566 |
3.22e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 107.08 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEY-- 420
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG-------GRDVTDLpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 ----IGVMHQAPYLFRT-TILNNI----RIGREEASEAE--VWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHR 489
Cdd:COG3839 73 kdrnIAMVFQSYALYPHmTVYENIafplKLRKVPKAEIDrrVREAAELLGLEDLLDRKPKQL-----------SGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 490 LALARILLQDTPIVLLDEPTTGLDP------ITE-QQLLETFfealkDKTVIWITHH-LQGVTLMDQVIFIEDGQLEMSG 561
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAklrvemRAEiKRLHRRL-----GTTTIYVTHDqVEAMTLADRIAVMNDGRIQQVG 216
|
....*
gi 256953159 562 TPEEL 566
Cdd:COG3839 217 TPEEL 221
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
357-557 |
4.39e-25 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 103.59 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 357 QEKK----VLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEIL-----LGNIPTEAFGETMTEYIGVMHQA 427
Cdd:TIGR02211 12 QEGKldtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLfngqsLSKLSSNERAKLRNKKLGFIYQF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 428 PYLFRT-TILNNIR----IGREEASEAE--VWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDT 500
Cdd:TIGR02211 92 HHLLPDfTALENVAmpllIGKKSVKEAKerAYEMLEKVGLEHRINHRPSEL-----------SGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 501 PIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVTLMDQVIFIEDGQL 557
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELntSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
345-538 |
6.07e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.17 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYE--NQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMteyiG 422
Cdd:COG4525 4 LTVRHVSVRYPggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR----G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 VMHQA----PYLfrtTILNNIRIG------REEASEAEVWAVLEKVGLKE----MVNQLpeglqtmvdeaglrfSGGERH 488
Cdd:COG4525 80 VVFQKdallPWL---NVLDNVAFGlrlrgvPKAERRARAEELLALVGLADfarrRIWQL---------------SGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 256953159 489 RLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITH 538
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITH 193
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
364-569 |
6.62e-25 |
|
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: 106.35 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 364 DLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTE------------YIGVMHQAPYLF 431
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN-------GRTLFDsrkgiflppekrRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 432 -RTTILNNIRIGREEASEAEVW----AVLEKVGLKEMVNQLPEglqtmvdeaglRFSGGERHRLALARILLQDTPIVLLD 506
Cdd:TIGR02142 88 pHLSVRGNLRYGMKRARPSERRisfeRVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 507 EPTTGLDPITEQQLLeTFFEALKDKT---VIWITHHLQGVTLM-DQVIFIEDGQLEMSGTPEELLAT 569
Cdd:TIGR02142 157 EPLAALDDPRKYEIL-PYLERLHAEFgipILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
260-539 |
6.98e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.74 E-value: 6.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 260 QLLFGVIAIAVLAWTSVRfpgnhgGAANWIgafvltvfplIDAFAPLPAaaqettiYKDSIRRFNEL------PEGEDDS 333
Cdd:COG4178 295 EITLGGLMQAASAFGQVQ------GALSWF----------VDNYQSLAE-------WRATVDRLAGFeealeaADALPEA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 334 TEAPVQPNGTSLSIEHLSFaYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGdLRP-TSGEILLgniPTEA 412
Cdd:COG4178 352 ASRIETSEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIAR---PAGA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 413 fgETMteyigVMHQAPYLfrttILNNIR------IGREEASEAEVWAVLEKVGLKEMVNQLPEglqtmVDEAGLRFSGGE 486
Cdd:COG4178 427 --RVL-----FLPQRPYL----PLGTLReallypATAEAFSDAELREALEAVGLGHLAERLDE-----EADWDQVLSLGE 490
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 256953159 487 RHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHH 539
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
343-568 |
7.27e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.54 E-value: 7.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGE---TMTE 419
Cdd:PRK13636 4 YILKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 YIGVMHQAP--YLFRTTILNNIRIGR------EEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLA 491
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGAvnlklpEDEVRKRVDNALKRTGIEHLKDKPTHCL-----------SFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALK--DKTVIWITHHLQGVTLM-DQVIFIEDGQLEMSGTPEELLA 568
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
345-577 |
7.81e-25 |
|
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: 103.01 E-value: 7.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEY---- 420
Cdd:cd03218 1 LRAENLSKRYGK--RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD-------GQDITKLpmhk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 -----IGVMHQAPYLFRT-TILNNIRigreeaseaevwAVLEKVGL-----KEMVNQLPE--GLQTMVDEAGLRFSGGER 487
Cdd:cd03218 72 rarlgIGYLPQEASIFRKlTVEENIL------------AVLEIRGLskkerEEKLEELLEefHITHLRKSKASSLSGGER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 488 HRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKDKTV-IWITHHLQGVTL--MDQVIFIEDGQLEMSGTPE 564
Cdd:cd03218 140 RRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKI-LKDRGIgVLITDHNVRETLsiTDRAYIIYEGKVLAEGTPE 218
|
250
....*....|...
gi 256953159 565 ElLATNAHYQKLY 577
Cdd:cd03218 219 E-IAANELVRKVY 230
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
354-538 |
8.35e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 101.73 E-value: 8.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 354 YENqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY---IGVMHQAP-- 428
Cdd:TIGR01166 1 YPG-GPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERrqrVGLVFQDPdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 429 YLFRTTILNNIRIG------REEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPI 502
Cdd:TIGR01166 80 QLFAADVDQDVAFGplnlglSEAEVERRVREALTAVGASGLRERPTHCL-----------SGGEKKRVAIAGAVAMRPDV 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 256953159 503 VLLDEPTTGLDPITEQQLLETfFEALKD--KTVIWITH 538
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAI-LRRLRAegMTVVISTH 185
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
358-561 |
8.39e-25 |
|
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: 102.37 E-value: 8.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLN---DLSLTIPEkQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG-----------NIPTEAFGetmteyIGV 423
Cdd:cd03297 7 EKRLPDftlKIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkiNLPPQQRK------IGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYLF-RTTILNNIRIGREEASEAE----VWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQ 498
Cdd:cd03297 80 VFQQYALFpHLNVRENLAFGLKRKRNREdrisVDELLDLLGLDHLLNRYPAQL-----------SGGEKQRVALARALAA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 499 DTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHLQGVTLM-DQVIFIEDGQLEMSG 561
Cdd:cd03297 149 QPELLLLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
345-557 |
9.29e-25 |
|
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: 102.30 E-value: 9.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEI-LLGNIPTEAfgETMTEYIGV 423
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYQKN--IEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAP--YLFRTTiLNNIRIGREEA--SEAEVWAVLEKVGLKemvnqlpeglqtmvDEAGLR---FSGGERHRLALARIL 496
Cdd:cd03268 77 LIEAPgfYPNLTA-RENLRLLARLLgiRKKRIDEVLDVVGLK--------------DSAKKKvkgFSLGMKQRLGIALAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 497 LQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKD--KTVIWITHHLQGVTLM-DQVIFIEDGQL 557
Cdd:cd03268 142 LGNPDLLILDEPTNGLDPDGIKELRE-LILSLRDqgITVLISSHLLSEIQKVaDRIGIINKGKL 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
364-568 |
1.05e-24 |
|
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: 105.57 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 364 DLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG-----------NIPTEAFGetmteyIGVMHQAPYLF- 431
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqdsargiFLPPHRRR------IGYVFQEARLFp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 432 RTTILNNIRIGREEASEAEVWAVLEKV----GLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDE 507
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVvellGIGHLLDRRPATL-----------SGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 508 PTTGLDPITEQQLLEtFFEALKDKT---VIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:COG4148 160 PLAALDLARKAEILP-YLERLRDELdipILYVSHSLDEVArLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-558 |
1.44e-24 |
|
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: 107.58 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 21 FLKRYKKTLYFALLLGFLTFFSAGALMftsgYLISRAASLPENILLIYIP-----IVLTRAFGIGrpVFRYVERLTSHnw 95
Cdd:COG4615 7 LLRESRWLLLLALLLGLLSGLANAGLI----ALINQALNATGAALARLLLlfaglLVLLLLSRLA--SQLLLTRLGQH-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 96 vlkMTSDLRLKLYN-VLEKDAIFFKtKYRTGDILGLLSEDINHIQNLYLRtIFPTVIAWILYIFLVIALGFFSWW-FALC 173
Cdd:COG4615 79 ---AVARLRLRLSRrILAAPLERLE-RIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPlFLLT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 174 MLLM-LGVVVFLLPLVSV--LVNGARQEKHKYakNELYQTLTDNI--LGVSdwvfSQRGSEFVAR-YETDEANVRALDEK 247
Cdd:COG4615 154 LVLLgLGVAGYRLLVRRArrHLRRAREAEDRL--FKHFRALLEGFkeLKLN----RRRRRAFFDEdLQPTAERYRDLRIR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 248 -MKQFNRGRDFVLQLLFGVIAIAVLAwtsvrFPGNHGGAANWIGAFVLTVF----PLIDAFAPLPAAAQEttiyKDSIRR 322
Cdd:COG4615 228 aDTIFALANNWGNLLFFALIGLILFL-----LPALGWADPAVLSGFVLVLLflrgPLSQLVGALPTLSRA----NVALRK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 323 FNEL-------PEGEDDSTEAPVQPNGTSLSIEHLSFAYENQEKK---VLNDLSLTIPEKQKLAILGRSGSGKSTLASLI 392
Cdd:COG4615 299 IEELelalaaaEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 393 RGDLRPTSGEILLGNIPTEAfgETMTEY---IGVMHQAPYLFRTTILnniriGREEASEAEVWAVLEKVGLKEMVnQLPE 469
Cdd:COG4615 379 TGLYRPESGEILLDGQPVTA--DNREAYrqlFSAVFSDFHLFDRLLG-----LDGEADPARARELLERLELDHKV-SVED 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 470 G-LQTmvdeagLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPiteqQLLETFFE----ALKD--KTVIWITH---- 538
Cdd:COG4615 451 GrFST------TDLSQGQRKRLALLVALLEDRPILVFDEWAADQDP----EFRRVFYTellpELKArgKTVIAISHddry 520
|
570 580
....*....|....*....|.
gi 256953159 539 -HlqgvtLMDQVIFIEDGQLE 558
Cdd:COG4615 521 fD-----LADRVLKMDYGKLV 536
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
347-568 |
1.44e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 103.93 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 347 IEHLSFAYENQ---EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY--- 420
Cdd:PRK13645 9 LDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 ---IGVMHQAP--YLFRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVnQLPEglqTMVDEAGLRFSGGERHRLALARI 495
Cdd:PRK13645 89 rkeIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPE---DYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 496 LLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHL-QGVTLMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
71-563 |
2.17e-24 |
|
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: 108.95 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 71 IVLTRAFgigrPVFRYVERLTSHNWVLK---MTSDLRLK--LYNVLEKDAIFFKTKYRtgDILGLLSEDInhiqnlYLRT 145
Cdd:TIGR01257 649 IILNRCF----PIFMVLAWIYSVSMTVKsivLEKELRLKetLKNQGVSNAVIWCTWFL--DSFSIMSMSI------FLLT 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 146 IFPT-------VIAWILYIFLviaLGFFSWWFALCMLLML------------GVVVFLLPLVSVLVNgARQEKHKYAKNE 206
Cdd:TIGR01257 717 IFIMhgrilhySDPFILFLFL---LAFSTATIMQCFLLSTffskaslaaacsGVIYFTLYLPHILCF-AWQDRMTADLKT 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 207 LYQTLTDNILGVsdwvfsqrGSEFVARYETDE-----ANVRALDEKMKQFNrgrdFVLQLLFGVIAIAV---LAW-TSVR 277
Cdd:TIGR01257 793 AVSLLSPVAFGF--------GTEYLVRFEEQGlglqwSNIGNSPLEGDEFS----FLLSMKMMLLDAALyglLAWyLDQV 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 278 FPGNHGGAANWIGAFVLTVFPLIDAFAPLPAAAQETTIYKDSIRRFNELPEGEDDS---TEAPVQPNGtsLSIEHLSFAY 354
Cdd:TIGR01257 861 FPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEEMEDPEHPEGINDSffeRELPGLVPG--VCVKNLVKIF 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 355 ENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGVMHQAPYLFR-T 433
Cdd:TIGR01257 939 EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHhL 1018
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 434 TILNNIRI-----GRE-EASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDE 507
Cdd:TIGR01257 1019 TVAEHILFyaqlkGRSwEEAQLEMEAMLEDTGLHHKRNEEAQDL-----------SGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 508 PTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVTLM-DQVIFIEDGQLEMSGTP 563
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGTP 1144
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
345-566 |
3.18e-24 |
|
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: 101.54 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQekKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG-----NIPTEAFGetmte 419
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditNLPPHKRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 yIGVMHQAPYLF-RTTILNNIRIG------REEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLAL 492
Cdd:cd03300 74 -VNTVFQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 493 ARILLQDTPIVLLDEPTTGLDpiteQQLLETFFEALKD------KTVIWITH-HLQGVTLMDQVIFIEDGQLEMSGTPEE 565
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALD----LKLRKDMQLELKRlqkelgITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
.
gi 256953159 566 L 566
Cdd:cd03300 218 I 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
320-578 |
3.83e-24 |
|
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: 107.72 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 320 IRRFNELPEGEDDSTE-APVQP-NGTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLR 397
Cdd:TIGR00957 610 LRIFLSHEELEPDSIErRTIKPgEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 398 PTSGEIllgnipteafgeTMTEYIGVMHQAPYLFRTTILNNIRIGREeASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDE 477
Cdd:TIGR00957 690 KVEGHV------------HMKGSVAYVPQQAWIQNDSLRENILFGKA-LNEKYYQQVLEACALLPDLEILPSGDRTEIGE 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 478 AGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFF---EALKDKTVIWITHHLQGVTLMDQVIFIED 554
Cdd:TIGR00957 757 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpeGVLKNKTRILVTHGISYLPQVDVIIVMSG 836
|
250 260
....*....|....*....|....
gi 256953159 555 GQLEMSGTPEELLATNAHYQKLYR 578
Cdd:TIGR00957 837 GKISEMGSYQELLQRDGAFAEFLR 860
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
345-557 |
4.16e-24 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 100.94 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPteaFGETMTEYIGVM 424
Cdd:TIGR03740 1 LETKNLSKRFGKQT--AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP---WTRKDLHKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFRT-TILNN--IRIGREEASEAEVWAVLEKVGL----KEMVNQlpeglqtmvdeaglrFSGGERHRLALARILL 497
Cdd:TIGR03740 76 IESPPLYENlTARENlkVHTTLLGLPDSRIDEVLNIVDLtntgKKKAKQ---------------FSLGMKQRLGIAIALL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 498 QDTPIVLLDEPTTGLDPITEQQLLEtFFEALKDK--TVIWITHHLQGVTLM-DQVIFIEDGQL 557
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRE-LIRSFPEQgiTVILSSHILSEVQQLaDHIGIISEGVL 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
345-568 |
4.59e-24 |
|
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: 106.04 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRG--DLRPTSGEILL--------GNIPTEAF- 413
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYhvalcekcGYVERPSKv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 414 -------GETMTEY------------------IGVMHQAPYLF--RTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNq 466
Cdd:TIGR03269 79 gepcpvcGGTLEPEevdfwnlsdklrrrirkrIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQ- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 467 lpegLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTV-IWITHHLQGVT- 544
Cdd:TIGR03269 158 ----LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHWPEVIe 233
|
250 260
....*....|....*....|....*
gi 256953159 545 -LMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:TIGR03269 234 dLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
344-554 |
7.10e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.86 E-value: 7.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRP---TSGEILLGN-----IPTEAFGe 415
Cdd:COG4136 1 MLSLENLTITLGGRP--LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltaLPAEQRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 416 tmteyIGVMHQAPYLF-RTTILNNI------RIGREEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERH 488
Cdd:COG4136 78 -----IGILFQDDLLFpHLSVGENLafalppTIGRAQR-RARVEQALEEAGLAGFADRDPATL-----------SGGQRA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 489 RLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKT--VIWITHHLQGVTLMDQVIFIED 554
Cdd:COG4136 141 RVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGipALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
360-557 |
1.12e-23 |
|
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: 99.40 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY----IGVMHQAPYLFRT-T 434
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrkIGVVFQDFRLLPDrN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 435 ILNNIRI-------GREEASEaEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDE 507
Cdd:cd03292 95 VYENVAFalevtgvPPREIRK-RVPAALELVGLSHKHRALPAEL-----------SGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 256953159 508 PTTGLDPITEQQLLETFFEA-LKDKTVIWITHHLQGVTLMD-QVIFIEDGQL 557
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
345-557 |
1.23e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.24 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIR--GDLRP---TSGEILLG--NI--PTEAFGE 415
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNghNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 416 TMTEyIGVMHQAPYLFRTTILNNIRIGreeaseAEVWAVLEKVGLKEMVNQLPEG------LQTMVDEAGLRFSGGERHR 489
Cdd:PRK14239 84 LRKE-IGMVFQQPNPFPMSIYENVVYG------LRLKGIKDKQVLDEAVEKSLKGasiwdeVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 490 LALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVT-LMDQVIFIEDGQL 557
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASrISDRTGFFLDGDL 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
345-568 |
1.45e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYeNQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY---I 421
Cdd:PRK13639 2 LETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrktV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAP--YLFRTTILNNIRIG------REEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALA 493
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 494 RILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKDK--TVIWITHHLQGVTL-MDQVIFIEDGQLEMSGTPEELLA 568
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYD-LNKEgiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
358-568 |
2.79e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.24 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEA-----FGETMTEYIGVMHQAP--YL 430
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRPVRKRIGMVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 431 FRTTILNNIRIGRE------EASEAEVWAVLEKVGLKEMVNQLpeglqtmvdeAGLRFSGGERHRLALARILLQDTPIVL 504
Cdd:PRK13646 99 FEDTVEREIIFGPKnfkmnlDEVKNYAHRLLMDLGFSRDVMSQ----------SPFQMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 505 LDEPTTGLDPITEQQLLETF--FEALKDKTVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
345-561 |
2.90e-23 |
|
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: 98.21 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKV--LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIG 422
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 VMHQAPYLF-RTTILNNIR-------IGREEAsEAEVWAVLEKVGLKEMVNQLPEGlqtmvdeaglrFSGGERHRLALAR 494
Cdd:cd03266 82 FVSDSTGLYdRLTARENLEyfaglygLKGDEL-TARLEELADRLGMEELLDRRVGG-----------FSTGMRQKVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 495 ILLQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKD--KTVIWITHHLQGV-TLMDQVIFIEDGQLEMSG 561
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALRE-FIRQLRAlgKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
345-561 |
3.80e-23 |
|
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: 97.71 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEY---- 420
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-------GRDVTDLppkd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 --IGVMHQAPYLF-RTTILNNI------RIGREEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLA 491
Cdd:cd03301 72 rdIAMVFQNYALYpHMTVYDNIafglklRKVPKDEIDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQL---LETFFEALKdKTVIWITH-HLQGVTLMDQVIFIEDGQLEMSG 561
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMraeLKRLQQRLG-TTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
358-569 |
4.03e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 4.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAF-GETMTEYIGVMHQAPYL-FRTTI 435
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALsARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 436 LNNIRIGR----------EEASEAEVWAVLEKVGlkemVNQLpeglqtmVDEAGLRFSGGERHRLALARILLQDTPIVLL 505
Cdd:PRK09536 95 RQVVEMGRtphrsrfdtwTETDRAAVERAMERTG----VAQF-------ADRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 506 DEPTTGLDPITEQQLLETFFEALKD-KTVIWITHHLQ-GVTLMDQVIFIEDGQLEMSGTPEELLAT 569
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTA 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
344-566 |
6.59e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.54 E-value: 6.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMT----- 418
Cdd:PRK10851 2 SIEIANIKKSFGR--TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-------GTDVSrlhar 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 -EYIGVMHQAPYLFR-TTILNNIRIG------REEASEAE----VWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGE 486
Cdd:PRK10851 73 dRKVGFVFQHYALFRhMTVFDNIAFGltvlprRERPNAAAikakVTQLLEMVQLAHLADRYPAQL-----------SGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 487 RHRLALARILLQDTPIVLLDEPTTGLDPITEQQL---LETFFEALKdKTVIWITHHLQ-GVTLMDQVIFIEDGQLEMSGT 562
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALDAQVRKELrrwLRQLHEELK-FTSVFVTHDQEeAMEVADRVVVMSQGNIEQAGT 220
|
....
gi 256953159 563 PEEL 566
Cdd:PRK10851 221 PDQV 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
319-576 |
7.39e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 104.05 E-value: 7.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 319 SIRRFNELPEGEDD--STEAPVQPNGTSLSIEHLSFAYENQ-EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGD 395
Cdd:PLN03130 587 SLKRLEELLLAEERvlLPNPPLEPGLPAISIKNGYFSWDSKaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGE 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 396 LRPTSGeillGNIpteafgeTMTEYIGVMHQAPYLFRTTILNNIRIGREEASEaEVWAVLEKVGLKEMVNQLPEGLQTMV 475
Cdd:PLN03130 667 LPPRSD----ASV-------VIRGTVAYVPQVSWIFNATVRDNILFGSPFDPE-RYERAIDVTALQHDLDLLPGGDLTEI 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 476 DEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFF-EALKDKTVIWITHHLQGVTLMDQVIFIED 554
Cdd:PLN03130 735 GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIkDELRGKTRVLVTNQLHFLSQVDRIILVHE 814
|
250 260
....*....|....*....|..
gi 256953159 555 GQLEMSGTPEELLATNAHYQKL 576
Cdd:PLN03130 815 GMIKEEGTYEELSNNGPLFQKL 836
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
345-577 |
7.55e-23 |
|
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: 97.36 E-value: 7.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTeyigvm 424
Cdd:COG0410 4 LEVENLHAGYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD-------GEDIT------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPY---------------LFRT-TILNNIRIG-REEASEAEVWAVLEKVG-----LKEMVNQLpeglqtmvdeAGLrF 482
Cdd:COG0410 69 GLPPHriarlgigyvpegrrIFPSlTVEENLLLGaYARRDRAEVRADLERVYelfprLKERRRQR----------AGT-L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 483 SGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETfFEALKDktviwithhlQGVT-LM------------DQV 549
Cdd:COG0410 138 SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEI-IRRLNR----------EGVTiLLveqnarfaleiaDRA 206
|
250 260
....*....|....*....|....*...
gi 256953159 550 IFIEDGQLEMSGTPEELLAtNAHYQKLY 577
Cdd:COG0410 207 YVLERGRIVLEGTAAELLA-DPEVREAY 233
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
344-568 |
7.56e-23 |
|
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: 97.73 E-value: 7.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFgeTMTEY--- 420
Cdd:TIGR04406 1 TLVAENLIKSY--KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHL--PMHERarl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 -IGVMHQAPYLFRT-TILNNIRI---GREEASEAEVWAVLEKVgLKEMvnqlpeGLQTMVDEAGLRFSGGERHRLALARI 495
Cdd:TIGR04406 77 gIGYLPQEASIFRKlTVEENIMAvleIRKDLDRAEREERLEAL-LEEF------QISHLRDNKAMSLSGGERRRVEIARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 496 LLQDTPIVLLDEPTTGLDPITEQQlLETFFEALKDKTV-IWITHHLQGVTL--MDQVIFIEDGQLEMSGTPEELLA 568
Cdd:TIGR04406 150 LATNPKFILLDEPFAGVDPIAVGD-IKKIIKHLKERGIgVLITDHNVRETLdiCDRAYIISDGKVLAEGTPAEIVA 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
345-567 |
1.02e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 98.65 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQE---KKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGET----- 416
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 MTEYIGVMHQAP--YLFRTTILNNIRIGRE----EASEAEVWAV--LEKVGL-KEMVNQLPeglqtmvdeagLRFSGGER 487
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQnfgiPKEKAEKIAAekLEMVGLaDEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 488 HRLALARILLQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKD--KTVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPE 564
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQsgQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPS 229
|
...
gi 256953159 565 ELL 567
Cdd:PRK13643 230 DVF 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
345-556 |
1.05e-22 |
|
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: 96.58 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYI--- 421
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLpee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 -------GVMHQAPYLFRTTILNNirigREEASEAEVWavLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALAR 494
Cdd:cd03269 79 rglypkmKVIDQLVYLAQLKGLKK----EEARRRIDEW--LERLELSEYANKRVEEL-----------SKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 495 ILLQDTPIVLLDEPTTGLDPITeQQLLETFFEALKD--KTVIWITHHLQGVT-LMDQVIFIEDGQ 556
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVN-VELLKDVIRELARagKTVILSTHQMELVEeLCDRVLLLNKGR 205
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
323-566 |
1.12e-22 |
|
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: 98.39 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 323 FNELPEGEDDSTEAPVQPNG-TSLSIEHLSFayenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSG 401
Cdd:cd03291 17 FGELLEKAKQENNDRKHSSDdNNLFFSNLCL----VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 402 EIllgnipteafgeTMTEYIGVMHQAPYLFRTTILNNIRIGREeASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLR 481
Cdd:cd03291 93 KI------------KHSGRISFSSQFSWIMPGTIKENIIFGVS-YDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 482 FSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLET-FFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMS 560
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFY 239
|
....*.
gi 256953159 561 GTPEEL 566
Cdd:cd03291 240 GTFSEL 245
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
361-550 |
1.27e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 361 VLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEyigvmhqAPYLFRTTILNNIR 440
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSE-------VPDSLPLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 441 IGR----------EEASEAEVWAVLEKVGLKEMvnqlpEGLQtmVDEaglrFSGGERHRLALARILLQDTPIVLLDEPTT 510
Cdd:NF040873 80 MGRwarrglwrrlTRDDRAAVDDALERVGLADL-----AGRQ--LGE----LSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 256953159 511 GLDPITEQQLLETFFEALKDK-TVIWITHHLQGVTLMDQVI 550
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGaTVVVVTHDLELVRRADPCV 189
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
360-566 |
1.29e-22 |
|
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: 98.62 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGE-ILLG-NIPTEAfgETMTEYIGVMHQAPYLFR--TTI 435
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTaRVAGyDVVREP--RKVRRSIGIVPQYASVDEdlTGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 436 LNNIRIGR-----EEASEAEVWAVLEKVGLKEMVNQLPEGlqtmvdeaglrFSGGERHRLALARILLQDTPIVLLDEPTT 510
Cdd:TIGR01188 85 ENLEMMGRlyglpKDEAEERAEELLELFELGEAADRPVGT-----------YSGGMRRRLDIAASLIHQPDVLFLDEPTT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 511 GLDPITEQQLLEtFFEALK--DKTVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:TIGR01188 154 GLDPRTRRAIWD-YIRALKeeGVTILLTTHYMEEAdKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
359-557 |
1.84e-22 |
|
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: 95.31 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 359 KKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRP--TSGEILLGNIPTEAFgeTMTEYIGVMHQAPYLFRT-TI 435
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKR--SFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 436 lnnirigREeaseaevwavlekvglkemvnqlpeglqTMVDEAGLR-FSGGERHRLALARILLQDTPIVLLDEPTTGLDP 514
Cdd:cd03213 100 -------RE----------------------------TLMFAAKLRgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 256953159 515 ITEQQLLETFFE-ALKDKTVIWITHHL--QGVTLMDQVIFIEDGQL 557
Cdd:cd03213 145 SSALQVMSLLRRlADTGRTIICSIHQPssEIFELFDKLLLLSQGRV 190
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
358-571 |
2.19e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.85 E-value: 2.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILL------GNIPTEAFGETMTEY----------- 420
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdekNKKKTKEKEKVLEKLviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 --------IGVMHQ-APY-LFRTTILNNIRIG-------REEASEAEVwAVLEKVGLKEmvnqlpeglqTMVDEAGLRFS 483
Cdd:PRK13651 99 kikeirrrVGVVFQfAEYqLFEQTIEKDIIFGpvsmgvsKEEAKKRAA-KYIELVGLDE----------SYLQRSPFELS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 484 GGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD-KTVIWITHHLQGV-TLMDQVIFIEDGQLEMSG 561
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDG 247
|
250
....*....|
gi 256953159 562 TPEELLATNA 571
Cdd:PRK13651 248 DTYDILSDNK 257
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
360-569 |
3.31e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.93 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNI----PTEAFGETMTEyIGVMHQAPYLF-RTT 434
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvndPKVDERLIRQE-AGMVFQQFYLFpHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 435 ILNNIRIG--------REEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLD 506
Cdd:PRK09493 94 ALENVMFGplrvrgasKEEA-EKQARELLAKVGLAERAHHYPSEL-----------SGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 507 EPTTGLDPITEQQLLeTFFEALKDK--TVIWITHHlqgVTLMDQV----IFIEDGQLEMSGTPEELLAT 569
Cdd:PRK09493 162 EPTSALDPELRHEVL-KVMQDLAEEgmTMVIVTHE---IGFAEKVasrlIFIDKGRIAEDGDPQVLIKN 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
323-566 |
3.40e-22 |
|
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: 101.91 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 323 FNELPEGEDDSTEAPVQPNG-TSLSIEHLSFayenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSG 401
Cdd:TIGR01271 406 IGELFEKIKQNNKARKQPNGdDGLFFSNFSL----YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 402 EIllgnipteafgeTMTEYIGVMHQAPYLFRTTILNNIRIGREeASEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLR 481
Cdd:TIGR01271 482 KI------------KHSGRISFSPQTSWIMPGTIKDNIIFGLS-YDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGIT 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 482 FSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLET-FFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMS 560
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFY 628
|
....*.
gi 256953159 561 GTPEEL 566
Cdd:TIGR01271 629 GTFSEL 634
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
354-569 |
3.82e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 101.78 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 354 YENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILlgnipteafGETMTEYIGvmhQAPYLFRT 433
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---------AERSIAYVP---QQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 434 TILNNIRIGREEaSEAEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLD 513
Cdd:PTZ00243 736 TVRGNILFFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 514 P-ITEQQLLETFFEALKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLAT 569
Cdd:PTZ00243 815 AhVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT 871
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
345-577 |
4.27e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 101.26 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEK-KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLI----------------------------RGD 395
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyQGD 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 396 --------------------------LRPTSGEILLGNIPTEAFG-ETMTEYIGVMHQAPYLFRTTILNNIRIGREEASE 448
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNlKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 449 AEVWAVLEKVGLKEMVNQLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEqQLLETFFEAL 528
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE-KLIEKTIVDI 1404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 529 KDK---TVIWITHHLQGVTLMDQVIFIEDGQ-----LEMSGTPEELLATNAHYQKLY 577
Cdd:PTZ00265 1405 KDKadkTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKKY 1461
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
345-568 |
4.33e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG--ETMTEYIG 422
Cdd:PRK13644 2 IRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSklQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 VMHQAP---YLFRtTILNNIRIGREEAS------EAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALA 493
Cdd:PRK13644 81 IVFQNPetqFVGR-TVEEDLAFGPENLClppieiRKRVDRALAEIGLEKYRHRSPKTL-----------SGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 494 RILLQDTPIVLLDEPTTGLDPITEQQLLETFFEA-LKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
345-572 |
5.50e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 97.46 E-value: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLS--FAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEY-- 420
Cdd:COG1135 2 IELENLSktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD-------GVDLTALse 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 ---------IGVMHQAPYLFRT-TILNNI-------RIGREEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfS 483
Cdd:COG1135 75 relraarrkIGMIFQHFNLLSSrTVAENValpleiaGVPKAEI-RKRVAELLELVGLSDKADAYPSQL-----------S 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 484 GGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETffeaLKD------KTVIWITHHLQGV-TLMDQVIFIEDGQ 556
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDL----LKDinrelgLTIVLITHEMDVVrRICDRVAVLENGR 218
|
250
....*....|....*.
gi 256953159 557 LEMSGTPEELLATNAH 572
Cdd:COG1135 219 IVEQGPVLDVFANPQS 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
345-567 |
6.36e-22 |
|
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: 93.75 E-value: 6.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSfaYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRG--DLRPTSGEILLG-----NIPTEafgETM 417
Cdd:cd03217 1 LEIKDLH--VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKgeditDLPPE---ERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 418 TEYIGVMHQAPylfrttilnnIRIgreeaseaevwavlEKVGLKEMVNQLPEGlqtmvdeaglrFSGGERHRLALARILL 497
Cdd:cd03217 76 RLGIFLAFQYP----------PEI--------------PGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 498 QDTPIVLLDEPTTGLDpITEQQLLETFFEALKD--KTVIWITHHLQGVTLM--DQVIFIEDGQLEMSGTPEELL 567
Cdd:cd03217 121 LEPDLAILDEPDSGLD-IDALRLVAEVINKLREegKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKELAL 193
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
345-577 |
6.82e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.71 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEY---- 420
Cdd:COG1137 4 LEAENLVKSY--GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLD-------GEDITHLpmhk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 -----IGVMHQAPYLFRT-TILNNIRigreeaseaevwAVLEKVGL-----KEMVNQLPE--GLQTMVDEAGLRFSGGER 487
Cdd:COG1137 75 rarlgIGYLPQEASIFRKlTVEDNIL------------AVLELRKLskkerEERLEELLEefGITHLRKSKAYSLSGGER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 488 HRLALARILLQDTPIVLLDEPTTGLDPIT--E-QQLLETffeaLKDKTV-IWITHH-----LqGVTlmDQVIFIEDGQLE 558
Cdd:COG1137 143 RRVEIARALATNPKFILLDEPFAGVDPIAvaDiQKIIRH----LKERGIgVLITDHnvretL-GIC--DRAYIISEGKVL 215
|
250
....*....|....*....
gi 256953159 559 MSGTPEELLAtNAHYQKLY 577
Cdd:COG1137 216 AEGTPEEILN-NPLVRKVY 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
344-566 |
7.19e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.97 E-value: 7.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENQ---EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGE----- 415
Cdd:PRK13649 2 GINLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 416 TMTEYIGVMHQAP--YLFRTTILNNIRIG------REEASEAEVWAVLEKVGLKEmvnqlpeglqTMVDEAGLRFSGGER 487
Cdd:PRK13649 82 QIRKKVGLVFQFPesQLFEETVLKDVAFGpqnfgvSQEEAEALAREKLALVGISE----------SLFEKNPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 488 HRLALARILLQDTPIVLLDEPTTGLDPITEQQLLeTFFEALKDK--TVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPE 564
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELM-TLFKKLHQSgmTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPK 230
|
..
gi 256953159 565 EL 566
Cdd:PRK13649 231 DI 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
347-566 |
9.04e-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: 93.97 E-value: 9.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 347 IEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLgnipteaFGETMT-EYIGVMH 425
Cdd:cd03265 3 VENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV-------AGHDVVrEPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 426 QAPYLFRTTILNNIRIGREEAseaEVWAVLEKVG---LKEMVNQLPE--GLQTMVDEAGLRFSGGERHRLALARILLQDT 500
Cdd:cd03265 74 RIGIVFQDLSVDDELTGWENL---YIHARLYGVPgaeRRERIDELLDfvGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 501 PIVLLDEPTTGLDPITEQQLLEtFFEALKDK---TVIWITHHL-QGVTLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWE-YIEKLKEEfgmTILLTTHYMeEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
361-558 |
1.26e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.11 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 361 VLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEIL-----LGNIPTEAFGETMTEYIGVMHQAPYLFRT-T 434
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqpMSKLSSAAKAELRNQKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 435 ILNNIR----IGREEASEAEVWA--VLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDEP 508
Cdd:PRK11629 104 ALENVAmpllIGKKKPAEINSRAleMLAAVGLEHRANHRPSEL-----------SGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 509 TTGLDpiteQQLLETFFEALKDKTV------IWITHHLQGVTLMDQVIFIEDGQLE 558
Cdd:PRK11629 173 TGNLD----ARNADSIFQLLGELNRlqgtafLVVTHDLQLAKRMSRQLEMRDGRLT 224
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
333-574 |
2.11e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 333 STEAPVQPNGTSLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKST-LASLIRGDLRPT----SGEILLGN 407
Cdd:PRK14271 10 SGAADVDAAAPAMAAVNLTLGFAG--KTVLDQVSMGFPARAVTSLMGPTGSGKTTfLRTLNRMNDKVSgyrySGDVLLGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 408 IPTEAFGETMT--EYIGVMHQAPYLFRTTILNNIRIG--------REEAsEAEVWAVLEKVGLKEMVnqlpeglQTMVDE 477
Cdd:PRK14271 88 RSIFNYRDVLEfrRRVGMLFQRPNPFPMSIMDNVLAGvrahklvpRKEF-RGVAQARLTEVGLWDAV-------KDRLSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 478 AGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQlLETFFEALKDK-TVIWITHHL-QGVTLMDQVIFIEDG 555
Cdd:PRK14271 160 SPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK-IEEFIRSLADRlTVIIVTHNLaQAARISDRAALFFDG 238
|
250
....*....|....*....
gi 256953159 556 QLEMSGTPEELLATNAHYQ 574
Cdd:PRK14271 239 RLVEEGPTEQLFSSPKHAE 257
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
345-564 |
2.24e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.59 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRG--DLRPTSGEILLGnipteafGETMTEY-- 420
Cdd:COG0396 1 LEIKNLHVSVE--GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLD-------GEDILELsp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 -------IGVMHQAP---------YLFRTtILNNIRIGREEASE--AEVWAVLEKVGL-KEM----VNqlpEGlqtmvde 477
Cdd:COG0396 72 deraragIFLAFQYPveipgvsvsNFLRT-ALNARRGEELSAREflKLLKEKMKELGLdEDFldryVN---EG------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 478 aglrFSGGERHRLALARILLQDTPIVLLDEPTTGLDpiteqqlLETF------FEAL--KDKTVIWITHH---LQGVTLm 546
Cdd:COG0396 141 ----FSGGEKKRNEILQMLLLEPKLAILDETDSGLD-------IDALrivaegVNKLrsPDRGILIITHYqriLDYIKP- 208
|
250
....*....|....*...
gi 256953159 547 DQVIFIEDGQLEMSGTPE 564
Cdd:COG0396 209 DFVHVLVDGRIVKSGGKE 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
344-566 |
6.83e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.25 E-value: 6.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPteaFGETMTEYIG- 422
Cdd:COG4152 1 MLELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEP---LDPEDRRRIGy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 ------------VMHQAPYLFRttiLNNirIGREEA-SEAEVWavLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHR 489
Cdd:COG4152 76 lpeerglypkmkVGEQLVYLAR---LKG--LSKAEAkRRADEW--LERLGLGDRANKKVEEL-----------SKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 490 LALARILLQDTPIVLLDEPTTGLDPITeQQLLETFFEALKDK--TVIWITHHLQGVTLM-DQVIFIEDGQLEMSGTPEEL 566
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVN-VELLKDVIRELAAKgtTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
345-557 |
1.13e-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: 89.02 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQekKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGEtmteyigvm 424
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-------GK--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 hqaPYLFRTTIlnnirigreEASEAEVwavlekvglkEMVNQLpeglqtmvdeaglrfSGGERHRLALARILLQDTPIVL 504
Cdd:cd03216 63 ---EVSFASPR---------DARRAGI----------AMVYQL---------------SVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 505 LDEPTTGLDPITEQQLLEtFFEALKD--KTVIWITHHLQGV-TLMDQVIFIEDGQL 557
Cdd:cd03216 106 LDEPTAALTPAEVERLFK-VIRRLRAqgVAVIFISHRLDEVfEIADRVTVLRDGRV 160
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
327-572 |
1.97e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 327 PEGEDDSTEAPVQPngtSLSIEHLSFAYENQ---------EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLA-SLIRgdL 396
Cdd:PRK15134 261 PSGDPVPLPEPASP---LLDVEQLQVAFPIRkgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGlALLR--L 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 397 RPTSGEILLGNIPTEAFG-ETMTEY---IGVMHQAPYLFRTTILNNIRIGRE-----------EASEAEVWAVLEKVGLK 461
Cdd:PRK15134 336 INSQGEIWFDGQPLHNLNrRQLLPVrhrIQVVFQDPNSSLNPRLNVLQIIEEglrvhqptlsaAQREQQVIAVMEEVGLD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 462 emvnqlPEGLQTMVDEaglrFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLeTFFEALKDK---TVIWITH 538
Cdd:PRK15134 416 ------PETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL-ALLKSLQQKhqlAYLFISH 484
|
250 260 270
....*....|....*....|....*....|....*
gi 256953159 539 HLQGV-TLMDQVIFIEDGQLEMSGTPEELLATNAH 572
Cdd:PRK15134 485 DLHVVrALCHQVIVLRQGEVVEQGDCERVFAAPQQ 519
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
345-546 |
2.65e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.53 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMteyiGVM 424
Cdd:PRK11248 2 LQISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFR-TTILNNIRIGRE------EASEAEVWAVLEKVGLkemvnqlpeglqtmvDEAGLRF----SGGERHRLALA 493
Cdd:PRK11248 76 FQNEGLLPwRNVQDNVAFGLQlagvekMQRLEIAHQMLKKVGL---------------EGAEKRYiwqlSGGQRQRVGIA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 494 RILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHLQGVTLM 546
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITHDIEEAVFM 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
355-539 |
3.88e-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: 88.70 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 355 ENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTE---YIGvmHQAPYLF 431
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARgllYLG--HAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 432 RTTILNNIRIGREEASEAEVWAVLEKVGLKemvnqlpeGLQtmvDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTG 511
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQVEEALARVGLN--------GFE---DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*....
gi 256953159 512 LDPITEQQLLETFFEAL-KDKTVIWITHH 539
Cdd:cd03231 156 LDKAGVARFAEAMAGHCaRGGMVVLTTHQ 184
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
343-572 |
4.04e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.19 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEA---FGE---- 415
Cdd:PRK11264 2 SAIEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSQqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 416 --TMTEYIGVMHQAPYLF-RTTILNNIRIG--------REEAsEAEVWAVLEKVGLKEMVNQLPEglqtmvdeaglRFSG 484
Cdd:PRK11264 80 irQLRQHVGFVFQNFNLFpHRTVLENIIEGpvivkgepKEEA-TARARELLAKVGLAGKETSYPR-----------RLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 485 GERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITHHLQ-GVTLMDQVIFIEDGQLEMSGT 562
Cdd:PRK11264 148 GQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGP 227
|
250
....*....|
gi 256953159 563 PEELLATNAH 572
Cdd:PRK11264 228 AKALFADPQQ 237
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-567 |
4.62e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.82 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 321 RRFNELPEGEDDST----EAPVQPNGTSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDL 396
Cdd:PRK13536 12 RRLELSPIERKHQGiseaKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 397 RPTSGEILLGNIPTEAFGETMTEYIGVMHQAPYLFRT-TILNNIRI-GR-----EEASEAEVWAVLEKVGLKEMVNqlpe 469
Cdd:PRK13536 92 SPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEfTVRENLLVfGRyfgmsTREIEAVIPSLLEFARLESKAD---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 470 glqTMVDEaglrFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEAL-KDKTVIWITHHLQGVT-LMD 547
Cdd:PRK13536 168 ---ARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAErLCD 240
|
250 260
....*....|....*....|
gi 256953159 548 QVIFIEDGQLEMSGTPEELL 567
Cdd:PRK13536 241 RLCVLEAGRKIAEGRPHALI 260
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
343-572 |
4.82e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.23 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLS--FAYEN-----QEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEaFGE 415
Cdd:PRK15112 3 TLLEVRNLSktFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 416 T--MTEYIGVMHQAPylfrTTILN-NIRIGR-------------EEASEAEVWAVLEKVGL-KEMVNQLPEGLQTmvdea 478
Cdd:PRK15112 82 YsyRSQRIRMIFQDP----STSLNpRQRISQildfplrlntdlePEQREKQIIETLRQVGLlPDHASYYPHMLAP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 479 glrfsgGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKDK---TVIWITHHLqGVT--LMDQVIFIE 553
Cdd:PRK15112 153 ------GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLE-LQEKqgiSYIYVTQHL-GMMkhISDQVLVMH 224
|
250
....*....|....*....
gi 256953159 554 DGQLEMSGTPEELLATNAH 572
Cdd:PRK15112 225 QGEVVERGSTADVLASPLH 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
360-572 |
5.97e-20 |
|
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: 93.21 E-value: 5.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLA-SLIRgdLRPTSGEILLGNIPTEAFGET-MTEY---IGVMHQAPY--LF- 431
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGlALLR--LIPSEGEIRFDGQDLDGLSRRaLRPLrrrMQVVFQDPFgsLSp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 432 RTTI---------LNNIRIGREEaSEAEVWAVLEKVGLK-EMVNQLP-EglqtmvdeaglrFSGGERHRLALARILLQDT 500
Cdd:COG4172 378 RMTVgqiiaeglrVHGPGLSAAE-RRARVAEALEEVGLDpAARHRYPhE------------FSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 501 PIVLLDEPTTGLDPITEQQLLEtFFEALKDK---TVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPEELLATNAH 572
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQILD-LLRDLQREhglAYLFISHDLAVVrALAHRVMVMKDGKVVEQGPTEQVFDAPQH 519
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
345-570 |
7.28e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.77 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQ-EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILL-GNIPTEAFGETMTEYIG 422
Cdd:PRK13642 5 LEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 VMHQAP--YLFRTTILNNIRIGREEaseaevwavlEKVGLKEMVNQLPEGLQT--MVD---EAGLRFSGGERHRLALARI 495
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMEN----------QGIPREEMIKRVDEALLAvnMLDfktREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 496 LLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKDK---TVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPEELLATN 570
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
345-557 |
9.45e-20 |
|
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: 89.48 E-value: 9.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEN-------QEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIP-TEAFGET 416
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDlYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 MTEY---IGVMHQ-APYLF--RTTI-------LNNIRIGREEASEAEVWAVLEKVGLK-EMVNQLPEglqtmvdeaglRF 482
Cdd:TIGR02769 83 RRAFrrdVQLVFQdSPSAVnpRMTVrqiigepLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPR-----------QL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 483 SGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKDK---TVIWITHHLQGV-TLMDQVIFIEDGQL 557
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILE-LLRKLQQAfgtAYLFITHDLRLVqSFCQRVAVMDKGQI 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-572 |
9.60e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 9.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRG--DLRP---TSGEILLGNipTEAFGETMTE 419
Cdd:PRK14247 4 IEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEVYLDG--QDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 Y---IGVMHQAPYLFRT-TILNNIRIG---------REEASEAEVWAvLEKVglkemvnQLPEGLQTMVDEAGLRFSGGE 486
Cdd:PRK14247 80 LrrrVQMVFQIPNPIPNlSIFENVALGlklnrlvksKKELQERVRWA-LEKA-------QLWDEVKDRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 487 RHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHH-LQGVTLMDQVIFIEDGQLEMSGTPEE 565
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFpQQAARISDYVAFLYKGQIVEWGPTRE 231
|
....*..
gi 256953159 566 LLATNAH 572
Cdd:PRK14247 232 VFTNPRH 238
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
358-568 |
1.29e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.99 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTE--------YIGVMHQAPY 429
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID-------GKDVTKlpeykrakYIGRVFQDPM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 430 L---FRTTILNN--------------IRIGREEASEaevwavlekvgLKEMVNQLPEGLQT-MVDEAGLrFSGGERHRLA 491
Cdd:COG1101 91 MgtaPSMTIEENlalayrrgkrrglrRGLTKKRREL-----------FRELLATLGLGLENrLDTKVGL-LSGGQRQALS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHL-QGVTLMDQVIFIEDGQ--LEMSG----- 561
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMeQALDYGNRLIMMHEGRiiLDVSGeekkk 238
|
....*...
gi 256953159 562 -TPEELLA 568
Cdd:COG1101 239 lTVEDLLE 246
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
362-572 |
1.50e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.25 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEIL-----LGNIPTEAFGETMTEYIGVMHQAPYLF-RTTI 435
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdIAKISDAELREVRRKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 436 LNNIRIGRE------EASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDEPT 509
Cdd:PRK10070 124 LDNTAFGMElaginaEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 510 TGLDPI--TEQQLLETFFEALKDKTVIWITHHL-QGVTLMDQVIFIEDGQLEMSGTPEELLATNAH 572
Cdd:PRK10070 193 SALDPLirTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
338-557 |
2.15e-19 |
|
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: 87.39 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 338 VQPNGTSLSIEHLsFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEI-LLGNIPTEAFGET 416
Cdd:cd03267 14 SKEPGLIGSLKSL-FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRKKF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 MTEYIGVMHQapylfRTTILNNIRIGREEASEAEVWAvLEKVGLKEMVNQLPEGLQT--MVDEAGLRFSGGERHRLALAR 494
Cdd:cd03267 93 LRRIGVVFGQ-----KTQLWWDLPVIDSFYLLAAIYD-LPPARFKKRLDELSELLDLeeLLDTPVRQLSLGQRMRAEIAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 495 ILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVT-LMDQVIFIEDGQL 557
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEaLARRVLVIDKGRL 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
358-538 |
2.53e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILL--GNIPTEAFGETMTeYIGvmHQ---APYLfr 432
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdgGDIDDPDVAEACH-YLG--HRnamKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 433 tTILNNIRIGRE--EASEAEVWAVLEKVGLKemvnqlpeglqtmvDEAGLRF---SGGERHRLALARILLQDTPIVLLDE 507
Cdd:PRK13539 89 -TVAENLEFWAAflGGEELDIAAALEAVGLA--------------PLAHLPFgylSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 256953159 508 PTTGLDPITEQQLLETFFEALK-DKTVIWITH 538
Cdd:PRK13539 154 PTAALDAAAVALFAELIRAHLAqGGIVIAATH 185
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
352-567 |
2.80e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.65 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 352 FAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTL----ASLIRGDLRpTSGEILLGNIPTEAfgETMTEYIGVMHQA 427
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLmnalAFRSPKGVK-GSGSVLLNGMPIDA--KEMRAISAYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 428 PYLFRT-------TILNNIRIGREEASE---AEVWAVLEKVGLKEMVNQLpegLQTMVDEAGLrfSGGERHRLALARILL 497
Cdd:TIGR00955 108 DLFIPTltvrehlMFQAHLRMPRRVTKKekrERVDEVLQALGLRKCANTR---IGVPGRVKGL--SGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 498 QDTPIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIwITHHLQGVTLM---DQVIFIEDGQLEMSGTPEELL 567
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTII-CTIHQPSSELFelfDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
345-572 |
3.14e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 3.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQ--EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLA-SLIRgdLRPT------SGEILL-GNIPTEAFG 414
Cdd:PRK15134 6 LAIENLSVAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILR--LLPSppvvypSGDIRFhGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 415 ETMT----EYIGVMHQAPyLFRTTILNNI-----------RIGREEASEAEVWAVLEKVGLKEMVNQL---PEGLqtmvd 476
Cdd:PRK15134 84 QTLRgvrgNKIAMIFQEP-MVSLNPLHTLekqlyevlslhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQL----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 477 eaglrfSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLK---DKTVIWITHHLQGV-TLMDQVIFI 552
Cdd:PRK15134 158 ------SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRE-LQqelNMGLLFITHNLSIVrKLADRVAVM 230
|
250 260
....*....|....*....|
gi 256953159 553 EDGQLEMSGTPEELLATNAH 572
Cdd:PRK15134 231 QNGRCVEQNRAATLFSAPTH 250
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
358-566 |
4.97e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.13 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG--NIPTEAFGE--TMTEYIGVMHQAPYLFR- 432
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDgeNIPAMSRSRlyTVRKRMSMLFQSGALFTd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 433 TTILNNIRIGREEASE-------AEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLL 505
Cdd:PRK11831 99 MNVFDNVAYPLREHTQlpapllhSTVMMKLEAVGLRGAAKLMPSEL-----------SGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 506 DEPTTGLDPITEQQLLETFFE---ALkDKTVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISElnsAL-GVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
345-539 |
6.49e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.24 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFayENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPT----EAFGETMTeY 420
Cdd:PRK13538 2 LEARNLAC--ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqrDEYHQDLL-Y 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 IGvmHQA---PYLfrtTILNNIRI---GREEASEAEVWAVLEKVGLK--EMV--NQLpeglqtmvdeaglrfSGGERHRL 490
Cdd:PRK13538 79 LG--HQPgikTEL---TALENLRFyqrLHGPGDDEALWEALAQVGLAgfEDVpvRQL---------------SAGQQRRV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 256953159 491 ALARILLQDTPIVLLDEPTTGLDpiteQQ---LLETFFEALKDK--TVIWITHH 539
Cdd:PRK13538 139 ALARLWLTRAPLWILDEPFTAID----KQgvaRLEALLAQHAEQggMVILTTHQ 188
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
359-571 |
8.52e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.01 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 359 KKVLNDLSL----TIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG-----------NIPTEafgetmTEYIGV 423
Cdd:PRK11144 7 KQQLGDLCLtvnlTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekgiCLPPE------KRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYLF-RTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPI 502
Cdd:PRK11144 81 VFQDARLFpHYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSL-----------SGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 503 VLLDEPTTGLDPITEQQLLeTFFEALKDKT---VIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELLATNA 571
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELL-PYLERLAREInipILYVSHSLDEILrLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-572 |
9.37e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.05 E-value: 9.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTL------------ASLIRGDLRPTSGEILLGNI-PT 410
Cdd:PRK14267 4 AIETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLlrtfnrllelneEARVEGEVRLFGRNIYSPDVdPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 411 EAFGEtmteyIGVMHQAPYLF-RTTILNNIRIG---------REEASEAEVWAvLEKVGL----KEMVNQLPEGLqtmvd 476
Cdd:PRK14267 82 EVRRE-----VGMVFQYPNPFpHLTIYDNVAIGvklnglvksKKELDERVEWA-LKKAALwdevKDRLNDYPSNL----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 477 eaglrfSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHH-LQGVTLMDQVIFIEDG 555
Cdd:PRK14267 151 ------SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLG 224
|
250
....*....|....*..
gi 256953159 556 QLEMSGTPEELLATNAH 572
Cdd:PRK14267 225 KLIEVGPTRKVFENPEH 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
347-572 |
1.02e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.55 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 347 IEHLSFAYENQEKKV--LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEY---- 420
Cdd:PRK11153 4 LKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD-------GQDLTALseke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 -------IGVMHQAPYLF-RTTILNNI-------RIGREEaSEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGG 485
Cdd:PRK11153 77 lrkarrqIGMIFQHFNLLsSRTVFDNValplelaGTPKAE-IKARVTELLELVGLSDKADRYPAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 486 ERHRLALARILLQDtPIVLL-DEPTTGLDPITEQQLLETffeaLKD------KTVIWITHHLQGV-TLMDQVIFIEDGQL 557
Cdd:PRK11153 145 QKQRVAIARALASN-PKVLLcDEATSALDPATTRSILEL----LKDinrelgLTIVLITHEMDVVkRICDRVAVIDAGRL 219
|
250
....*....|....*
gi 256953159 558 EMSGTPEELLATNAH 572
Cdd:PRK11153 220 VEQGTVSEVFSHPKH 234
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
346-580 |
1.60e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 85.52 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 346 SIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIP-TEAFGETMTEYIGVM 424
Cdd:COG4604 3 EIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLfrttilnNIRI--------GR--------EEASEAEVWAVLEKVGLKEMVNQLpeglqtmVDEaglrFSGGERH 488
Cdd:COG4604 81 RQENHI-------NSRLtvrelvafGRfpyskgrlTAEDREIIDEAIAYLDLEDLADRY-------LDE----LSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 489 RLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHL-QGVTLMDQVIFIEDGQLEMSGTPEE 565
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLHDInFASCYADHIVAMKDGRVVAQGTPEE 222
|
250
....*....|....*
gi 256953159 566 LLaTNAHYQKLYRID 580
Cdd:COG4604 223 II-TPEVLSDIYDTD 236
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
345-568 |
1.94e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 85.24 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLaslirgdLR-------PTSGEILLGnipteafGETM 417
Cdd:COG4598 9 LEVRDLHKSFGDLE--VLKGVSLTARKGDVISIIGSSGSGKSTF-------LRcinlletPDSGEIRVG-------GEEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 418 TeyigvMHQAPYL------------FRT---------------TILNNI--------RIGREEASE-AEvwAVLEKVGLK 461
Cdd:COG4598 73 R-----LKPDRDGelvpadrrqlqrIRTrlgmvfqsfnlwshmTVLENVieapvhvlGRPKAEAIErAE--ALLAKVGLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 462 EMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDEPTTGLDPiteqqllETFFEALK--------DKTV 533
Cdd:COG4598 146 DKRDAYPAHL-----------SGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEVLKvmrdlaeeGRTM 207
|
250 260 270
....*....|....*....|....*....|....*...
gi 256953159 534 IWITHHLQ---GVTlmDQVIFIEDGQLEMSGTPEELLA 568
Cdd:COG4598 208 LVVTHEMGfarDVS--SHVVFLHQGRIEEQGPPAEVFG 243
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
347-567 |
2.93e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.17 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 347 IEHLSFAYENqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEI-LLGNIPTEAFGETMTEYIGVMH 425
Cdd:PRK13647 7 VEDLHFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 426 QAP--YLFRTTILN-------NIRIGREEASEaEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARIL 496
Cdd:PRK13647 86 QDPddQVFSSTVWDdvafgpvNMGLDKDEVER-RVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 497 LQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD-KTVIWITHHLQ-GVTLMDQVIFIEDGQLEMSGTPEELL 567
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
345-556 |
4.37e-18 |
|
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: 83.64 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLS--FAYENQEKK---VLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLgnipteAFGETMTE 419
Cdd:COG4778 5 LEVENLSktFTLHLQGGKrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV------RHDGGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 yigvMHQAP-----YLFRTTI------LNNI-RIG---------------REEAsEAEVWAVLEKVGLKEMVNQLPEGlq 472
Cdd:COG4778 79 ----LAQASpreilALRRRTIgyvsqfLRVIpRVSaldvvaepllergvdREEA-RARARELLARLNLPERLWDLPPA-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 473 TmvdeaglrFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKDK--TVIWITHHLQGV-TLMDQV 549
Cdd:COG4778 152 T--------FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVE-LIEEAKARgtAIIGIFHDEEVReAVADRV 222
|
....*..
gi 256953159 550 IFIEDGQ 556
Cdd:COG4778 223 VDVTPFS 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
335-583 |
5.31e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.07 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 335 EAPVQPnGTSLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG 414
Cdd:PRK10575 3 EYTNHS-DTTFALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 415 ETM--TEYIGVMHQAPYLFRTTILNNIRIGR----------EEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrf 482
Cdd:PRK10575 80 SKAfaRKVAYLPQQLPAAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSL----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 483 SGGERHRLALARILLQDTPIVLLDEPTTGLDpITEQQLLETFFEALKDK---TVIWITHHLQ-GVTLMDQVIFIEDGQLE 558
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALD-IAHQVDVLALVHRLSQErglTVIAVLHDINmAARYCDYLVALRGGEMI 227
|
250 260
....*....|....*....|....*
gi 256953159 559 MSGTPEELLATNAhYQKLYRIDRGI 583
Cdd:PRK10575 228 AQGTPAELMRGET-LEQIYGIPMGI 251
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
345-554 |
5.61e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.97 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAY-------ENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAF-GET 416
Cdd:PRK10419 4 LNVSGLSHHYahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 MTEYIG----VMHQAPYLF--RTTILNNIRIG-------REEASEAEVWAVLEKVGLK-EMVNQLPEGLqtmvdeaglrf 482
Cdd:PRK10419 84 RKAFRRdiqmVFQDSISAVnpRKTVREIIREPlrhllslDKAERLARASEMLRAVDLDdSVLDKRPPQL----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 483 SGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKDKT---VIWITHHL-------QGVTLMDQVIFI 552
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR-LLKKLQQQFgtaCLFITHDLrlverfcQRVMVMDNGQIV 231
|
..
gi 256953159 553 ED 554
Cdd:PRK10419 232 ET 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
362-540 |
6.39e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTE--------AFGetmteyIGVMHQAPYLFRT 433
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdaiALG------IGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 434 -TILNNIRIGRE---------EASEAEVWAVLEKVGLK----EMVNQLPeglqtmVdeaglrfsgGERHRLALARILLQD 499
Cdd:COG3845 95 lTVAENIVLGLEptkggrldrKAARARIRELSERYGLDvdpdAKVEDLS------V---------GEQQRVEILKALYRG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 256953159 500 TPIVLLDEPTTGLDPiteqQLLETFFEALKD-----KTVIWITHHL 540
Cdd:COG3845 160 ARILILDEPTAVLTP----QEADELFEILRRlaaegKSIIFITHKL 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
340-557 |
6.52e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.90 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 340 PNGTSLSIEHL--SFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEI-LLG----NIPTEA 412
Cdd:PRK10584 2 PAENIVEVHHLkkSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVsLVGqplhQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 413 FGETMTEYIGVMHQAPYLFRT-TILNNI------RIGREEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGG 485
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFMLIPTlNALENVelpallRGESSRQSRNGAKALLEQLGLGKRLDHLPAQL-----------SGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 486 ERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHLQGVTLMDQVIFIEDGQL 557
Cdd:PRK10584 151 EQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
353-539 |
8.17e-18 |
|
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: 82.02 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 353 AYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTE---YIGvmHQAPY 429
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEnilYLG--HLPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 430 LFRTTILNNIRIGREEASEAE--VWAVLEKVGLKEM----VNQLpeglqtmvdeaglrfSGGERHRLALARILLQDTPIV 503
Cdd:TIGR01189 85 KPELSALENLHFWAAIHGGAQrtIEDALAAVGLTGFedlpAAQL---------------SAGQQRRLALARLWLSRRPLW 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 256953159 504 LLDEPTTGLDPiTEQQLLETFFEA--LKDKTVIWITHH 539
Cdd:TIGR01189 150 ILDEPTTALDK-AGVALLAGLLRAhlARGGIVLLTTHQ 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
360-569 |
1.32e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPT--------EAFGetmteyIGVMHQ----A 427
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsprdaQAAG------IAIIHQelnlV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 428 PYLfrtTILNNIRIGREEAS-----------EAEvwAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARIL 496
Cdd:COG1129 92 PNL---SVAENIFLGREPRRgglidwramrrRAR--ELLARLGLDIDPDTPVGDL-----------SVAQQQLVEIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 497 LQDTPIVLLDEPTTGLDPiTEQQLLetfFE---ALKDK--TVIWITHHLQGV-TLMDQVIFIEDGQL----EMSGTPEEL 566
Cdd:COG1129 156 SRDARVLILDEPTASLTE-REVERL---FRiirRLKAQgvAIIYISHRLDEVfEIADRVTVLRDGRLvgtgPVAELTEDE 231
|
...
gi 256953159 567 LAT 569
Cdd:COG1129 232 LVR 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
343-588 |
1.56e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTL----ASLIRGDLRPTSGEILLGNIPTEAfGETMT 418
Cdd:PRK09984 3 TIIRVEKLAKTF--NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITGDKSAGSHIELLGRTVQRE-GRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 EYIGVMHQAPYLF-------RTTILNNIRIGR--------------EEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvde 477
Cdd:PRK09984 80 DIRKSRANTGYIFqqfnlvnRLSVLENVLIGAlgstpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTL------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 478 aglrfSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQ-GVTLMDQVIFIED 554
Cdd:PRK09984 154 -----SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQ 228
|
250 260 270
....*....|....*....|....*....|....
gi 256953159 555 GQLEMSGTPEELlaTNAHYQKLYridRGISSFEE 588
Cdd:PRK09984 229 GHVFYDGSSQQF--DNERFDHLY---RSINRVEE 257
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
298-571 |
1.58e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 298 PLIDAFAPLPA--AAQettIYKDSIRRFNeLPEGEDDSTEAPVQPNGTSLSIEHLSFAYENQEKKVlNDLSLTIPEKQKL 375
Cdd:PRK10522 278 PLLSAVGALPTllSAQ---VAFNKLNKLA-LAPYKAEFPRPQAFPDWQTLELRNVTFAYQDNGFSV-GPINLTIKRGELL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 376 AILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAfgETMTEY---IGVMHQAPYLFrTTILNNiriGREEASEAEVW 452
Cdd:PRK10522 353 FLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA--EQPEDYrklFSAVFTDFHLF-DQLLGP---EGKPANPALVE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 453 AVLEKVGLKEMVnqlpeglqTMVDE--AGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPiteqQLLETFFEAL-- 528
Cdd:PRK10522 427 KWLERLKMAHKL--------ELEDGriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDP----HFRREFYQVLlp 494
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 256953159 529 ----KDKTVIWITHHLQGVTLMDQVIFIEDGQL-EMSGTPEELLATNA 571
Cdd:PRK10522 495 llqeMGKTIFAISHDDHYFIHADRLLEMRNGQLsELTGEERDAASRDA 542
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-572 |
1.85e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.39 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENQekKVLNDLSLTIPEKQKLAILGRSGSGKST-LASLIRgdLRPTSGEILL-GNIptEAFGETMTE-- 419
Cdd:PRK14258 7 AIKVNNLSFYYDTQ--KILEGVSMEIYQSKVTAIIGPSGCGKSTfLKCLNR--MNELESEVRVeGRV--EFFNQNIYErr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 --------YIGVMHQAPYLFRTTILNNIRIGREEAS---EAEVWAVLEKvGLKEMvnQLPEGLQTMVDEAGLRFSGGERH 488
Cdd:PRK14258 81 vnlnrlrrQVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpKLEIDDIVES-ALKDA--DLWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 489 RLALARILLQDTPIVLLDEPTTGLDPITEQQlLETFFEALK---DKTVIWITHHLQGVT-LMDQVIFIED-----GQLEM 559
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMK-VESLIQSLRlrsELTMVIVSHNLHQVSrLSDFTAFFKGnenriGQLVE 236
|
250
....*....|...
gi 256953159 560 SGTPEELLaTNAH 572
Cdd:PRK14258 237 FGLTKKIF-NSPH 248
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
354-550 |
1.89e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.68 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 354 YENQEKKVLNDLSLTI-PEKQKLaILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYIGVMHQAPYLF 431
Cdd:PRK10247 15 YLAGDAKILNNISFSLrAGEFKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 432 RTTILNNI----RIGREEASEAEVWAVLEKVGLKEmvnqlpeglqTMVDEAGLRFSGGERHRLALARIlLQDTP-IVLLD 506
Cdd:PRK10247 94 GDTVYDNLifpwQIRNQQPDPAIFLDDLERFALPD----------TILTKNIAELSGGEKQRISLIRN-LQFMPkVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 256953159 507 EPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVTLMDQVI 550
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVI 208
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
343-577 |
2.36e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.34 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG-ETMTEYI 421
Cdd:PRK10253 6 ARLRGEQLTLGYGK--YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAsKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQ-APYLFRTTILNNIRIGR----------EEASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRL 490
Cdd:PRK10253 84 GLLAQnATTPGDITVQELVARGRyphqplftrwRKEDEEAVTKAMQATGITHLADQSVDTL-----------SGGQRQRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 491 ALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHL-QGVTLMDQVIFIEDGQLEMSGTPEELL 567
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
250
....*....|
gi 256953159 568 aTNAHYQKLY 577
Cdd:PRK10253 233 -TAELIERIY 241
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
361-566 |
3.80e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 83.23 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 361 VLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEY------IGVMHQAPYLF-RT 433
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID-------GEDVTHRsiqqrdICMVFQSYALFpHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 434 TILNNIRIGREeaseaevwavLEKVGLKEMVNQLPEGLQtMVDEAGL--RF----SGGERHRLALARILLQDTPIVLLDE 507
Cdd:PRK11432 94 SLGENVGYGLK----------MLGVPKEERKQRVKEALE-LVDLAGFedRYvdqiSGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256953159 508 PTTGLDPITEQQLLETFFEALK--DKTVIWITH-HLQGVTLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
345-566 |
3.86e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.35 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEY---- 420
Cdd:PRK11607 20 LEIRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD-------GVDLSHVppyq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 --IGVMHQAPYLF-RTTILNNIRIG--REEASEAEVWA----VLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLA 491
Cdd:PRK11607 91 rpINMMFQSYALFpHMTVEQNIAFGlkQDKLPKAEIASrvneMLGLVHMQEFAKRKPHQL-----------SGGQRQRVA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALK--DKTVIWITH-HLQGVTLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
345-576 |
4.13e-17 |
|
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: 84.35 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLS--FAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKS-TLASLIR---GDLRPTSGEILLGNIPTEAFGE-TM 417
Cdd:COG4172 7 LSVEDLSvaFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRllpDPAAHPSGSILFDGQDLLGLSErEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 418 TEY----IGVMHQAPylfrTTILNNI-RIGR-------------EEASEAEVWAVLEKVGLKE---MVNQLPEglqtmvd 476
Cdd:COG4172 87 RRIrgnrIAMIFQEP----MTSLNPLhTIGKqiaevlrlhrglsGAAARARALELLERVGIPDperRLDAYPH------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 477 eaglRFSGGERHRLALARILLQDtPIVLL-DEPTTGLDPITEQQLLETFFEaLKDKT---VIWITHHLQGVTLM-DQVIF 551
Cdd:COG4172 156 ----QLSGGQRQRVMIAMALANE-PDLLIaDEPTTALDVTVQAQILDLLKD-LQRELgmaLLLITHDLGVVRRFaDRVAV 229
|
250 260
....*....|....*....|....*..
gi 256953159 552 IEDGQLEMSGTPEELLATNAH-Y-QKL 576
Cdd:COG4172 230 MRQGEIVEQGPTAELFAAPQHpYtRKL 256
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
344-577 |
4.47e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG--NIPTEAFGETMTEYI 421
Cdd:PRK10895 3 TLTAKNLAKAY--KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAPYLFRT-TILNNIrigreeASEAEVWAVLEKVGLKEMVNQLPE--GLQTMVDEAGLRFSGGERHRLALARILLQ 498
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNL------MAVLQIRDDLSAEQREDRANELMEefHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 499 DTPIVLLDEPTTGLDPITEQQlLETFFEALKDKTV-IWITHHLQGVTL--MDQVIFIEDGQLEMSGTPEELLAtNAHYQK 575
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVID-IKRIIEHLRDSGLgVLITDHNVRETLavCERAYIVSQGHLIAHGTPTEILQ-DEHVKR 232
|
..
gi 256953159 576 LY 577
Cdd:PRK10895 233 VY 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
358-569 |
5.48e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.16 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGVMHQAPYL---FrtT 434
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDNLdpdF--T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 435 ILNNIRI-GReeaseaevWAVLEKVGLKEMVNQLPE--GLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTG 511
Cdd:PRK13537 97 VRENLLVfGR--------YFGLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 512 LDPITEQQLLETFFEAL-KDKTVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELLAT 569
Cdd:PRK13537 169 LDPQARHLMWERLRSLLaRGKTILLTTHFMEEAErLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
345-571 |
8.30e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 79.92 E-value: 8.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG--NIPTEAFGETMTEYIG 422
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 VMHQAPYLF-RTTILNNIRIGREEASEAEVWAVLEKVglkemVNQLPEGLQTMVDEAGlRFSGGERHRLALARILLQDTP 501
Cdd:PRK11614 84 IVPEGRRVFsRMTVEENLAMGGFFAERDQFQERIKWV-----YELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256953159 502 IVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHH--LQGVTLMDQVIFIEDGQLEMSGTPEELLATNA 571
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQnaNQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
345-565 |
9.96e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.30 E-value: 9.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG-----NIPTEAfgetmtE 419
Cdd:PRK09452 15 VELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqditHVPAEN------R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 420 YIGVMHQAPYLF-RTTILNNIRIG--REEASEAE----VWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLAL 492
Cdd:PRK09452 87 HVNTVFQSYALFpHMTVFENVAFGlrMQKTPAAEitprVMEALRMVQLEEFAQRKPHQL-----------SGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 493 ARILLQDTPIVLLDEPTTGLDPITEQQL-LEtfFEALKDK---TVIWITH-HLQGVTLMDQVIFIEDGQLEMSGTPEE 565
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMqNE--LKALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
362-555 |
1.27e-16 |
|
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: 79.43 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILL-GNIPTEAFGETMteyigVMHQAPYLFR-TTILNNI 439
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 440 RIG----REEASEAEVWAVLEK----VGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDEPTTG 511
Cdd:TIGR01184 76 ALAvdrvLPDLSKSERRAIVEEhialVGLTEAADKRPGQL-----------SGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 256953159 512 LDPITEQQLLETFFEALKDK--TVIWITHHL-QGVTLMDQVIFIEDG 555
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
341-541 |
1.39e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 341 NGTS--LSIEHLSFAYENQekKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIR--GDLRPT---SGEILLG--NI--- 408
Cdd:PRK14243 5 NGTEtvLRTENLNVYYGSF--LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlNDLIPGfrvEGKVTFHgkNLyap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 409 ---PTEafgetMTEYIGVMHQAPYLFRTTILNNIRIG-REEASEAEVWAVLEKvGLKEMVnqLPEGLQTMVDEAGLRFSG 484
Cdd:PRK14243 83 dvdPVE-----VRRRIGMVFQKPNPFPKSIYDNIAYGaRINGYKGDMDELVER-SLRQAA--LWDEVKDKLKQSGLSLSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 485 GERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQ 541
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
344-544 |
2.68e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.16 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENQEKkVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPT-EAFGETMTEYIG 422
Cdd:PRK15056 6 GIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrQALQKNLVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 VMHQAPYLFRTTILNNIRIGR----------EEASEAEVWAVLEKVGLKEMVN-QLPEglqtmvdeaglrFSGGERHRLA 491
Cdd:PRK15056 85 QSEEVDWSFPVLVEDVVMMGRyghmgwlrraKKRDRQIVTAALARVDMVEFRHrQIGE------------LSGGQKKRVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKD--KTVIWITHHLQGVT 544
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE-LRDegKTMLVSTHNLGSVT 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
289-543 |
2.92e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.77 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 289 IGAFVLT-VFPLIDAFAplpAAAQETTIYKDSIRRfNELPEGEDDSTEAPvqpNGTSLSIEHLSFAYENQEK-KVLNDLS 366
Cdd:PTZ00265 333 ISMFMLTiILPNITEYM---KSLEATNSLYEIINR-KPLVENNDDGKKLK---DIKKIQFKNVRFHYDTRKDvEIYKDLN 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 367 LTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNipTEAFGETMTEY----IGVMHQAPYLFRTTILNNIRIG 442
Cdd:PTZ00265 406 FTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND--SHNLKDINLKWwrskIGVVSQDPLLFSNSIKNNIKYS 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 443 ----------REEASE-----------------------------------------------AEVWAVLEKVGLKEMVN 465
Cdd:PTZ00265 484 lyslkdlealSNYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdSEVVDVSKKVLIHDFVS 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 466 QLPEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETF--FEALKDKTVIWITHHLQGV 543
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRLSTI 643
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
345-588 |
3.44e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.08 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEK--KVLNDLSLTIPEKQKLAILGRSGSGKSTLASlIRGDL-RPTSGEILLG--NIPT---EAFGET 416
Cdd:PRK10535 5 LELKDIRRSYPSGEEqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAgqDVATldaDALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 MTEYIGVMHQAPYLF-RTTILNNIRI-----GRE-EASEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHR 489
Cdd:PRK10535 84 RREHFGFIFQRYHLLsHLTAAQNVEVpavyaGLErKQRLLRAQELLQRLGLEDRVEYQPSQL-----------SGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 490 LALARILLQDTPIVLLDEPTTGLDPITEQQLLeTFFEALKDK--TVIWITHHLQGVTLMDQVIFIEDGQL---------- 557
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVM-AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIvrnppaqekv 231
|
250 260 270
....*....|....*....|....*....|.
gi 256953159 558 EMSGTPEELLATNAHYQKLyridrgISSFEE 588
Cdd:PRK10535 232 NVAGGTEPVVNTASGWRQF------VSGFRE 256
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
345-558 |
3.80e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 81.75 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGN-IPTEAFGEtmteyigv 423
Cdd:PRK10636 313 LKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgIKLGYFAQ-------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 mHQAPYLfrttilnnirigreEASEAEVWAvLEKVGLKEMVNQLPE-----GLQ-TMVDEAGLRFSGGERHRLALARILL 497
Cdd:PRK10636 383 -HQLEFL--------------RADESPLQH-LARLAPQELEQKLRDylggfGFQgDKVTEETRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 498 QDTPIVLLDEPTTGLDPITEQQLLETFFEAlkDKTVIWITH--HLQGVTlMDQVIFIEDGQLE 558
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVVVSHdrHLLRST-TDDLYLVHDGKVE 506
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
363-566 |
4.61e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 78.11 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 363 NDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGVMH--QAPYLFRT-TILNNI 439
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRtfQHVRLFREmTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 440 -----------------------RIGREEASEAEVWavLEKVGLKEMVNQlpeglqtmvdEAGlRFSGGERHRLALARIL 496
Cdd:PRK11300 102 lvaqhqqlktglfsgllktpafrRAESEALDRAATW--LERVGLLEHANR----------QAG-NLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 497 LQDTPIVLLDEPTTGLDPiTEQQLLETFFEALKDK---TVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEEL 566
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNP-KETKELDELIAELRNEhnvTVLLIEHDMKLVMgISDRIYVVNQGTPLANGTPEEI 241
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
361-538 |
1.28e-15 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 76.28 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 361 VLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLgniptEAFGETMTEYIGVMHQAPYLFRTTI----- 435
Cdd:TIGR02324 23 VLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILV-----RHEGAWVDLAQASPREVLEVRRKTIgyvsq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 436 -----------------LNNIRIGREEAsEAEVWAVLEKVGLKEMVNQLPEGlqtmvdeaglRFSGGERHRLALARILLQ 498
Cdd:TIGR02324 98 flrviprvsalevvaepLLERGVPREAA-RARARELLARLNIPERLWHLPPA----------TFSGGEQQRVNIARGFIA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 256953159 499 DTPIVLLDEPTTGLDPITEQQLLETFFEALKDK-TVIWITH 538
Cdd:TIGR02324 167 DYPILLLDEPTASLDAANRQVVVELIAEAKARGaALIGIFH 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
344-562 |
1.65e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.20 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYENQEkkVLNDLSLTIPEKQKLAILGRSGSGKSTLaslirgdLR-------PTSGEILLGN-------IP 409
Cdd:COG4161 2 SIQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSL-------LRvlnlletPDSGQLNIAGhqfdfsqKP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 410 TEAFGETMTEYIGVMHQA----PYLfrtTILNNIrigreeaSEAEVWAV-LEKVGLKEMVNQLPEGLQtMVDEAG---LR 481
Cdd:COG4161 73 SEKAIRLLRQKVGMVFQQynlwPHL---TVMENL-------IEAPCKVLgLSKEQAREKAMKLLARLR-LTDKADrfpLH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 482 FSGGERHRLALARILLQDTPIVLLDEPTTGLDP-ITEQ------QLLETFFealkdkTVIWITHHLQ-GVTLMDQVIFIE 553
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPeITAQvveiirELSQTGI------TQVIVTHEVEfARKVASQVVYME 215
|
....*....
gi 256953159 554 DGQLEMSGT 562
Cdd:COG4161 216 KGRIIEQGD 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
337-576 |
2.26e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.43 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 337 PVQPNGTSLSIEHLsFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEIL-LGNIPTE---A 412
Cdd:COG4586 14 YEKEPGLKGALKGL-FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGYVPFKrrkE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 413 FGETmteyIG-VMHQapylfRT------------TILNNI-RIGREEASEAevwavlekvgLKEMVN--QLPEGLQTMVD 476
Cdd:COG4586 93 FARR----IGvVFGQ-----RSqlwwdlpaidsfRLLKAIyRIPDAEYKKR----------LDELVEllDLGELLDTPVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 477 EAGLrfsgGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLEtFFEALKDK---TVIWITHHLQGVT-LMDQVIFI 552
Cdd:COG4586 154 QLSL----GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIRE-FLKEYNRErgtTILLTSHDMDDIEaLCDRVIVI 228
|
250 260
....*....|....*....|....
gi 256953159 553 EDGQLEMSGTPEELLATNAHYQKL 576
Cdd:COG4586 229 DHGRIIYDGSLEELKERFGPYKTI 252
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
345-539 |
3.52e-15 |
|
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: 73.34 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKStlaSLIR--GDLRP-TSGEIllgNIPTEAfgETMteyi 421
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKS---SLFRalAGLWPwGSGRI---GMPEGE--DLL---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 gVMHQAPYLFRTTilnnirigreeaseaevwavlekvgLKEMVNqLPeglqtmvdeAGLRFSGGERHRLALARILLQDTP 501
Cdd:cd03223 68 -FLPQRPYLPLGT-------------------------LREQLI-YP---------WDDVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 256953159 502 IVLLDEPTTGLDPITEQQLLETFFEALkdKTVIWITHH 539
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
345-564 |
5.57e-15 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 74.60 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGD--LRPTSGEILLGNI-------------- 408
Cdd:TIGR01978 1 LKIKDLHVSVE--DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTILFKGQdllelepderarag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 409 -------PTEAFGETMTEYIgvmhqapylfrTTILNNIRIGREEaseaevwavlEKVGLKEMVNQLPEGLQTM-VDEAGL 480
Cdd:TIGR01978 79 lflafqyPEEIPGVSNLEFL-----------RSALNARRSARGE----------EPLDLLDFEKLLKEKLALLdMDEEFL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 481 R------FSGGERHRLALARILLQDTPIVLLDEPTTGLD-----PITEQ-QLLETffealKDKTVIWITHHLQGVTLM-- 546
Cdd:TIGR01978 138 NrsvnegFSGGEKKRNEILQMALLEPKLAILDEIDSGLDidalkIVAEGiNRLRE-----PDRSFLIITHYQRLLNYIkp 212
|
250
....*....|....*...
gi 256953159 547 DQVIFIEDGQLEMSGTPE 564
Cdd:TIGR01978 213 DYVHVLLDGRIVKSGDVE 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
344-550 |
7.44e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.28 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAY-ENQekkVLNDLSLTIPEKQKLAILGRSGSGKSTLaslirgdLR-------PTSGEIL-------LGNI 408
Cdd:PRK11124 2 SIQLNGINCFYgAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSL-------LRvlnllemPRSGTLNiagnhfdFSKT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 409 PTEAFGETMTEYIGVMHQA----PYLfrtTILNN-----IRI---GREEASEaEVWAVLEKVGLKEMVNQLPeglqtmvd 476
Cdd:PRK11124 72 PSDKAIRELRRNVGMVFQQynlwPHL---TVQQNlieapCRVlglSKDQALA-RAEKLLERLRLKPYADRFP-------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 477 eagLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDP-ITEQqlletffealkdktVIWITHHLQGvTLMDQVI 550
Cdd:PRK11124 140 ---LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPeITAQ--------------IVSIIRELAE-TGITQVI 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
364-572 |
7.84e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.74 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 364 DLSLTIPEKQKLAILGRSGSGKS-----TLASLIRGdLRPTSGEILLGNIPTEAFGETMTEYIGVMhQAPylfRTTiLNN 438
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAG-VRQTAGRVLLDGKPVAPCALRGRKIATIM-QNP---RSA-FNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 439 IRIGREEASE-----------AEVWAVLEKVGLkemvnqlpEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDE 507
Cdd:PRK10418 95 LHTMHTHAREtclalgkpaddATLTAALEAVGL--------ENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 508 PTTGLDPITEQQLLETFFEALKDKT--VIWITHHLqGVT--LMDQVIFIEDGQLEMSGTPEELLATNAH 572
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDM-GVVarLADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
360-524 |
7.90e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.77 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEI------LLGNIPTEAfgETMTEYIGVMHQAPYLF-- 431
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELyyqgqdLLKADPEAQ--KLLRQKIQIVFQNPYGSln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 432 -RTTI--------LNNIRIGREEASEaEVWAVLEKVGLK-EMVNQLPEglqtMvdeaglrFSGGERHRLALARILLQDTP 501
Cdd:PRK11308 107 pRKKVgqileeplLINTSLSAAERRE-KALAMMAKVGLRpEHYDRYPH----M-------FSGGQRQRIAIARALMLDPD 174
|
170 180
....*....|....*....|...
gi 256953159 502 IVLLDEPTTGLDPITEQQLLETF 524
Cdd:PRK11308 175 VVVADEPVSALDVSVQAQVLNLM 197
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-569 |
1.15e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.31 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLR------PTSGEIL-LGNIPTEAFGETMTEYIGVMHQAPYL 430
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLyFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 431 F-RTTILNNIRI-----GREEASEAE--VWAVLEKVGL-KEMVNQLpeglqtmvDEAGLRFSGGERHRLALARILLQDTP 501
Cdd:PRK14246 102 FpHLSIYDNIAYplkshGIKEKREIKkiVEECLRKVGLwKEVYDRL--------NSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 502 IVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELLAT 569
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVArVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
358-568 |
1.30e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.85 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGVMHQAPYLFRT---- 433
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLRTrltm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 434 -----------TILNNIR--------IGREEASEAEVWaVLEKVGLKEMVNqlpeglqtmvDEAGLRFSGGERHRLALAR 494
Cdd:PRK10619 97 vfqhfnlwshmTVLENVMeapiqvlgLSKQEARERAVK-YLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 495 ILLQDTPIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITHHLQ-GVTLMDQVIFIEDGQLEMSGTPEELLA 568
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGfARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
345-572 |
1.96e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.76 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKV--LNDLSLTIPEKQKLAILGRSGSGKST--------LAS--LIRGDLRPTSGEILlgNIPTEA 412
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSQtafalmglLAAngRIGGSATFNGREIL--NLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 413 FGETMTEYIGVMHQAPylfrTTILNN-IRIGRE---------EASEAEvwAVLEKVGLKEMVnQLPEGLQTMvdeaGL-- 480
Cdd:PRK09473 91 LNKLRAEQISMIFQDP----MTSLNPyMRVGEQlmevlmlhkGMSKAE--AFEESVRMLDAV-KMPEARKRM----KMyp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 481 -RFSGGERHRLALARILLQDTPIVLLDEPTTGLDpITEQQLLETFFEALKDK---TVIWITHHLqGVT--LMDQVIFIED 554
Cdd:PRK09473 160 hEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD-VTVQAQIMTLLNELKREfntAIIMITHDL-GVVagICDKVLVMYA 237
|
250
....*....|....*...
gi 256953159 555 GQLEMSGTPEELLATNAH 572
Cdd:PRK09473 238 GRTMEYGNARDVFYQPSH 255
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
357-578 |
5.36e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 357 QEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILL-GNIPteafgeTMTEYIGVMHqaPYLfrtTI 435
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVnGRVS------ALLELGAGFH--PEL---TG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 436 LNNIRI-----GreeASEAEVWAVLEKVglkemvnqlpeglqtmVDEAGL---------RFSGGERHRLALARILLQDTP 501
Cdd:COG1134 106 RENIYLngrllG---LSRKEIDEKFDEI----------------VEFAELgdfidqpvkTYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 502 IVLLDEPT-TGlDpITEQQLLETFFEALKD--KTVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPEELLatnAHYQKLY 577
Cdd:COG1134 167 ILLVDEVLaVG-D-AAFQKKCLARIRELREsgRTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDGDPEEVI---AAYEALL 241
|
.
gi 256953159 578 R 578
Cdd:COG1134 242 A 242
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
345-568 |
5.69e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGE---TMTEYI 421
Cdd:PRK13638 2 LATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQAP--YLFRTTILNNIRIGREEASEAEvwavlekvglKEMVNQLPEGLqTMVDEAGLR------FSGGERHRLALA 493
Cdd:PRK13638 80 ATVFQDPeqQIFYTDIDSDIAFSLRNLGVPE----------AEITRRVDEAL-TLVDAQHFRhqpiqcLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 494 RILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHHlqGVTLM----DQVIFIEDGQLEMSGTPEELLA 568
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH--DIDLIyeisDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
359-568 |
1.20e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 70.90 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 359 KKVLNDLSL-----TIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLgNIPTEAFG-------------ETMTEY 420
Cdd:cd03237 7 KKTLGEFTLeveggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKpqyikadyegtvrDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 IGVMHQAPYlFRTTILNNIRIgreeaseaevwavlEKVglkeMVNQLPEglqtmvdeaglrFSGGERHRLALARILLQDT 500
Cdd:cd03237 86 TKDFYTHPY-FKTEIAKPLQI--------------EQI----LDREVPE------------LSGGELQRVAIAACLSKDA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 501 PIVLLDEPTTGLDpiTEQQLLET-----FFEAlKDKTVIWITHHLQGVTLMDQVIFIEDGQLEMSG---TPEELLA 568
Cdd:cd03237 135 DIYLLDEPSAYLD--VEQRLMASkvirrFAEN-NEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGvanPPQSLRS 207
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
345-513 |
1.55e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.73 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQekKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGN-----IPTEAFGET--- 416
Cdd:PRK11701 7 LSVRGLTKLYGPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 ---MTEYiGVMHQAPYL-FRTTILNNIRIG--------------REEASEaevWavLEKVglkemvnqlpEGLQTMVDEA 478
Cdd:PRK11701 85 rllRTEW-GFVHQHPRDgLRMQVSAGGNIGerlmavgarhygdiRATAGD---W--LERV----------EIDAARIDDL 148
|
170 180 190
....*....|....*....|....*....|....*
gi 256953159 479 GLRFSGGERHRLALARILLQDTPIVLLDEPTTGLD 513
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
350-561 |
1.73e-13 |
|
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: 69.87 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 350 LSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEI-LLGNI--PTEA---FGETMT--EYI 421
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVtVRGRVssLLGLgggFNPELTgrENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 gvmhqapyLFRTTILNnirigreeASEAEVWAVLEKVglkEMVNQLPEGLQTMVdeagLRFSGGERHRLALARILLQDTP 501
Cdd:cd03220 106 --------YLNGRLLG--------LSRKEIDEKIDEI---IEFSELGDFIDLPV----KTYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256953159 502 IVLLDEPTTGLDPITEQQLLETFFEALKD-KTVIWITHHLQGVTLM-DQVIFIEDGQLEMSG 561
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
345-577 |
1.87e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAyeNQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDL----RP----TSGEILLGNIPTEAFGET 416
Cdd:PRK13547 2 LTADHLHVA--RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPrgarVTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 -MTEYIGVMHQA-----PYLFRTTIL-----NNIRIGREEASEAEV-WAVLEKVGLKEMVNQlpeglqtmvDEAGLrfSG 484
Cdd:PRK13547 80 rLARLRAVLPQAaqpafAFSAREIVLlgrypHARRAGALTHRDGEIaWQALALAGATALVGR---------DVTTL--SG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 485 GERHRLALARILLQ---------DTPIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHHLQ-GVTLMDQVIFI 552
Cdd:PRK13547 149 GELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNlAARHADRIAML 228
|
250 260
....*....|....*....|....*
gi 256953159 553 EDGQLEMSGTPEELLaTNAHYQKLY 577
Cdd:PRK13547 229 ADGAIVAHGAPADVL-TPAHIARCY 252
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
363-573 |
4.33e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.83 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 363 NDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNipteafgETMTEY------IGVMHQA----PYLfr 432
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE-------KRMNDVppaergVGMVFQSyalyPHL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 433 tTILNNIRIGREEASeaevwavLEKVGLKEMVNQLPEGLQT--MVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTT 510
Cdd:PRK11000 91 -SVAENMSFGLKLAG-------AKKEEINQRVNQVAEVLQLahLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 511 GLDPITEQQL---LETFFEALKdKTVIWITH-HLQGVTLMDQVIFIEDGQLEMSGTPEELLatnaHY 573
Cdd:PRK11000 163 NLDAALRVQMrieISRLHKRLG-RTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELY----HY 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
343-564 |
4.59e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILlgnipteafgETMTEYIG 422
Cdd:PRK09544 3 SLVSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 VMHQAPYLFRTTILNNIRIG--REEASEAEVWAVLEKVGLKEMVNQlpeGLQtmvdeaglRFSGGERHRLALARILLQDT 500
Cdd:PRK09544 71 YVPQKLYLDTTLPLTVNRFLrlRPGTKKEDILPALKRVQAGHLIDA---PMQ--------KLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 501 PIVLLDEPTTGLDpITEQQLLETFFEALKDK---TVIWITHHLQGVTLMDQVIFIEDGQLEMSGTPE 564
Cdd:PRK09544 140 QLLVLDEPTQGVD-VNGQVALYDLIDQLRREldcAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPE 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
347-558 |
6.51e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 347 IEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafgeTMTE--YIGvM 424
Cdd:PRK11147 322 MENVNYQID--GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG---------TKLEvaYFD-Q 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFRTTILNNIRIGREEAseaevwavlekvglkeMVNQLPEG----LQ--------TMVDEAGLrfSGGERHRLAL 492
Cdd:PRK11147 390 HRAELDPEKTVMDNLAEGKQEV----------------MVNGRPRHvlgyLQdflfhpkrAMTPVKAL--SGGERNRLLL 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 493 ARILLQDTPIVLLDEPTTGLDpITEQQLLEtffEALKD--KTVIWITHHLQGV--TLMDQVIFIEDGQLE 558
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLD-VETLELLE---ELLDSyqGTVLLVSHDRQFVdnTVTECWIFEGNGKIG 517
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
362-562 |
7.82e-13 |
|
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: 66.96 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLASlirgDLRPTSGEILLGNIPTeAFGETMTEYIGvmhQAPYLFRTTiLNNIRI 441
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN----EGLYASGKARLISFLP-KFSRNKLIFID---QLQFLIDVG-LGYLTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 442 GREeaseaevwavlekvglkemvnqlpegLQTMvdeaglrfSGGERHRLALARILLQDTP--IVLLDEPTTGLDPITEQQ 519
Cdd:cd03238 82 GQK--------------------------LSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 256953159 520 LLETfFEALKDK--TVIWITHHLQGVTLMDQVIFIEDGQLEMSGT 562
Cdd:cd03238 128 LLEV-IKGLIDLgnTVILIEHNLDVLSSADWIIDFGPGSGKSGGK 171
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
346-538 |
8.42e-13 |
|
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: 71.12 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 346 SIEHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLaslirgdLRptsgeILLGnIPTEAFGETMTE---YIG 422
Cdd:TIGR03719 6 TMNRVSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTL-------LR-----IMAG-VDKDFNGEARPQpgiKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 VMHQAPYLFRT-TILNNIRIGREE--------------------------ASEAEVWAVLEKVGLKEMVNQL-------- 467
Cdd:TIGR03719 72 YLPQEPQLDPTkTVRENVEEGVAEikdaldrfneisakyaepdadfdklaAEQAELQEIIDAADAWDLDSQLeiamdalr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 468 -PEGlqtmvDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPIT----EQQLLEtfFEAlkdkTVIWITH 538
Cdd:TIGR03719 152 cPPW-----DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE--YPG----TVVAVTH 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
348-538 |
1.87e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 348 EHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG--NIPTEAFGET--MTEYIGV 423
Cdd:PRK10908 5 EHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghDITRLKNREVpfLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 424 MHQAPYLFRT-TILNNIRI------GREEASEAEVWAVLEKVGLKEMVNQLPeglqtmvdeagLRFSGGERHRLALARIL 496
Cdd:PRK10908 84 IFQDHHLLMDrTVYDNVAIpliiagASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 256953159 497 LQDTPIVLLDEPTTGLDPITEQQLLETFFEALK-DKTVIWITH 538
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATH 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
343-539 |
2.68e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.52 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDL--RPTSGEIllgNIPTEAFGEtmtey 420
Cdd:COG2401 27 VAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV---DVPDNQFGR----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 421 igvmhqapylfRTTILNNIRIgreEASEAEVWAVLEKVGLKEMVNQLpeglqTMVDEaglrFSGGERHRLALARILLQDT 500
Cdd:COG2401 99 -----------EASLIDAIGR---KGDFKDAVELLNAVGLSDAVLWL-----RRFKE----LSTGQKFRFRLALLLAERP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 256953159 501 PIVLLDEPTTGLDPITEQQLLETFFEALKD--KTVIWITHH 539
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLARRagITLVVATHH 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
340-572 |
2.81e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 340 PNGTSLSIEHLSFAYENQEKKV--LNDLSLTIPEKQKLAILGRSGSGKSTLA-SLIR------GD-------LRPTSGEI 403
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTAlALMRlleqagGLvqcdkmlLRRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 404 LLGNIPTEA-------------FGETMTEYIGVmhqapYLFRTTILNNIRI----GREEASeAEVWAVLEKVglkemvnQ 466
Cdd:PRK10261 88 IELSEQSAAqmrhvrgadmamiFQEPMTSLNPV-----FTVGEQIAESIRLhqgaSREEAM-VEAKRMLDQV-------R 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 467 LPEGlQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKT--VIWITHHLQGVT 544
Cdd:PRK10261 155 IPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVA 233
|
250 260
....*....|....*....|....*....
gi 256953159 545 -LMDQVIFIEDGQLEMSGTPEELLATNAH 572
Cdd:PRK10261 234 eIADRVLVMYQGEAVETGSVEQIFHAPQH 262
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
345-539 |
2.85e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.04 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGETMTEYIGVM 424
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVA-------GKSILTNISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQA-PYLFRTTILNNIRIGREEASeaeVWAVLEKVGLKEMVNQLPEGLQTM-----VDEAGLRFSGGERHRLALARILLQ 498
Cdd:TIGR01257 2011 HQNmGYCPQFDAIDDLLTGREHLY---LYARLRGVPAEEIEKVANWSIQSLglslyADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 256953159 499 DTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHH 539
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
31-218 |
9.70e-12 |
|
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: 66.03 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 31 FALLLGFLTFFSAGALMFTSGYLISRAASLPENILLIYIPIVLTrAFGIGRPVFRYVERLTSHNWVLKMTSDLRLKLYN- 109
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLL-LLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 110 VLEKDAIFFKtKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFALCMLLMLGVVVFLLPLVS 189
Cdd:cd07346 82 LQRLSLSFFD-RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190
....*....|....*....|....*....|
gi 256953159 190 VLVNGA-RQEKHKYAknELYQTLTDNILGV 218
Cdd:cd07346 161 RRIRKAsREVRESLA--ELSAFLQESLSGI 188
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
358-564 |
1.31e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 358 EKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRG--DLRPTSGEILLGNI------PTE--------AFgETMTEYI 421
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGEsildlePEErahlgiflAF-QYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 422 GVMHQApylFRTTILNNIRI--GREEASEAEVWAVL-EKVglkEMVNQLPEGLQTMVDEAglrFSGGERHRLALARILLQ 498
Cdd:CHL00131 98 GVSNAD---FLRLAYNSKRKfqGLPELDPLEFLEIInEKL---KLVGMDPSFLSRNVNEG---FSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 499 DTPIVLLDEPTTGLDpITEQQLLETFFEAL--KDKTVIWITHHLQgvtLMDQVI-----FIEDGQLEMSGTPE 564
Cdd:CHL00131 169 DSELAILDETDSGLD-IDALKIIAEGINKLmtSENSIILITHYQR---LLDYIKpdyvhVMQNGKIIKTGDAE 237
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
317-524 |
1.86e-11 |
|
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: 66.88 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 317 KDSIRRFNELPEGEDDSTEAPVQ---PNGTSL-----SIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTL 388
Cdd:TIGR03719 287 KARLARYEELLSQEFQKRNETAEiyiPPGPRLgdkviEAENLTKAFG--DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 389 ASLIRGDLRPTSGEIllgnipteAFGETMTeyIGVMHQapylFRTTILNN-------------IRIG-REEASEAEVWAV 454
Cdd:TIGR03719 365 FRMITGQEQPDSGTI--------EIGETVK--LAYVDQ----SRDALDPNktvweeisggldiIKLGkREIPSRAYVGRF 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 455 LEKVGlkemvNQlpeglQTMVDEaglrFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQL---LETF 524
Cdd:TIGR03719 431 NFKGS-----DQ-----QKKVGQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALeeaLLNF 489
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
345-568 |
2.53e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEI------LLGNIP---TEAFGE 415
Cdd:PRK15064 320 LEVENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGYYAqdhAYDFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 416 TMT--EYigvMHQapylFRTtilnnirigrEEASEAEVWAVLEKV-----GLKEMVNQLpeglqtmvdeaglrfSGGERH 488
Cdd:PRK15064 398 DLTlfDW---MSQ----WRQ----------EGDDEQAVRGTLGRLlfsqdDIKKSVKVL---------------SGGEKG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 489 RLALARILLQDTPIVLLDEPTTGLDpiteQQLLETFFEALK--DKTVIWITHHLQGV-TLMDQVIFIEDGQL-EMSGTPE 564
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD----MESIESLNMALEkyEGTLIFVSHDREFVsSLATRIIEITPDGVvDFSGTYE 521
|
....
gi 256953159 565 ELLA 568
Cdd:PRK15064 522 EYLR 525
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
360-575 |
2.72e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.11 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEIL-LGNIPTEAFGETMTEY---IGVMHQAPYLF---R 432
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLGMKDDEWRAVrsdIQMIFQDPLASlnpR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 433 TTILNNI---------RIGREEASEaEVWAVLEKVGLKE-MVNQLPEglqtmvdeaglRFSGGERHRLALARILLQDTPI 502
Cdd:PRK15079 115 MTIGEIIaeplrtyhpKLSRQEVKD-RVKAMMLKVGLLPnLINRYPH-----------EFSGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 256953159 503 VLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVT-LMDQVIFIEDGQLEMSGTPEELLATNAH-YQK 575
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEVYHNPLHpYTK 259
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
360-567 |
2.81e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.09 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTeAFGETMTEY---IGVMHQ----APYLfr 432
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAALaagVAIIYQelhlVPEM-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 433 tTILNNIRIGR---------EEASEAEVWAVLEKVGLKemvnqlpeglqtmVD-EAGLR-FSGGERHRLALARILLQDTP 501
Cdd:PRK11288 95 -TVAENLYLGQlphkggivnRRLLNYEAREQLEHLGVD-------------IDpDTPLKyLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 502 IVLLDEPTTGLDpITEQQLLETFFEALKD--KTVIWITHHLQGV-TLMDQVIFIEDGQL-----EMSGTPEELL 567
Cdd:PRK11288 161 VIAFDEPTSSLS-AREIEQLFRVIRELRAegRVILYVSHRMEEIfALCDAITVFKDGRYvatfdDMAQVDRDQL 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
357-556 |
3.13e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 357 QEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTS--GEILLGN-IPTEafgETMTEyIGVMHQAPYLF-- 431
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNrKPTK---QILKR-TGFVTQDDILYph 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 432 ---RTTI-------LNNIRIGREEASEAEvwAVLEKVGLKEMVNqlpeglqTMVDEAGLR-FSGGERHRLALARILLQDT 500
Cdd:PLN03211 155 ltvRETLvfcsllrLPKSLTKQEKILVAE--SVISELGLTKCEN-------TIIGNSFIRgISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 501 PIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITHHLQG--VTLMDQVIFIEDGQ 556
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSlAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
361-566 |
4.87e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 361 VLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGV--MHQAPYLF-RTTILN 437
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIylVPQEPLLFpNLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 438 NI--RIGREEASEAEvwavlekvgLKEMVNQLPEGLQTMVDEAGLRFSggERHRLALARILLQDTPIVLLDEPTTGLDPI 515
Cdd:PRK15439 106 NIlfGLPKRQASMQK---------MKQLLAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPTASLTPA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 256953159 516 tEQQLLETFFEALKDKTV--IWITHHLQGV-TLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:PRK15439 175 -ETERLFSRIRELLAQGVgiVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
345-513 |
5.66e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.20 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFayeNQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEYIGvm 424
Cdd:PRK13541 2 LSLHQLQF---NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFRTTILNNIRIGREEASEAE-VWAVLEKVglkemvnqlpeGLQTMVDEAGLRFSGGERHRLALARILLQDTPIV 503
Cdd:PRK13541 77 HNLGLKLEMTVFENLKFWSEIYNSAEtLYAAIHYF-----------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLW 145
|
170
....*....|
gi 256953159 504 LLDEPTTGLD 513
Cdd:PRK13541 146 LLDEVETNLS 155
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
362-561 |
5.83e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFGETMTEY--IGVMHQAPYLF-RTTILNN 438
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlgIGIIYQELSVIdELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 439 IRIGREEASeaEVWAVlEKVGLKEMVNQLPE-----GLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLD 513
Cdd:PRK09700 101 LYIGRHLTK--KVCGV-NIIDWREMRVRAAMmllrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 256953159 514 PITEQQLLETFFEALKD-KTVIWITHHLQGV-TLMDQVIFIEDGQLEMSG 561
Cdd:PRK09700 178 NKEVDYLFLIMNQLRKEgTAIVYISHKLAEIrRICDRYTVMKDGSSVCSG 227
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
344-538 |
1.17e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 344 SLSIEHLSFAYEnqekKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEIL---------LGNIPTEAFG 414
Cdd:PRK11147 5 SIHGAWLSFSDA----PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyeqdlivarLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 415 ETMTEYI--GVMHQAPYLFR-TTILNNIRigrEEASE------AEVWAVLEKVGLKEMVNQLPEGLQTM---VDEAGLRF 482
Cdd:PRK11147 81 GTVYDFVaeGIEEQAEYLKRyHDISHLVE---TDPSEknlnelAKLQEQLDHHNLWQLENRINEVLAQLgldPDAALSSL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 483 SGGERHRLALARILLQDTPIVLLDEPTTGLDpITEQQLLETFfeaLKD--KTVIWITH 538
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IETIEWLEGF---LKTfqGSIIFISH 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
359-538 |
1.36e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 359 KKVLNDLSLTIPEKQKLAILGRSGSGKSTLaslirgdLRptsgeILLGnIPTEAFGET--MTEY-IGVMHQAPYLFRT-T 434
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTL-------LR-----IMAG-VDKEFEGEArpAPGIkVGYLPQEPQLDPEkT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 435 ILNNIrigrEEASeAEVWAVLEKvgLKEMVNQLPEG-------------LQTMVDEAG--------------LR------ 481
Cdd:PRK11819 87 VRENV----EEGV-AEVKAALDR--FNEIYAAYAEPdadfdalaaeqgeLQEIIDAADawdldsqleiamdaLRcppwda 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 482 ----FSGGERHRLALARILLQDTPIVLLDEPTTGLDpiTEQ-QLLETFfeaLKD--KTVIWITH 538
Cdd:PRK11819 160 kvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD--AESvAWLEQF---LHDypGTVVAVTH 218
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
376-560 |
1.95e-10 |
|
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: 60.70 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 376 AILGRSGSGKSTLASLIR----GDLRPTSGeilLGNIPTEAFGETmtEYIGVMHQApylFRTTILNNIRIGREeaseaev 451
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNSK---GGAHDPKLIREG--EVRAQVKLA---FENANGKKYTITRS------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 452 WAVLEKVglkEMVNQlpEGLQT-MVDEAGlRFSGGER------HRLALARILLQDTPIVLLDEPTTGLDPIT-EQQLLET 523
Cdd:cd03240 91 LAILENV---IFCHQ--GESNWpLLDMRG-RCSGGEKvlasliIRLALAETFGSNCGILALDEPTTNLDEENiEESLAEI 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 256953159 524 FFEALKDKT--VIWITHHLQGVTLMDQVIFIEDGQLEMS 560
Cdd:cd03240 165 IEERKSQKNfqLIVITHDEELVDAADHIYRVEKDGRQKS 203
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
343-557 |
2.08e-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: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 343 TSLSIEHLSFayenqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGEtmteyig 422
Cdd:cd03215 3 PVLEVRGLSV------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-------GK------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 423 vmhqaPYLFRTTilnnirigrEEASEAEVWAVLE---KVGLkemvnqLPEglQTMVDEAGLRF--SGGERHRLALARILL 497
Cdd:cd03215 63 -----PVTRRSP---------RDAIRAGIAYVPEdrkREGL------VLD--LSVAENIALSSllSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256953159 498 QDTPIVLLDEPTTGLDPITEQQLLETFFEALKD-KTVIWITHHLQGVTLM-DQVIFIEDGQL 557
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
365-567 |
3.96e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 365 LSLTIPEKQKLAILGRSGSGKSTLASLIRGdLRPTSGEILLGnipteafGETMTEYIGV--MHQAPYL------------ 430
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFA-------GQPLEAWSAAelARHRAYLsqqqtppfampv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 431 FRTTILNNIRIGREEASEAEVWAVLEKVGLKE----MVNQLpeglqtmvdeaglrfSGGERHRLALARILLQDTP----- 501
Cdd:PRK03695 87 FQYLTLHQPDKTRTEAVASALNEVAEALGLDDklgrSVNQL---------------SGGEWQRVRLAAVVLQVWPdinpa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 256953159 502 --IVLLDEPTTGLDpITEQQLLETFFEALKDK--TVIWITHHLQGvTL--MDQVIFIEDGQLEMSGTPEELL 567
Cdd:PRK03695 152 gqLLLLDEPMNSLD-VAQQAALDRLLSELCQQgiAVVMSSHDLNH-TLrhADRVWLLKQGKLLASGRRDEVL 221
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
345-539 |
5.48e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRG--DLRPTSGEI------LLGNIPTEAFGET 416
Cdd:PRK09580 2 LSIKDLHVSVE--DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVefkgkdLLELSPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 417 M-------TEYIGVMHQapyLFRTTILNNIRIGREEASeaevwavLEKVGLKEMVN------QLPEGLQTMVDEAGlrFS 483
Cdd:PRK09580 80 IfmafqypVEIPGVSNQ---FFLQTALNAVRSYRGQEP-------LDRFDFQDLMEekiallKMPEDLLTRSVNVG--FS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 484 GGERHRLALARILLQDTPIVLLDEPTTGLDpITEQQLLETFFEALKD--KTVIWITHH 539
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIVADGVNSLRDgkRSFIIVTHY 204
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
345-539 |
7.25e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQekKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLgnipteaFGETMTEYIGVM 424
Cdd:PRK13540 2 LDVIELDFDYHDQ--PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF-------ERQSIKKDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQA-----------PYLfrtTILNNIRIGREEASEAevwavlekVGLKEMVNQLpeGLQTMVDEAGLRFSGGERHRLALA 493
Cdd:PRK13540 73 QKQlcfvghrsginPYL---TLRENCLYDIHFSPGA--------VGITELCRLF--SLEHLIDYPCGLLSSGQKRQVALL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 256953159 494 RILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKTVIWITHH 539
Cdd:PRK13540 140 RLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
360-556 |
1.16e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGdLRPT---SGEILLGNIPTEAFGETMTEY--IGVMHQAPYLFRT- 433
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRDTERagIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 434 TILNNIRIGRE----------EASEAEVWAVLEKVGLKEMVNQLPEGlqtmvdeaglRFSGGERHRLALARILLQDTPIV 503
Cdd:TIGR02633 94 SVAENIFLGNEitlpggrmayNAMYLRAKNLLRELQLDADNVTRPVG----------DYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 504 LLDEPTTGLDPiTEQQLLETFFEALKDKTV--IWITHHLQGV-TLMDQVIFIEDGQ 556
Cdd:TIGR02633 164 ILDEPSSSLTE-KETEILLDIIRDLKAHGVacVYISHKLNEVkAVCDTICVIRDGQ 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
359-538 |
1.56e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 359 KKVLNDLSL-----TIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafgetmteyIGVMHQAPYLfrt 433
Cdd:PRK13409 347 TKKLGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------------LKISYKPQYI--- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 434 tilnnirigrEEASEAEVWAVLEKVGLK--------EMVN--QLPEGLQTMVDEaglrFSGGERHRLALARILLQDTPIV 503
Cdd:PRK13409 410 ----------KPDYDGTVEDLLRSITDDlgssyyksEIIKplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 256953159 504 LLDEPTTGLDpiTEQQLLET-----FFEAlKDKTVIWITH 538
Cdd:PRK13409 476 LLDEPSAHLD--VEQRLAVAkairrIAEE-REATALVVDH 512
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
366-540 |
2.86e-09 |
|
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: 59.80 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 366 SLTIPEKQK-LAILGRSGSGKSTLASLIRGDLRPTsgeilLGNIPTEAFGETMTEYigvmhqapylFRTTIL-------- 436
Cdd:COG1245 92 GLPVPKKGKvTGILGPNGIGKSTALKILSGELKPN-----LGDYDEEPSWDEVLKR----------FRGTELqdyfkkla 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 437 -NNIRIGR-----EEASEA---EVWAVLEKVG----LKEMVNQLpeGLQTMVDEAGLRFSGGERHRLALARILLQDTPIV 503
Cdd:COG1245 157 nGEIKVAHkpqyvDLIPKVfkgTVRELLEKVDergkLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 256953159 504 LLDEPTTGLDpITE--------QQLLEtffealKDKTVIWITHHL 540
Cdd:COG1245 235 FFDEPSSYLD-IYQrlnvarliRELAE------EGKYVLVVEHDL 272
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
33-278 |
3.13e-09 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 58.04 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 33 LLLGFLTFFSAGALMFTSGYLISR------AASLPENILLIYIPIVLTrAFGIGRPVFRYVerltsHNWVL-----KMTS 101
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRildvllPDGDPETQALNVYSLALL-LLGLAQFILSFL-----QSYLLnhtgeRLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 102 DLRLKLYN-VLEKDAIFFKTKyRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFALCMLLMLgv 180
Cdd:pfam00664 75 RLRRKLFKkILRQPMSFFDTN-SVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 181 vvFLLPLVSVLVNGA---RQEKHKYAKNELYQTLTDNILGVSDwVFSQRGSE-FVARYetDEANVRALDEKMK-QFNRGR 255
Cdd:pfam00664 152 --PLYILVSAVFAKIlrkLSRKEQKAVAKASSVAEESLSGIRT-VKAFGREEyELEKY--DKALEEALKAGIKkAVANGL 226
|
250 260
....*....|....*....|...
gi 256953159 256 DFVLQLLFGVIAIAVLAWTSVRF 278
Cdd:pfam00664 227 SFGITQFIGYLSYALALWFGAYL 249
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
362-563 |
5.02e-09 |
|
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: 57.24 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLaslIRGDLRPTSGEILLGN--IPTEAFGETMTEYIG---VMHQAPyLFRTT-- 434
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSL---INDTLYPALARRLHLKkeQPGNHDRIEGLEHIDkviVIDQSP-IGRTPrs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 435 -------ILNNIRI-------GREEASE-----------AEVWA--VLEKVGLKEMVNQLPEGLQTMVDeAGLRF----- 482
Cdd:cd03271 87 npatytgVFDEIRElfcevckGKRYNREtlevrykgksiADVLDmtVEEALEFFENIPKIARKLQTLCD-VGLGYiklgq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 483 -----SGGERHRLALARILLQDTP---IVLLDEPTTGLDPITEQQLLETfFEALKDK--TVIWITHHLQGVTLMDQVIFI 552
Cdd:cd03271 166 pattlSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEV-LQRLVDKgnTVVVIEHNLDVIKCADWIIDL 244
|
250
....*....|....*..
gi 256953159 553 ------EDGQLEMSGTP 563
Cdd:cd03271 245 gpeggdGGGQVVASGTP 261
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
360-556 |
6.11e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAFG--ETMTEYIGVMHQA----PYLfrt 433
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpkSSQEAGIGIIHQElnliPQL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 434 TILNNIRIGREEASE----------AEVWAVLEKVGLK----EMVNQLPEGLQTMVDeaglrfsggerhrlaLARILLQD 499
Cdd:PRK10762 95 TIAENIFLGREFVNRfgridwkkmyAEADKLLARLNLRfssdKLVGELSIGEQQMVE---------------IAKVLSFE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 500 TPIVLLDEPTTGLDPiTEQQLLETFFEALKDKT--VIWITHHLQGV-TLMDQVIFIEDGQ 556
Cdd:PRK10762 160 SKVIIMDEPTDALTD-TETESLFRVIRELKSQGrgIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
326-541 |
7.59e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 326 LPEGEDDSTEAPVQPNGTSLSIEHLSFAYenQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDlRPTSGE--- 402
Cdd:PRK10938 242 LPEPDEPSARHALPANEPRIVLNNGVVSY--NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQGYSndl 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 403 ILLGNipTEAFGETMTE---YIGV----MHQApYLFRTTILNNI------RIGREEA-SE-----AEVWavLEKVGLKEm 463
Cdd:PRK10938 319 TLFGR--RRGSGETIWDikkHIGYvsssLHLD-YRVSTSVRNVIlsgffdSIGIYQAvSDrqqklAQQW--LDILGIDK- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 464 vnqlpeglqTMVDEAGLRFSGGERhRLAL-ARILLQDTPIVLLDEPTTGLDPITeQQLLETFFEAL---KDKTVIWITHH 539
Cdd:PRK10938 393 ---------RTADAPFHSLSWGQQ-RLALiVRALVKHPTLLILDEPLQGLDPLN-RQLVRRFVDVLiseGETQLLFVSHH 461
|
..
gi 256953159 540 LQ 541
Cdd:PRK10938 462 AE 463
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
366-540 |
9.45e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 9.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 366 SLTIPEKQK-LAILGRSGSGKSTLASLIRGDLRPTsgeilLGNIPTEAFGETMTEYigvmhqapylFRTTIL-------- 436
Cdd:PRK13409 92 GLPIPKEGKvTGILGPNGIGKTTAVKILSGELIPN-----LGDYEEEPSWDEVLKR----------FRGTELqnyfkkly 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 437 -NNIRIGR-----EEASEA---EVWAVLEKVG----LKEMVNQLpeGLQTMVDEAGLRFSGGERHRLALARILLQDTPIV 503
Cdd:PRK13409 157 nGEIKVVHkpqyvDLIPKVfkgKVRELLKKVDergkLDEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 256953159 504 LLDEPTTGLDpITEQ----QLLEtffEALKDKTVIWITHHL 540
Cdd:PRK13409 235 FFDEPTSYLD-IRQRlnvaRLIR---ELAEGKYVLVVEHDL 271
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
320-522 |
1.46e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 320 IRRFNELPEGEDDSTEAPVQ---PNGTSL-----SIEHLSFAYEnqEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASL 391
Cdd:PRK11819 292 LARYEELLSEEYQKRNETNEifiPPGPRLgdkviEAENLSKSFG--DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKM 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 392 IRGDLRPTSGEILLGnipteafgETMTeyIGVMHQapylFRTTI-------------LNNIRIG-REEASEAEVWAVlek 457
Cdd:PRK11819 370 ITGQEQPDSGTIKIG--------ETVK--LAYVDQ----SRDALdpnktvweeisggLDIIKVGnREIPSRAYVGRF--- 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 458 vGLK-----EMVNQLpeglqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDEPTTGLDPIT----EQQLLE 522
Cdd:PRK11819 433 -NFKggdqqKKVGVL---------------SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETlralEEALLE 490
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
313-538 |
2.27e-08 |
|
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: 57.07 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 313 TTIYKDSIRRFNELPegeddsteaPVQPNGtslsiehlsfayenqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLI 392
Cdd:TIGR00954 444 IVEYQDNGIKFENIP---------LVTPNG----------------DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 393 rGDLRPTSGEILLGNIPTEAFgetmteYIGvmhQAPYLFRTTILNNI-------RIGREEASEAEVWAVLEKVGLKEMVn 465
Cdd:TIGR00954 499 -GELWPVYGGRLTKPAKGKLF------YVP---QRPYMTLGTLRDQIiypdsseDMKRRGLSDKDLEQILDNVQLTHIL- 567
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 466 QLPEGLQTMVDEAGLrFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLletfFEALKDK--TVIWITH 538
Cdd:TIGR00954 568 EREGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM----YRLCREFgiTLFSVSH 637
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
360-556 |
2.95e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGdLRPT---SGEILLGNIPTEAFGETMTEY--IGVMHQ----APYL 430
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQASNIRDTERagIAIIHQelalVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 431 frtTILNNIRIGRE---------EASEAEVWAVLEKVGLKEMVNqlpeglqTMVDEAGlrfsGGERHRLALARILLQDTP 501
Cdd:PRK13549 98 ---SVLENIFLGNEitpggimdyDAMYLRAQKLLAQLKLDINPA-------TPVGNLG----LGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 502 IVLLDEPTTGLdpiTEQ--QLLETFFEALKDKTV--IWITHHLQGV-TLMDQVIFIEDGQ 556
Cdd:PRK13549 164 LLILDEPTASL---TESetAVLLDIIRDLKAHGIacIYISHKLNEVkAISDTICVIRDGR 220
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
360-556 |
3.11e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGdLRPT---SGEILL-------GNIP-TEAFGetmteyIGVMHQ-- 426
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFdgevcrfKDIRdSEALG------IVIIHQel 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 427 --APYLfrtTILNNIRIGREEAS---------EAEVWAVLEKVGLKE----MVNQLPEGLQTMVDeaglrfsggerhrla 491
Cdd:NF040905 88 alIPYL---SIAENIFLGNERAKrgvidwnetNRRARELLAKVGLDEspdtLVTDIGVGKQQLVE--------------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 492 LARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEaLKDK--TVIWITHHLQGVT-LMDQVIFIEDGQ 556
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLE-LKAQgiTSIIISHKLNEIRrVADSITVLRDGR 216
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
362-575 |
5.30e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.44 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEIllgniptEAFGETMTEYIGVMhqapylfrttiLNNIRI 441
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-------DRNGEVSVIAISAG-----------LSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 442 GREEASEAEVWAVLEKVGLKEMVNQLPE--GLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQ 519
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEfsELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 520 LLETFFE-ALKDKTVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPEELLatnAHYQK 575
Cdd:PRK13546 182 CLDKIYEfKEQNKTIFFVSHNLGQVrQFCTKIAWIEGGKLKDYGELDDVL---PKYEA 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-563 |
5.39e-08 |
|
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: 55.56 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 359 KKVLNDLSLT-----IPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG--------NIPTEaFGETMTEYIGVMH 425
Cdd:COG1245 348 TKSYGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqYISPD-YDGTVEEFLRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 426 QAPylFRTTILNNirigreeaseaevwAVLEKVGLKEMvnqlpegLQTMVDEaglrFSGGERHRLALARILLQDTPIVLL 505
Cdd:COG1245 427 TDD--FGSSYYKT--------------EIIKPLGLEKL-------LDKNVKD----LSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 506 DEPTTGLDpiTEQQLLET-----FFEAlKDKTVIWITHHLQgvtLMDqviFIEDGQLEMSGTP 563
Cdd:COG1245 480 DEPSAHLD--VEQRLAVAkairrFAEN-RGKTAMVVDHDIY---LID---YISDRLMVFEGEP 533
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
361-566 |
6.64e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.85 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 361 VLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNI------PTE----------AFGETMTEYiGVM 424
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnelePADrdiamvfqnyALYPHMSVR-ENM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQApylfrttiLNNIRIGREEASE--AEVWAVLEkvgLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPI 502
Cdd:PRK11650 98 AYG--------LKIRGMPKAEIEErvAEAARILE---LEPLLDRKPREL-----------SGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 256953159 503 VLLDEPTTGLDP---------ITE-QQLLETffealkdkTVIWITH-HLQGVTLMDQVIFIEDGQLEMSGTPEEL 566
Cdd:PRK11650 156 FLFDEPLSNLDAklrvqmrleIQRlHRRLKT--------TSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
483-538 |
8.43e-08 |
|
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: 51.98 E-value: 8.43e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 256953159 483 SGGERHRLALARIL----LQDTPIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITH 538
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITH 139
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
33-193 |
8.95e-08 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 53.95 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 33 LLLGFLTFFSAGALMFTSGYLISRA------ASLPENILLIYIPIVLTRAFGIGrpVFRYVERLTSHNWVLKMTSDLRLK 106
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAidaltaGTLTASQLLRYALLILLLALLIG--IFRFLWRYLIFGASRRIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 107 LYNVLEK-DAIFFKtKYRTGDILGLLSEDINHIQNLY---LRTIFPTViawILYIFLVIALGFFSWWFALcmllmlgVVV 182
Cdd:cd18541 79 LFAHLLTlSPSFYQ-KNRTGDLMARATNDLNAVRMALgpgILYLVDAL---FLGVLVLVMMFTISPKLTL-------IAL 147
|
170
....*....|.
gi 256953159 183 FLLPLVSVLVN 193
Cdd:cd18541 148 LPLPLLALLVY 158
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
340-566 |
1.40e-07 |
|
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: 54.63 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 340 PNGTSLSIehlSFAYENQekkvLNDLSLTIPEKQKLAILGRSGSGKSTLaslIRGDLRPTSGEILLGNIPTEAFGETMT- 418
Cdd:TIGR00630 609 GNGKFLTL---KGARENN----LKNITVSIPLGLFTCITGVSGSGKSTL---INDTLYPALANRLNGAKTVPGRYTSIEg 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 ------------------------EYIGVMHQAPYLFRTTILN------------NIRIGREEA---------------- 446
Cdd:TIGR00630 679 lehldkvihidqspigrtprsnpaTYTGVFDEIRELFAETPEAkvrgytpgrfsfNVKGGRCEAcqgdgvikiemhflpd 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 447 -------------------------SEAEV--WAVLEKVGLKEMVNQLPEGLQTMVDeAGLRF----------SGGERHR 489
Cdd:TIGR00630 759 vyvpcevckgkrynretlevkykgkNIADVldMTVEEAYEFFEAVPSISRKLQTLCD-VGLGYirlgqpattlSGGEAQR 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 490 LALARILLQ-DT--PIVLLDEPTTGL--DPIteQQLLETfFEALKDK--TVIWITHHLQGVTLMDQVIfieD-------- 554
Cdd:TIGR00630 838 IKLAKELSKrSTgrTLYILDEPTTGLhfDDI--KKLLEV-LQRLVDKgnTVVVIEHNLDVIKTADYII---Dlgpeggdg 911
|
330
....*....|...
gi 256953159 555 -GQLEMSGTPEEL 566
Cdd:TIGR00630 912 gGTVVASGTPEEV 924
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
354-556 |
1.54e-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: 51.88 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 354 YENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTL----ASLIRGDLRPtSGEILLGNIPTEAFGETMT-EYIGV----M 424
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLlkalANRTEGNVSV-EGDIHYNGIPYKEFAEKYPgEIIYVseedV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 425 HQAPYLFRTTIlnnirigreeaseaevwavleKVGLKEMVNQLPEGlqtmvdeaglrFSGGERHRLALARILLQDTPIVL 504
Cdd:cd03233 94 HFPTLTVRETL---------------------DFALRCKGNEFVRG-----------ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 505 LDEPTTGLDPITEQQL---LETFFEALKDKTVIWITHHLQGVT-LMDQVIFIEDGQ 556
Cdd:cd03233 142 WDNSTRGLDSSTALEIlkcIRTMADVLKTTTFVSLYQASDEIYdLFDKVLVLYEGR 197
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
353-514 |
1.73e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 353 AYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTEAfGETmTEYIGVMHQAPYLFR 432
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDR-SRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 433 T-TILNNI--------RIGREEASEAevwavLEKVGLKEMVnqlpeglQTMVDEaglrFSGGERHRLALARILLQDTPIV 503
Cdd:PRK13543 96 DlSTLENLhflcglhgRRAKQMPGSA-----LAIVGLAGYE-------DTLVRQ----LSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|.
gi 256953159 504 LLDEPTTGLDP 514
Cdd:PRK13543 160 LLDEPYANLDL 170
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
363-568 |
2.09e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 363 NDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLgnipteaFGETMT-------EYIGVMHQAPYLFRT-T 434
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL-------FGQPVDagdiatrRRVGYMSQAFSLYGElT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 435 ILNNI-------RIGREEAsEAEVWAVLEKVGLKEMVNQLPEGLqtmvdeaglrfSGGERHRLALARILLQDTPIVLLDE 507
Cdd:NF033858 356 VRQNLelharlfHLPAAEI-AARVAEMLERFDLADVADALPDSL-----------PLGIRQRLSLAVAVIHKPELLILDE 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 256953159 508 PTTGLDPITEQQlletFFEAL-----KDKTVIWITHHLQG-------VTLMDQvifiedGQLEMSGTPEELLA 568
Cdd:NF033858 424 PTSGVDPVARDM----FWRLLielsrEDGVTIFISTHFMNeaercdrISLMHA------GRVLASDTPAALVA 486
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
32-217 |
2.34e-07 |
|
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: 52.67 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 32 ALLLGFLTffsaGALMFTSGYLISRAAS---LPENILLIYIPIVLTRAFGIGRPVFRYVERLTSHNWVLKMTSDLRLKLY 108
Cdd:cd18561 1 SVLLGLLI----TALYIAQAWLLARALArifAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 109 NVLEKDAIFFKTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFALCMLLMLGVVVFLLPLV 188
Cdd:cd18561 77 AKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALW 156
|
170 180
....*....|....*....|....*....
gi 256953159 189 SVLVNGARQeKHKYAKNELYQTLTDNILG 217
Cdd:cd18561 157 DRLAKDTGR-RHWAAYGRLSAQFLDSLQG 184
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
478-566 |
4.92e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 478 AGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKD-KTVIWITHHL-QGVTLMDQVIFIEDG 555
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMeEAEQLAHELTVIDRG 220
|
90
....*....|.
gi 256953159 556 QLEMSGTPEEL 566
Cdd:NF000106 221 RVIADGKVDEL 231
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
325-513 |
4.94e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 325 ELPEGEDdsteapvQPNGTSLSIEHLSFAYENQeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEIL 404
Cdd:PLN03073 496 EFPTPDD-------RPGPPIISFSDASFGYPGG-PLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 405 LG-NIPTEAFGETMTEYIGvMHQAPYLFRTTILNNIrigreeaSEAEVWAVLEKVGLKEMVnqlpeGLQTMvdeagLRFS 483
Cdd:PLN03073 568 RSaKVRMAVFSQHHVDGLD-LSSNPLLYMMRCFPGV-------PEQKLRAHLGSFGVTGNL-----ALQPM-----YTLS 629
|
170 180 190
....*....|....*....|....*....|
gi 256953159 484 GGERHRLALARILLQDTPIVLLDEPTTGLD 513
Cdd:PLN03073 630 GGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
33-184 |
7.64e-07 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 50.89 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 33 LLLGFLTFFSAGALMFTSGYLISRA------ASLPENILLIYIPIVltrAFGIGRPVFRYVERLTSHNWVLKMTSDLRLK 106
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIidsvigGGLRELLWLLALLIL---GVALLRGVFRYLQGYLAEKASQKVAYDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 107 LYNVLEK-DAIFFKtKYRTGDILGLLSEDINHIQNLY---LRTIFPTViawILYIFLVIALGFFSWWFALCMLLMLGVVV 182
Cdd:cd18542 78 LYDHLQRlSFSFHD-KARTGDLMSRCTSDVDTIRRFLafgLVELVRAV---LLFIGALIIMFSINWKLTLISLAIIPFIA 153
|
..
gi 256953159 183 FL 184
Cdd:cd18542 154 LF 155
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
483-578 |
1.32e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 483 SGGERHRLALARILLQDTP---IVLLDEPTTGLDPITEQQLLETFFeALKDK--TVIWITHHLQGVTLMDQVIFI----- 552
Cdd:PRK00635 811 SGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQ-SLTHQghTVVIIEHNMHVVKVADYVLELgpegg 889
|
90 100
....*....|....*....|....*..
gi 256953159 553 -EDGQLEMSGTPEELLATNAHYQKLYR 578
Cdd:PRK00635 890 nLGGYLLASCSPEELIHLHTPTAKALR 916
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
360-556 |
1.32e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 360 KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNIPTE--AFGETMTEYIGVMHQAPYLFR-TTIL 436
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfkSSKEALENGISMVHQELNLVLqRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 437 NNIRIGR---------EEASEAEVWAVLEKVGL----KEMVNQLPEGLQTMVDeaglrfsggerhrlaLARILLQDTPIV 503
Cdd:PRK10982 92 DNMWLGRyptkgmfvdQDKMYRDTKAIFDELDIdidpRAKVATLSVSQMQMIE---------------IAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 504 LLDEPTTGLdpiTEQQL--LETFFEALKDK--TVIWITHHLQGV-TLMDQVIFIEDGQ 556
Cdd:PRK10982 157 IMDEPTSSL---TEKEVnhLFTIIRKLKERgcGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
471-573 |
1.95e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.80 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 471 LQTMVDeAGLRF----------SGGERHRLALARILLQ-DTP--IVLLDEPTTGL--DPIteQQLLEtFFEALKDK--TV 533
Cdd:COG0178 807 LQTLQD-VGLGYiklgqpattlSGGEAQRVKLASELSKrSTGktLYILDEPTTGLhfHDI--RKLLE-VLHRLVDKgnTV 882
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 256953159 534 IWITHHLQGVTLMDQVIfieD---------GQLEMSGTPEELLATNAHY 573
Cdd:COG0178 883 VVIEHNLDVIKTADWII---DlgpeggdggGEIVAEGTPEEVAKVKASY 928
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
345-578 |
2.30e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.80 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLSFAYENQEK--KVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRG----DLRPTSGEILLGNIpteafgetmt 418
Cdd:PRK15093 4 LDIRNLTIEFKTSDGwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADRMRFDDI---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 419 eyiGVMHQAPYLFRTTILNNI---------------RIGREEASEAEVWA------------------VLEKVGLKE--- 462
Cdd:PRK15093 74 ---DLLRLSPRERRKLVGHNVsmifqepqscldpseRVGRQLMQNIPGWTykgrwwqrfgwrkrraieLLHRVGIKDhkd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 463 MVNQLPEGLqtmvdeaglrfSGGERHRLALArILLQDTPIVLL-DEPTTGLDPITEQQL--LETFFEALKDKTVIWITHH 539
Cdd:PRK15093 151 AMRSFPYEL-----------TEGECQKVMIA-IALANQPRLLIaDEPTNAMEPTTQAQIfrLLTRLNQNNNTTILLISHD 218
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 256953159 540 LQGVT-LMDQVIFIEDGQLEMSGTPEELLATNAH--YQKLYR 578
Cdd:PRK15093 219 LQMLSqWADKINVLYCGQTVETAPSKELVTTPHHpyTQALIR 260
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
361-513 |
2.85e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 361 VLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG--------NIPTEAFGETMTEYI--GVMHQAPYL 430
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPgnwqlawvNQETPALPQPALEYVidGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 431 FRTTILNNIRIGREEASEAEVWAVLEKVGLKEMVNQLPEGL---QTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDE 507
Cdd:PRK10636 96 AQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
....*.
gi 256953159 508 PTTGLD 513
Cdd:PRK10636 176 PTNHLD 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
372-539 |
2.88e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.37 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 372 KQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGNipteafGETMTEYIGVmhqapylfrttilnnirigreeaseaev 451
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID------GEDILEEVLD---------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 452 wavlekvglkemvnqlpEGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEAL--- 528
Cdd:smart00382 48 -----------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLlll 110
|
170
....*....|....*
gi 256953159 529 ----KDKTVIWITHH 539
Cdd:smart00382 111 lkseKNLTVILTTND 125
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
483-569 |
3.71e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 483 SGGERHRLALARILLQDTPIV--LLDEPTTGLDPITEQQLLETfFEALKDK--TVIWITHHLQGVTLMDQVIFIE----- 553
Cdd:PRK00635 478 SGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINV-IKKLRDQgnTVLLVEHDEQMISLADRIIDIGpgagi 556
|
90
....*....|....*..
gi 256953159 554 -DGQLEMSGTPEELLAT 569
Cdd:PRK00635 557 fGGEVLFNGSPREFLAK 573
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
373-543 |
6.58e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 373 QKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG-----NIPTEAFgETMTEYIGVMHQAPYLF---RTTILNNI----- 439
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridTLSPGKL-QALRRDIQFIFQDPYASldpRQTVGDSImeplr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 440 --RIGREEASEAEVWAVLEKVGLKemvnqlPEGLQTMVDEaglrFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITE 517
Cdd:PRK10261 430 vhGLLPGKAAAARVAWLLERVGLL------PEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
|
170 180
....*....|....*....|....*...
gi 256953159 518 QQLLETFFEALKDKTV--IWITHHLQGV 543
Cdd:PRK10261 500 GQIINLLLDLQRDFGIayLFISHDMAVV 527
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
337-569 |
9.12e-06 |
|
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: 48.28 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 337 PVQPNGTS---LSIEHLSfAYE--NQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPT-SGEILL----- 405
Cdd:TIGR02633 247 PHEPHEIGdviLEARNLT-CWDviNPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFIngkpv 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 406 -----------------------GNIPTEAFGETMTeyIGVMHQapYLFRTTIlnnirigREEASEAEVWAVLEKVGLKE 462
Cdd:TIGR02633 326 dirnpaqairagiamvpedrkrhGIVPILGVGKNIT--LSVLKS--FCFKMRI-------DAAAELQIIGSAIQRLKVKT 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 463 MVNQLPEGlqtmvdeaglRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITHHLQ 541
Cdd:TIGR02633 395 ASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELA 464
|
250 260 270
....*....|....*....|....*....|....
gi 256953159 542 GVT-LMDQVIFIEDGQLEMSG-----TPEELLAT 569
Cdd:TIGR02633 465 EVLgLSDRVLVIGEGKLKGDFvnhalTQEQVLAA 498
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
336-513 |
9.78e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 336 APVQPNGTSLSIEHLSFAyENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLGnipteafGE 415
Cdd:COG3845 249 APAEPGEVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD-------GE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 416 TMTeyigvmHQAPYLFRT-------------------TILNNIRIGREEASEAEVWAVLEKVGLKEMVNQL-------PE 469
Cdd:COG3845 321 DIT------GLSPRERRRlgvayipedrlgrglvpdmSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELieefdvrTP 394
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 256953159 470 GLQTMVDeaglRFSGGERHRLALARILLQDTPIVLLDEPTTGLD 513
Cdd:COG3845 395 GPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
362-577 |
1.03e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 362 LNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEillgnipteafgetmteyIGVMHQAPYLFRTTILNNIRI 441
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT------------------VDIKGSAALIAISSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 442 GREEASEAEVWAVLEKVGLKEMVNQLPE--GLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQ 519
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEfaDIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 520 LLETFFE-ALKDKTVIWITHHLQGV-TLMDQVIFIEDGQLEMSGTPEELLATNAHYQKLY 577
Cdd:PRK13545 182 CLDKMNEfKEQGKTIFFISHSLSQVkSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKY 241
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
51-218 |
1.08e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 47.53 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 51 GYLISRAASLPENI-LLIYIPIVLTRAFgIGRPVFRYVERLTSHNWVLKMTSDLRLKLYNVLEKDAI-FFKTKyRTGDIL 128
Cdd:cd18778 23 RELVDLVTIGSKSLgLLLGLALLLLGAY-LLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLrYFDDR-QTGDLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 129 GLLSEDINHIQNLYLRTIfPTVIAWILYIFLVIALGFF-SWWFALCMLLMLGVVVFLLPLVSVLVNGARQEKHKyAKNEL 207
Cdd:cd18778 101 SRVINDVANVERLIADGI-PQGITNVLTLVGVAIILFSiNPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVRE-ALGEL 178
|
170
....*....|.
gi 256953159 208 YQTLTDNILGV 218
Cdd:cd18778 179 NALLQDNLSGI 189
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
367-513 |
1.54e-05 |
|
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: 46.59 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 367 LTIP-EKQKLAILGRSGSGKSTLASLIRGDLRPTsgeilLGNIPTE-AFGETMTEYIGVMHQApylFRTTILN-NIRIGR 443
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPN-----LGKFDDPpDWDEILDEFRGSELQN---YFTKLLEgDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 444 E--------EASEAEVWAVLEKVG----LKEMVNQLpeGLQTMVDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTG 511
Cdd:cd03236 92 KpqyvdlipKAVKGKVGELLKKKDergkLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
..
gi 256953159 512 LD 513
Cdd:cd03236 170 LD 171
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
483-568 |
2.67e-05 |
|
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: 47.32 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 483 SGGERHRLALARILLQDTPIVL--LDEPTTGLDPITEQQLLETfFEALKDK--TVIWITHHLQGVTLMDQVIFI------ 552
Cdd:TIGR00630 490 SGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINT-LKRLRDLgnTLIVVEHDEDTIRAADYVIDIgpgage 568
|
90
....*....|....*.
gi 256953159 553 EDGQLEMSGTPEELLA 568
Cdd:TIGR00630 569 HGGEVVASGTPEEILA 584
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
29-185 |
3.60e-05 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 45.88 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 29 LYFALLLGFLTFFSAGALMFTSGYLISRAASLPENILLIYIPIVLTRAFGIgRPVFRYVERLTShNWV-LKMTSDLRLKL 107
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLL-RGLASYLQTYLM-AYVgQRVVRDLRNDL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 108 YN-VLEKDAIFFkTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFALCMLLMLGVVVFLL 185
Cdd:cd18552 79 FDkLLRLPLSFF-DRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
345-572 |
3.91e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 345 LSIEHLS--FAYENQEKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRG------------------DLRPTSGE-- 402
Cdd:PRK11022 4 LNVDKLSvhFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidypgrvmaeklefngqDLQRISEKer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 403 -ILLGNIPTEAFGETMT-------------EYIGVmHQApylfrttilNNIRIGREEASEaevwaVLEKVGLKEMVNQLp 468
Cdd:PRK11022 84 rNLVGAEVAMIFQDPMTslnpcytvgfqimEAIKV-HQG---------GNKKTRRQRAID-----LLNQVGIPDPASRL- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 469 eglqtmvDEAGLRFSGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDK--TVIWITHHLQGVT-L 545
Cdd:PRK11022 148 -------DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAeA 220
|
250 260
....*....|....*....|....*..
gi 256953159 546 MDQVIFIEDGQLEMSGTPEELLATNAH 572
Cdd:PRK11022 221 AHKIIVMYAGQVVETGKAHDIFRAPRH 247
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
31-184 |
6.47e-05 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 45.17 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 31 FALLLGFLTFFSAGALMftsGYLISRAASLPENILLIYIPIVLTRAFGIgRPVFRYVERLTSHNWVLKMTSDLRLKLYNV 110
Cdd:cd18576 3 ILLLLSSAIGLVFPLLA---GQLIDAALGGGDTASLNQIALLLLGLFLL-QAVFSFFRIYLFARVGERVVADLRKDLYRH 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 256953159 111 LEKDAIFFKTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFALCMLLMLGVVVFL 184
Cdd:cd18576 79 LQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLV 152
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
98-184 |
7.97e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 44.81 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 98 KMTSDLRLKLYNVLEKDAIFFKTKYRTGDILGLLSEDINHIQNlYLRTIFPTVIAWILYIFLVIALGFF-SWWFALCMLL 176
Cdd:cd18563 73 RITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQD-FLSDGLPDFLTNILMIIGIGVVLFSlNWKLALLVLI 151
|
....*...
gi 256953159 177 MLGVVVFL 184
Cdd:cd18563 152 PVPLVVWG 159
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
31-188 |
9.27e-05 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 44.71 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 31 FALLLGFLTFFSAGALmftsGYLISRAASLPENILLIYIPIVLTRAFGIGRPVFRYVERLTSHNWVLKMTSDLRLKLYNV 110
Cdd:cd18584 4 LGLLAALLIIAQAWLL----ARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLAR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 111 LEKDAIFFKTKYRTGDILGLLSEDINHIQNlYLRTIFPTVIAWILY-IFLVIALGFFSWWFALCMLLMLGVVVFLLPLV 188
Cdd:cd18584 80 LLALGPALLRRQSSGELATLLTEGVDALDG-YFARYLPQLVLAAIVpLLILVAVFPLDWVSALILLVTAPLIPLFMILI 157
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
482-538 |
1.31e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 482 FSGGERHRLALARILLQDTPIVLLDEPTTGLDpITEQQLLETFFeaLK-DKTVIWITH 538
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLD-LHAVLWLETYL--LKwPKTFIVVSH 399
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
471-573 |
1.42e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.06 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 471 LQTMVDeAGLRF----------SGGERHRLALARILL-QDT--PIVLLDEPTTGL--DPIteQQLLETfFEALKDK--TV 533
Cdd:PRK00349 811 LQTLVD-VGLGYiklgqpattlSGGEAQRVKLAKELSkRSTgkTLYILDEPTTGLhfEDI--RKLLEV-LHRLVDKgnTV 886
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 256953159 534 IWITHHLqgvtlmDqVI----FIED---------GQLEMSGTPEELLATNAHY 573
Cdd:PRK00349 887 VVIEHNL------D-VIktadWIIDlgpeggdggGEIVATGTPEEVAKVEASY 932
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
328-513 |
1.74e-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: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 328 EGEDDSTEAPVQPNGTSLSIEHLSFayenqeKKVLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPTSGEILLG- 406
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVLEVEGLSV------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDg 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 407 ---NI--PTEAfgetMTEYIG-----------VMHQapylfrtTILNNI------RIGR-------EEASEAEvwAVLEK 457
Cdd:COG1129 314 kpvRIrsPRDA----IRAGIAyvpedrkgeglVLDL-------SIRENItlasldRLSRgglldrrRERALAE--EYIKR 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 458 VGLKemvnqlPEGLQTMVDEaglrFSGGERHRLALARILLQDTPIVLLDEPTTGLD 513
Cdd:COG1129 381 LRIK------TPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
449-577 |
1.82e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 449 AEVWAVLEKVglkemvnQLPegLQTMVDeAGLRF----------SGGERHRLALARILLQ--DTP-IVLLDEPTTGLDPI 515
Cdd:PRK00635 1667 AETFPFLKKI-------QKP--LQALID-NGLGYlplgqnlsslSLSEKIAIKIAKFLYLppKHPtLFLLDEIATSLDNQ 1736
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 516 TEQQLLETFFEAL-KDKTVIWITHHLQGVTLMDQVIFI------EDGQLEMSGTPEELLATNAHYQKLY 577
Cdd:PRK00635 1737 QKSALLVQLRTLVsLGHSVIYIDHDPALLKQADYLIEMgpgsgkTGGKILFSGPPKDISASKDSLLKTY 1805
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
71-184 |
2.86e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 43.32 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 71 IVLTRAFGIGRPVFRYVERLTSHNWVLKMTSDLRLKLYNVLEK-DAIFFKTKyRTGDILGLLSEDINHIQNLYLRTIfpT 149
Cdd:cd18565 57 GGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRlDMAFFEDR-QTGDLMSVLNNDVNQLERFLDDGA--N 133
|
90 100 110
....*....|....*....|....*....|....*..
gi 256953159 150 VIAWILYIFLVIALGFF--SWWFALCMLLMLGVVVFL 184
Cdd:cd18565 134 SIIRVVVTVLGIGAILFylNWQLALVALLPVPLIIAG 170
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
99-270 |
2.95e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 43.24 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 99 MTSDLRLKLYNVLEKDAIFFKTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFALCMLLML 178
Cdd:cd18550 70 VMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 179 gvVVFLLPLVSVlvnGARQEKHKYAKNELYQTLTDNI---LGVSDWVFSQ---RGSEFVARYETDEANVRALDekMKQFN 252
Cdd:cd18550 150 --PLFVLPTRRV---GRRRRKLTREQQEKLAELNSIMqetLSVSGALLVKlfgREDDEAARFARRSRELRDLG--VRQAL 222
|
170 180
....*....|....*....|
gi 256953159 253 RGRDF--VLQLLFGVIAIAV 270
Cdd:cd18550 223 AGRWFfaALGLFTAIGPALV 242
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
480-580 |
3.03e-04 |
|
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: 41.79 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 480 LRFSGGERHRLALARILLQDTPIVLLDEPTTGLDpiTEQQL-----LETFFEALKdKTVIWITHHLQGVTLMDQVIFIED 554
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD--IEQRLnaaraIRRLSEEGK-KTALVVEHDLAVLDYLSDRIHVFE 146
|
90 100
....*....|....*....|....*....
gi 256953159 555 GQLEMSGT---PEELLATNAHYQKLYRID 580
Cdd:cd03222 147 GEPGVYGIasqPKGTREGINRFLRGYLIT 175
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
376-513 |
4.66e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 376 AILGRSGSGKSTLASLIRGdlRPTSGEILlGNIPTEAF---GETMTEYIGV-----MHQAPYLFRTTILNN--IRIGREE 445
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFpkkQETFARISGYceqndIHSPQVTVRESLIYSafLRLPKEV 986
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 256953159 446 ASEAEVWAVLEKVGLKEMVNqLPEGLQTMVDEAGLrfSGGERHRLALARILLQDTPIVLLDEPTTGLD 513
Cdd:PLN03140 987 SKEEKMMFVDEVMELVELDN-LKDAIVGLPGVTGL--STEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
467-539 |
5.82e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 467 LPEGLQTMvdeaglrfSGGERH------RLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFEALKDKT----VIWI 536
Cdd:PRK01156 795 MVEGIDSL--------SGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipqVIMI 866
|
...
gi 256953159 537 THH 539
Cdd:PRK01156 867 SHH 869
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
76-204 |
8.13e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 41.69 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 76 AFGIGRPVFRYVErLTSHNWV-LKMTSDLRLKLYN-VLEKDAIFFkTKYRTGDILGLLSEDINHIQNlylrTI---FPTV 150
Cdd:cd18577 55 YLGIGSFVLSYIQ-TACWTITgERQARRIRKRYLKaLLRQDIAWF-DKNGAGELTSRLTSDTNLIQD----GIgekLGLL 128
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 256953159 151 IAWILYIFLVIALGF-FSWWFALCMLLMLGVVVFLLPLVSVLVNG-ARQEKHKYAK 204
Cdd:cd18577 129 IQSLSTFIAGFIIAFiYSWKLTLVLLATLPLIAIVGGIMGKLLSKyTKKEQEAYAK 184
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
361-568 |
1.26e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 361 VLNDLSLTIPEKQKLAILGRSGSGKSTLASLIRGDLRPT---SGEILLGN------IP--TEAFGETMTEYIGVMHQAPY 429
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGyrlnefVPrkTSAYISQNDVHVGVMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 430 L----------FRTTILNNIRIGREEAS---EAEVWAVLEKVGLKEMVNQLPE-------GLQ----TMVDEAGLR-FSG 484
Cdd:PLN03140 260 LdfsarcqgvgTRYDLLSELARREKDAGifpEAEVDLFMKATAMEGVKSSLITdytlkilGLDickdTIVGDEMIRgISG 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 485 GERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLetffealkdKTVIWITHHLQGVTLM-------------DQVIF 551
Cdd:PLN03140 340 GQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIV---------KCLQQIVHLTEATVLMsllqpapetfdlfDDIIL 410
|
250
....*....|....*..
gi 256953159 552 IEDGQLEMSGTPEELLA 568
Cdd:PLN03140 411 LSEGQIVYQGPRDHILE 427
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
118-272 |
4.18e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 39.43 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 118 FKTKYRTGDILGLLS--EDINHIQNLYLRTIFPTVIAwilyifLVIALGFFSWWFALCMLLMLGVVVFLLPLVSVLVNGA 195
Cdd:cd18583 87 FHDSKKSGEVLKAIEqgSSINDLLEQILFQIVPMIID------LVIAIVYLYYLFDPYMGLIVAVVMVLYVWSTIKLTSW 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 196 RQEKHKY---AKNELYQTLTDNILG---VSdwVFSQRGSEfVARYEtdeanvRALDEKMK---QFNRGRDF--VLQ---L 261
Cdd:cd18583 161 RTKLRRDmidADREERSILTESLLNwetVK--YFNREPYE-KERYR------EAVKNYQKaerKYLFSLNLlnAVQsliL 231
|
170
....*....|.
gi 256953159 262 LFGVIAIAVLA 272
Cdd:cd18583 232 TLGLLAGCFLA 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
483-557 |
5.07e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 5.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 256953159 483 SGGERHRLALARILLQDTPIVLLDEPTTGLDPITEQQLLETFFE-ALKDKTVIWITH---HLQGVTlmDQVIFIEDGQL 557
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSempELLGIT--DRILVMSNGLV 469
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
30-192 |
5.18e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 39.08 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 30 YFALLLGFLTFFS---AGALMFTSGYLISRAASLPENILLIYIPIVLTrafgigrPVFRYVERLTSHNWVLKMTSDLRLK 106
Cdd:cd18557 2 LLFLLISSAAQLLlpyLIGRLIDTIIKGGDLDVLNELALILLAIYLLQ-------SVFTFVRYYLFNIAGERIVARLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 107 LY-NVLEKDAIFFKtKYRTGDILGLLSEDINHIQNlylrtIFPTVIAWILyIFLVIALGffswwfALCMLLMLGVVVFLL 185
Cdd:cd18557 75 LFsSLLRQEIAFFD-KHKTGELTSRLSSDTSVLQS-----AVTDNLSQLL-RNILQVIG------GLIILFILSWKLTLV 141
|
....*..
gi 256953159 186 PLVSVLV 192
Cdd:cd18557 142 LLLVIPL 148
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
98-191 |
8.78e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 38.65 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 256953159 98 KMTSDLRLKLYNVLEKDAIFFKTKYRTGDILGLLSEDINHIQNLYLRTIFPTVIAWILYIFLVIALGFFSWWFAlcmLLM 177
Cdd:cd18564 84 RVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLA---LIA 160
|
90
....*....|....
gi 256953159 178 LGVVVFLLPLVSVL 191
Cdd:cd18564 161 LAVAPLLLLAARRF 174
|
|
| |
