|
Name |
Accession |
Description |
Interval |
E-value |
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-570 |
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: 643.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 6 WILPYIKQNARLFVLVIFLGAVTIFSAAFLMFTSGFLISKAATRPEnILLIYVPIVAVRTFGIARSVSRYVERLVGHHII 85
Cdd:COG4987 5 RLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGWLIAAAALAPP-ILNLFVPIVGVRAFAIGRTVFRYLERLVSHDAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 86 LKIVSDMRVRLYNMLEPGALMLRSRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAILIAL 165
Cdd:COG4987 84 LRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 166 YLFVLVVLFPVVSLLVTRARNAKLKSGRNVLYSRLTDAVMGVSDWMFSGRRHAFIDAYEKEEHDWFELERKKQRFTRWRD 245
Cdd:COG4987 164 GLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 246 FAAQCLVAGLILLMLFWTAGQQADGELAKTMIAAFVLVVFPLTEAFLPLSDALGEVPGYQDSIKRMNRVAPQPEASqTES 325
Cdd:COG4987 244 ALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAV-TEP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 326 GAQTLDLQDVTLSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TAL 403
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlRDL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 404 LKDQIADAVAVLNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIAL 483
Cdd:COG4987 403 DEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLAL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANER 563
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
....*..
gi 2218266673 564 YRRLYHL 570
Cdd:COG4987 563 YRQLYQR 569
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-531 |
0e+00 |
|
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: 564.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 6 WILPYIKQNARLFVLVIFLGAVTIFSAAFLMFTSGFLISKAATRPEnILLIYVPIVAVRTFGIARSVSRYVERLVGHHII 85
Cdd:TIGR02868 3 RILPLLKPRRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPP-VLYLSVAAVAVRAFGIGRAVFRYLERLVGHDAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 86 LKIVSDMRVRLYNMLEPGALMLRSRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAILIAL 165
Cdd:TIGR02868 82 LRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 166 YLFVLVVLFPVVSLLVTRARNAKLKSGRNVLYSRLTDAVMGVSDWMFSGRRHAFIDAYEKEEHDWFELERKKQRFTRWRD 245
Cdd:TIGR02868 162 GLLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 246 fAAQCLVAGLILLMLFWTAGQQ-ADGELAKTMIAAFVLVVFPLTEAFLPLSDALGEVPGYQDSIKRMNRV--APQPEASQ 322
Cdd:TIGR02868 242 -ALTLLAAGLAVLGALWAGGPAvADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVldAAGPVAEG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 323 TESGAQTLDLQDVTLSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-T 401
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPvS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 402 ALLKDQIADAVAVLNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRI 481
Cdd:TIGR02868 401 SLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRL 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2218266673 482 ALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHL 531
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-570 |
5.49e-123 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 374.12 E-value: 5.49e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 1 MKKEEW-----ILPYIKQNARLFVLVIFLGAVTIFSAAFLMFTSGFLISKAATRPENILLIYVPIVAVrTFGIARSVSRY 75
Cdd:COG1132 1 MSKSPRkllrrLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLL-GLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 76 VERLVGHHIILKIVSDMRVRLYnmlepgALMLR------SRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSV 149
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLF------EHLLRlplsffDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 150 IALGFFSWPFAIL------IALYLFVLVVLFPVVSLLVTRARNAKLksgrnvlYSRLTDAVMGVSDW-MFsGRRHAFIDA 222
Cdd:COG1132 154 VVLFVIDWRLALIvllvlpLLLLVLRLFGRRLRKLFRRVQEALAEL-------NGRLQESLSGIRVVkAF-GREERELER 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 223 YEKEEHDWFELERKKQRFTRWRDFAAQCLVAGLILLMLFWTAGQQADGELAKTMIAAFVLVVFPLTEAFLPLSDALGEVP 302
Cdd:COG1132 226 FREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 303 GYQDSIKRMNRVAPQPEASQTESGAQTLDLQDVTLSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLAL 382
Cdd:COG1132 306 RALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 383 IEGALKPDSGSVTLNGVETA-LLKDQIADAVAVLNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDG 461
Cdd:COG1132 386 LLRFYDPTSGRILIDGVDIRdLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 462 YHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIV 541
Cdd:COG1132 466 YDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRIL 545
|
570 580
....*....|....*....|....*....
gi 2218266673 542 FLENGKTEMEGTHEELLAANERYRRLYHL 570
Cdd:COG1132 546 VLDDGRIVEQGTHEELLARGGLYARLYRL 574
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
337-552 |
1.45e-96 |
|
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: 291.91 E-value: 1.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVL 415
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLFDTSILNNIrlgngeasdedvrraakqvklhdyieslpdgyhtsvqetGIRFSGGERQRIALARILLQDTPIII 495
Cdd:cd03247 81 NQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 496 LDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEG 552
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-568 |
3.98e-94 |
|
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: 302.91 E-value: 3.98e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 6 WILPYIKQNARLFVLVIFLG-AVTIFSAAFLMFTsGFLISKAATRpENILLIYVPIVAVRTFGIARSVSRYVERLVGHHI 84
Cdd:COG2274 146 WFLRLLRRYRRLLLQVLLASlLINLLALATPLFT-QVVIDRVLPN-QDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 85 ILKIVSDMRVRLYNMLepgaLMLRSRFR----TGDMLGILSeDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFA 160
Cdd:COG2274 224 GQRIDLRLSSRFFRHL----LRLPLSFFesrsVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 161 ----ILIALYLFVLVVLFPVVSLLVTRARNAKLKsgrnvLYSRLTDAVMGVSDWMFSGRRHAFIDAYEKEEHDWFELERK 236
Cdd:COG2274 299 lvvlLLIPLYVLLGLLFQPRLRRLSREESEASAK-----RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFK 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 237 KQRFTRWRDFAAQCLVAGLILLMLFWTAGQQADGELAKTMIAAFVLVVFPLTEAFLPLSDALGEvpgYQD---SIKRMNR 313
Cdd:COG2274 374 LRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQR---FQDakiALERLDD 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 314 VAPQPEASQTESGAQTLDLQDVTLSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSG 392
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 393 SVTLNGVETALL-KDQIADAVAVLNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGI 471
Cdd:COG2274 531 RILIDGIDLRQIdPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 472 RFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEME 551
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
570
....*....|....*..
gi 2218266673 552 GTHEELLAANERYRRLY 568
Cdd:COG2274 691 GTHEELLARKGLYAELV 707
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-561 |
7.10e-94 |
|
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: 298.21 E-value: 7.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 6 WILPYIKQNARLFVLVIFLGAVTIFSAAFLMFTSGFLISKAATRPENILLIYVPIVAVRTFGIARSVSRYVERLVGHHII 85
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 86 LKIVSDMRVRLYNMLEPGALMLRSRFRTGDMLGILSEDIEHLqDAFLKTIFPA-ISALLLYAVSVIALGFFSWP------ 158
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEAL-DGYFARYLPQlFLAALVPLLILVAVFPLDWLsglill 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 159 --------FAILIALylfvlvvlfpvvsllVTRARNAKLKSGRNVLYSRLTDAVMGVSDWMFSGRrhafidayEKEEHDw 230
Cdd:COG4988 166 vtapliplFMILVGK---------------GAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGR--------AKAEAE- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 231 fELERKKQRFTRwR---------------DFAAQ---CLVAGLILLMLFWtagqqadGELakTMIAA-FVLVVFPltEAF 291
Cdd:COG4988 222 -RIAEASEDFRK-RtmkvlrvaflssavlEFFASlsiALVAVYIGFRLLG-------GSL--TLFAAlFVLLLAP--EFF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 292 LPLSDaLGEVpgYQDS------IKRMNRVAPQPEASQTESGAQTLDLQDVTLSFRDVTFSYDNSSQVLDNFSFTLRQGEK 365
Cdd:COG4988 289 LPLRD-LGSF--YHARangiaaAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGER 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 366 MALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADAVAVLNQKPHLFDTSILNNIRLGNGEASDEDVRR 444
Cdd:COG4988 366 VALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDlSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 445 AAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTI 524
Cdd:COG4988 446 ALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV 525
|
570 580 590
....*....|....*....|....*....|....*..
gi 2218266673 525 LWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAAN 561
Cdd:COG4988 526 ILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-569 |
1.10e-92 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 295.58 E-value: 1.10e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 7 ILPYIK----QNARLFvLVIFLGAVTIFSAAFLMFTSGFLISKAATRPENILLIY---VPIVAVRTFGIARSVSRYVERL 79
Cdd:PRK11160 4 LLPFLKlykrHWFMLS-LGILLAIVTLLASIGLLTLSGWFLSASAVAGLAGLYSFnymLPAAGVRGAAIGRTAGRYGERL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 80 VGHHIILKIVSDMRVRLYNMLEP---GALmlrSRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFS 156
Cdd:PRK11160 83 VSHDATFRVLTHLRVFTFSKLLPlspAGL---ARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 157 WPFAILIALYLFVLVVLFPVVSLLVTRARNAKLKSGRNVLYSRLTDAVMGVSDWMFSGRRHAFIDAYEKEEHDWFELERK 236
Cdd:PRK11160 160 LTLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 237 KQRFTrwrDFAAQCLVA--GLILLMLFWTAGQQ-ADGELAKTMIAAFVLVVFPLTEAFLPLSDA---LGEVPGyqdSIKR 310
Cdd:PRK11160 240 QANLT---GLSQALMILanGLTVVLMLWLAAGGvGGNAQPGALIALFVFAALAAFEALMPVAGAfqhLGQVIA---SARR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 311 MNRVAPQpEASQTESGAQTLDLQDVTLSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKP 389
Cdd:PRK11160 314 INEITEQ-KPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 390 DSGSVTLNGVE-TALLKDQIADAVAVLNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESlPDGYHTSVQE 468
Cdd:PRK11160 393 QQGEILLNGQPiADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 469 TGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKT 548
Cdd:PRK11160 472 GGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
570 580
....*....|....*....|.
gi 2218266673 549 EMEGTHEELLAANERYRRLYH 569
Cdd:PRK11160 552 IEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
337-569 |
1.61e-77 |
|
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: 244.83 E-value: 1.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIADAVAVL 415
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTlDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIII 495
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 496 LDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRLYH 569
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
337-568 |
3.34e-76 |
|
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: 241.37 E-value: 3.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDN-SSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIADAVAV 414
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPII 494
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 495 ILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRLY 568
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
339-570 |
4.87e-75 |
|
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: 238.59 E-value: 4.87e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 339 FRDVTFSYDN--SSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVET-----ALLKDQIAda 411
Cdd:cd03249 3 FKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdlnlRWLRSQIG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 vaVLNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDT 491
Cdd:cd03249 81 --LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 492 PIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRLYHL 570
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
339-561 |
1.99e-69 |
|
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: 223.64 E-value: 1.99e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 339 FRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADAVAVLNQ 417
Cdd:cd03254 5 FENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDiRDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 418 KPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILD 497
Cdd:cd03254 85 DTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 498 EPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAAN 561
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-570 |
2.21e-69 |
|
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: 234.71 E-value: 2.21e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 6 WILPYIKQNARLFVLVIFLGAVTIFSAAFLMFTSGFLISKAATRPENILLIYVPIVAVRTFGIARSVSRYVERL------ 79
Cdd:COG5265 24 LLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAYGLLRLLSVLFGELrdalfa 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 80 -VGHHIILKIVSDMRVRLYnmlepgALMLR---SRfRTGDmlgiLSEDIEH-------LQDAFLKTIFPAISALLLyaVS 148
Cdd:COG5265 104 rVTQRAVRRLALEVFRHLH------ALSLRfhlER-QTGG----LSRDIERgtkgiefLLRFLLFNILPTLLEIAL--VA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 149 VIALGFFSWPFA--ILIALylfvlvvlfpvvsllvtrarnaklksgrnVLYSRLTdavMGVSDWMFSGRRHA-------- 218
Cdd:COG5265 171 GILLVKYDWWFAliTLVTV-----------------------------VLYIAFT---VVVTEWRTKFRREMneadsean 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 219 --FIDA---YE--K----EEHdwfELERKKQRFTRWRDFA------------AQCLV--AGLILLMlfWTAGQQ-ADGEL 272
Cdd:COG5265 219 trAVDSllnYEtvKyfgnEAR---EARRYDEALARYERAAvksqtslallnfGQALIiaLGLTAMM--LMAAQGvVAGTM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 273 aktMIAAFVLVVFPLTEAFLPLSdALGEVpgYQDsIK-------RMNRVAPQPEASQTESGAQTLDLQDVTLSFRDVTFS 345
Cdd:COG5265 294 ---TVGDFVLVNAYLIQLYIPLN-FLGFV--YRE-IRqaladmeRMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 346 YDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADAVAVLNQKPHLFDT 424
Cdd:COG5265 367 YDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDiRDVTQASLRAAIGIVPQDTVLFND 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 425 SILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLD 504
Cdd:COG5265 447 TIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 505 PITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRLYHL 570
Cdd:COG5265 527 SRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWAR 592
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-543 |
3.60e-66 |
|
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: 224.47 E-value: 3.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 16 RLFVLVIFLGAVTIFSAAFLMftsGFLISKAATRPENILLIYVPIVAVRTFGIARSVSRYVERLVGHHIILKIVSDMRVR 95
Cdd:TIGR02857 6 ALLALLGVLGALLIIAQAWLL---ARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 96 LYN-MLEPGALMLRSRfRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAILIALyLFVLVVLF 174
Cdd:TIGR02857 83 LLEaVAALGPRWLQGR-PSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLL-TAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 175 PVVSLLVTRARNAKLKSGRNVLYSRLTDAVMGVSDWMFSGRRHAFIDAYEKEEHdwfELERKKQRFTRWR-------DFA 247
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSE---EYRERTMRVLRIAflssavlELF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 248 AQCLVA------GLILL---MLFWTAgqqadgelaktmiaAFVLVVFPltEAFLPLSDaLGEVpgYQDsikRMNRVA--- 315
Cdd:TIGR02857 238 ATLSVAlvavyiGFRLLagdLDLATG--------------LFVLLLAP--EFYLPLRQ-LGAQ--YHA---RADGVAaae 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 316 ---------PQPEASQTESGAqtldLQDVTLSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGA 386
Cdd:TIGR02857 296 alfavldaaPRPLAGKAPVTA----APASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 387 LKPDSGSVTLNGVETA-LLKDQIADAVAVLNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTS 465
Cdd:TIGR02857 372 VDPTEGSIAVNGVPLAdADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTP 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 466 VQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFL 543
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-568 |
3.07e-65 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 223.05 E-value: 3.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 7 ILPYIKQNARLFVLV---IFLGAVTifSAAFLMFTSGFLISKAATRPENIL----LIYVPIVAVRtfGIARSVSRYVERL 79
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAgvaMILVAAT--ESTLAALLKPLLDDGFGGRDRSVLwwvpLVVIGLAVLR--GICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 80 VGhhiiLKIVSDMRVRLYNMLepgaLMLRSRF----RTGDML---GILSEDIEH-LQDAFLKTIFPAISALLLYAVsvia 151
Cdd:TIGR02203 81 VS----NKVVRDIRVRMFEKL----LGLPVSFfdrqPTGTLLsriTFDSEQVASaATDAFIVLVRETLTVIGLFIV---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 152 LGFFSWPFAILIALylfvlvvlFPVVSLLVTRARNAKLKSgRNVLYSRLTDAVMGVSDWMFSGrrHAFIDAYEKEEhdwF 231
Cdd:TIGR02203 149 LLYYSWQLTLIVVV--------MLPVLSILMRRVSKRLRR-ISKEIQNSMGQVTTVAEETLQG--YRVVKLFGGQA---Y 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 232 ELERKKQRFTRWRDFAAQC------------LVAGLILLMLFWTAGQQA-DGELAKTMIAAFVLvvfplteAFLPLSDAL 298
Cdd:TIGR02203 215 ETRRFDAVSNRNRRLAMKMtsagsisspitqLIASLALAVVLFIALFQAqAGSLTAGDFTAFIT-------AMIALIRPL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 299 GEVPGYQDSIKRM----NRVAPQPEASQtESGAQTLDLQDVT--LSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGR 371
Cdd:TIGR02203 288 KSLTNVNAPMQRGlaaaESLFTLLDSPP-EKDTGTRAIERARgdVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 372 SGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIADAVAVLNQKPHLFDTSILNNIRLGN-GEASDEDVRRAAKQV 449
Cdd:TIGR02203 367 SGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTlASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 450 KLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITH 529
Cdd:TIGR02203 447 YAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH 526
|
570 580 590
....*....|....*....|....*....|....*....
gi 2218266673 530 HLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRLY 568
Cdd:TIGR02203 527 RLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLH 565
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
337-547 |
8.09e-63 |
|
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: 204.15 E-value: 8.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL-KDQIADAVAV 414
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLdLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHLFDTSILNNIrlgngeasdedvrraakqvklhdyieslpdgyhtsvqetgirFSGGERQRIALARILLQDTPII 494
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 495 ILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGK 547
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
331-567 |
1.09e-62 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 216.37 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 331 DLQDV--TLSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQ- 407
Cdd:PRK13657 327 DLGRVkgAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAs 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 408 IADAVAVLNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARIL 487
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 488 LQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRL 567
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
337-570 |
6.51e-58 |
|
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: 193.47 E-value: 6.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYD-NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL-KDQIADAVAV 414
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPII 494
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 495 ILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRLYHL 570
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
339-552 |
4.40e-56 |
|
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: 188.18 E-value: 4.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 339 FRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQ-IADAVAVLN 416
Cdd:cd03245 5 FRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIIL 496
Cdd:cd03245 85 QDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 497 DEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEG 552
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
337-570 |
4.97e-56 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 198.32 E-value: 4.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGV-----ETALLKDQiad 410
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQ--- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 aVAVLNQKPHLFDTSILNNIRLG-NGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQ 489
Cdd:PRK11176 419 -VALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 490 DTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRLYH 569
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHK 577
|
.
gi 2218266673 570 L 570
Cdd:PRK11176 578 M 578
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
339-547 |
1.07e-53 |
|
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: 181.90 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 339 FRDVTFSYDN--SSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQ-IADAVAVL 415
Cdd:cd03248 14 FQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIII 495
Cdd:cd03248 94 GQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 496 LDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGK 547
Cdd:cd03248 174 LDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGR 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
222-567 |
1.03e-52 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 191.47 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 222 AYEKEEHDWFE--LERKKQrFTRWRDFA------AQCLVAGLILLMLFWTAGQQA-DGELAKTMIAAFVLVVFPLTEAFL 292
Cdd:TIGR00958 357 AAEEGEASRFKeaLEETLQ-LNKRKALAyagylwTTSVLGMLIQVLVLYYGGQLVlTGKVSSGNLVSFLLYQEQLGEAVR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 293 PLSDALGEVPGYQDSIKR----MNRvapQPEASQTESGAQTLDLQDVTlsFRDVTFSYDN--SSQVLDNFSFTLRQGEKM 366
Cdd:TIGR00958 436 VLSYVYSGMMQAVGASEKvfeyLDR---KPNIPLTGTLAPLNLEGLIE--FQDVSFSYPNrpDVPVLKGLTFTLHPGEVV 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 367 ALLGRSGSGKSTSLALIEGALKPDSGSVTLNGV-----ETALLKDQiadaVAVLNQKPHLFDTSILNNIRLGNGEASDED 441
Cdd:TIGR00958 511 ALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqyDHHYLHRQ----VALVGQEPVLFSGSVRENIAYGLTDTPDEE 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 442 VRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETvfEVLKG 521
Cdd:TIGR00958 587 IMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRAS 664
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2218266673 522 KTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRL 567
Cdd:TIGR00958 665 RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
280-569 |
5.03e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 184.66 E-value: 5.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 280 FVLVVFPltEAFLPLSDaLG-------EVPGYQDSIKRMnrvaPQPEASQTESGAQTLDLQD-VTLSFRD-VTFSYDNSs 350
Cdd:PRK11174 292 FVLILAP--EFYQPLRD-LGtfyhakaQAVGAAESLVTF----LETPLAHPQQGEKELASNDpVTIEAEDlEILSPDGK- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALkPDSGSVTLNGVE-TALLKDQIADAVAVLNQKPHLFDTSILNN 429
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIElRELDPESWRKHLSWVGQNPQLPHGTLRDN 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 430 IRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITER 509
Cdd:PRK11174 443 VLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 510 ELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRLYH 569
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
337-569 |
1.41e-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: 179.94 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL-KDQIADAVAVL 415
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIdRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLFDTSILNNIRLGNGE-ASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPII 494
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 495 ILDEPTVGLDPITERELMETVFEvLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRLYH 569
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
337-560 |
1.98e-48 |
|
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: 177.25 E-value: 1.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL-KDQIADAVAV 414
Cdd:COG4618 331 LSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWdREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHLFDTSILNNI-RLGngEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPI 493
Cdd:COG4618 411 LPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 494 IILDEPTVGLDPITERELMETVfEVLK--GKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAA 560
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAI-RALKarGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
337-547 |
6.47e-48 |
|
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: 166.51 E-value: 6.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGRSGSGKST-SLAL---IEgalkPDSGSVTLNGVETALL-KDQIAD 410
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSlLLALfrlVE----LSSGSILIDGVDISKIgLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 AVAVLNQKPHLFDTSILNNIRLgNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQD 490
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDP-FGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 491 TPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGK 547
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGR 214
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
322-567 |
6.61e-48 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 176.23 E-value: 6.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 322 QTESGAQTLDLQDV--TLSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGV 399
Cdd:TIGR01192 318 QREEPADAPELPNVkgAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGI 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 400 ETALL-KDQIADAVAVLNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGER 478
Cdd:TIGR01192 398 DINTVtRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELL 558
Cdd:TIGR01192 478 QRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELI 557
|
....*....
gi 2218266673 559 AANERYRRL 567
Cdd:TIGR01192 558 QKDGRFYKL 566
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
337-563 |
7.07e-48 |
|
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: 166.74 E-value: 7.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIADAVAVL 415
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNlRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPH--LFDTSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARIL 487
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 488 LQDTPIIILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLAANER 563
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
337-560 |
2.24e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 165.62 E-value: 2.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLN 416
Cdd:COG1131 1 IEVRGLTKRYGDK-TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLFDT-SILNNIRL------GNGEASDEDVRRAAKQVKLHDYIESLPDGYhtsvqetgirfSGGERQRIALARILLQ 489
Cdd:COG1131 80 QEPALYPDlTVRENLRFfarlygLPRKEARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 490 DTPIIILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELLAA 560
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
338-547 |
7.85e-45 |
|
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: 157.63 E-value: 7.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 338 SFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADAVAVL 415
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDlTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPH--LFDTSI-------LNNIRLGNGEAsDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARI 486
Cdd:cd03225 81 FQNPDdqFFGPTVeeevafgLENLGLPEEEI-EERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 487 LLQDTPIIILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGVEA-ADKIVFLENGK 547
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
337-573 |
1.11e-44 |
|
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: 159.13 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSS-QVLDNFSFTLRQGEKMALLGRSGSGKSTsLA-LIEGALKPDSGSVTLNGVETALLKD--QIADAV 412
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKST-LAkLLNGLLLPTSGKVTVDGLDTLDEENlwEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPhlfDTSI------------LNNIrlgnGEASDEDVRR---AAKQVKLHDYIESLPdgyHtsvqetgiRFSGGE 477
Cdd:TIGR04520 80 GMVFQNP---DNQFvgatveddvafgLENL----GVPREEMRKRvdeALKLVGMEDFRDREP---H--------LLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 478 RQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEAADKIVFLENGKTEMEGTHE 555
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
250
....*....|....*...
gi 2218266673 556 ELLAANERYRRLyHLDVP 573
Cdd:TIGR04520 222 EIFSQVELLKEI-GLDVP 238
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
319-569 |
2.75e-44 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 165.66 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 319 EASQTESGAQTLDLQDVTLSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLN 397
Cdd:PRK10789 296 EAPVVKDGSEPVPEGRGELDVNIRQFTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 398 GVETALLK-DQIADAVAVLNQKPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGG 476
Cdd:PRK10789 376 DIPLTKLQlDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 477 ERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEE 556
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQ 535
|
250
....*....|...
gi 2218266673 557 LLAANERYRRLYH 569
Cdd:PRK10789 536 LAQQSGWYRDMYR 548
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
337-559 |
6.89e-43 |
|
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: 153.47 E-value: 6.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLN 416
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLFDT-SILNNIRLgNGEASDEDVRRAAKQVKlhDYIES--LPDGYHTSVQEtgirFSGGERQRIALARILLQDTPI 493
Cdd:COG4555 81 DERGLYDRlTVRENIRY-FAELYGLFDEELKKRIE--ELIELlgLEEFLDRRVGE----LSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 494 IILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELLA 559
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
337-547 |
2.94e-42 |
|
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: 149.47 E-value: 2.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLN 416
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLFDtsilnnirlgngeasdedvrraakqvklhdyieslpdgyHTSVQETgIRFSGGERQRIALARILLQDTPIIIL 496
Cdd:cd03230 80 EEPSLYE---------------------------------------NLTVREN-LKLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 497 DEPTVGLDPITERELMETVFE-VLKGKTILWITHHLAGVEA-ADKIVFLENGK 547
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGR 172
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
337-559 |
3.55e-42 |
|
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: 151.50 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK----DQIADAV 412
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaelYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPHLFDT-SILNNIRLG---NGEASDEDVRRAAKQ----VKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALA 484
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLEkleaVGLRGAEDLYPA-----------ELSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 485 RILLQDTPIIILDEPTVGLDPITERELMETVFEV--LKGKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLA 559
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
337-572 |
9.81e-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: 150.96 E-value: 9.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKD-QIADAVAVL 415
Cdd:COG1120 2 LEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHL-FDTSILNNIRLG-------NGEASDED---VRRAAKQVKLHDYIeslpdgyHTSVQEtgirFSGGERQRIALA 484
Cdd:COG1120 81 PQEPPApFGLTVRELVALGryphlglFGRPSAEDreaVEEALERTGLEHLA-------DRPVDE----LSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 485 RILLQDTPIIILDEPTVGLDPITERELMETVFEV--LKGKTILWITHHL--AgVEAADKIVFLENGKTEMEGTHEELLAA 560
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLnlA-ARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
250
....*....|..
gi 2218266673 561 nERYRRLYHLDV 572
Cdd:COG1120 229 -ELLEEVYGVEA 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
337-561 |
2.15e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 149.13 E-value: 2.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNssQVLdNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVEtaLLKDQIAD-AVAVL 415
Cdd:COG3840 2 LRLDDLTYRYGD--FPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD--LTALPPAErPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQK----PHLfdtSILNNIRLG---NGEASDED---VRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALAR 485
Cdd:COG3840 77 FQEnnlfPHL---TVAQNIGLGlrpGLKLTAEQraqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 486 ILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELLAAN 561
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
337-547 |
2.40e-41 |
|
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: 148.00 E-value: 2.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQ----VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGvetallkdqiadAV 412
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPHLFDTSILNNIRLGngeaSDEDVRRAAKQVK---LHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQ 489
Cdd:cd03250 69 AYVSQEPWIQNGTIRENILFG----KPFDEERYEKVIKacaLEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 490 DTPIIILDEPTVGLDPITERELMETVF--EVLKGKTILWITHHLAGVEAADKIVFLENGK 547
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENCIlgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
337-547 |
3.01e-41 |
|
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: 148.41 E-value: 3.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSY---DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADA-- 411
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 ---VAVLNQKPHLFDT-SILNNIRLG---NGEASDEDVRRAA---KQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRI 481
Cdd:cd03255 81 rrhIGFVFQSFNLLPDlTALENVELPlllAGVPKKERRERAEellERVGLGDRLNHYPS-----------ELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 482 ALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEAADKIVFLENGK 547
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
257-570 |
8.30e-41 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 156.03 E-value: 8.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 257 LLMLFwtaGQQADGELAKTMIAAFVLVVFPLTEAFLPLSDalgevpgyQDSIKRMNRVAPQP-----EASQTESGAQTLD 331
Cdd:PRK10790 267 LLMLF---GFSASGTIEVGVLYAFISYLGRLNEPLIELTT--------QQSMLQQAVVAGERvfelmDGPRQQYGNDDRP 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQI-AD 410
Cdd:PRK10790 336 LQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 AVAVLNQKPHLFDTSILNNIRLGNgEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQD 490
Cdd:PRK10790 416 GVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 491 TPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRLYHL 570
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQL 574
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
337-547 |
1.39e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.03 E-value: 1.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSY---DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDqiaDAVA 413
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE---RELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VL-N-------QKPHLFDT-SILNNIRLG---NGEASDEDVRRAA---KQVKLHDYIESLPDgyhtsvqetgiRFSGGER 478
Cdd:COG1136 82 RLrRrhigfvfQFFNLLPElTALENVALPlllAGVSRKERRERARellERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEAADKIVFLENGK 547
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGR 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
337-574 |
2.32e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.08 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIA------- 409
Cdd:COG1121 7 IELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGyvpqrae 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 ----------DAVAvLNQKPHLfdtsilnNIRLGNGEASDEDVRRAAKQVKLHDY----IESLpdgyhtsvqetgirfSG 475
Cdd:COG1121 86 vdwdfpitvrDVVL-MGRYGRR-------GLFRRPSRADREAVDEALERVGLEDLadrpIGEL---------------SG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 476 GERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEvLK--GKTILWITHHLAGV-EAADKIVFLeNGKTEMEG 552
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRE-LRreGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHG 220
|
250 260
....*....|....*....|..
gi 2218266673 553 THEELLAAnERYRRLYHLDVPV 574
Cdd:COG1121 221 PPEEVLTP-ENLSRAYGGPVAL 241
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
336-560 |
2.58e-39 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 151.35 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL-KDQIADAVA 413
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWdRETFGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPHLFDTSILNNI-RLGNgEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTP 492
Cdd:TIGR01842 396 YLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 493 IIILDEPTVGLDPITERELMETVFEV-LKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAA 560
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
288-560 |
3.22e-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: 150.44 E-value: 3.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 288 TEAFLPLSDALGEVPGYQdsikrmnrvAPQPEASQTESGAQTLdlqdvtLSFRDVTFSYDNSS----QVLDNFSFTLRQG 363
Cdd:COG1123 227 PEEILAAPQALAAVPRLG---------AARGRAAPAAAAAEPL------LEVRNLSKRYPVRGkggvRAVDDVSLTLRRG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 364 EKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKD----QIADAVAVLNQKPhlfDTSI------------- 426
Cdd:COG1123 292 ETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslrELRRRVQMVFQDP---YSSLnprmtvgdiiaep 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 427 LNNIRLGNGEASDEDVRRAAKQVKLH-DYIESLPdgyHTsvqetgirFSGGERQRIALARILLQDTPIIILDEPTVGLDP 505
Cdd:COG1123 369 LRLHGLLSRAERRERVAELLERVGLPpDLADRYP---HE--------LSGGQRQRVAIARALALEPKLLILDEPTSALDV 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 506 ITERELMEtVFEVLK---GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELLAA 560
Cdd:COG1123 438 SVQAQILN-LLRDLQrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
333-561 |
7.21e-39 |
|
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: 142.43 E-value: 7.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 333 QDVTLSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAV 412
Cdd:COG1127 2 SEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 ----AVLNQKPHLFDT-SILNNIRLG---NGEASDEDVRRAA----KQVKLHDYIESLPDgyhtsvqetgiRFSGGERQR 480
Cdd:COG1127 81 rrriGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVleklELVGLPGAADKMPS-----------ELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 481 IALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEEL 557
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEEL 229
|
....
gi 2218266673 558 LAAN 561
Cdd:COG1127 230 LASD 233
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
337-573 |
8.17e-39 |
|
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: 143.75 E-value: 8.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYD----NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADA 411
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDiTAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 ---VAVLNQKP--HLFDTSILNNIRLG------NGEASDEDVRRAAKQVKL-HDYIESLPdgyhtsvqetgirF--SGGE 477
Cdd:TIGR04521 81 rkkVGLVFQFPehQLFEETVYKDIAFGpknlglSEEEAEERVKEALELVGLdEEYLERSP-------------FelSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 478 RQRIALARILLQDTPIIILDEPTVGLDPITERELMETvFEVL---KGKTILWITHHLAGV-EAADKIVFLENGKTEMEGT 553
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDL-FKRLhkeKGLTVILVTHSMEDVaEYADRVIVMHKGKIVLDGT 226
|
250 260
....*....|....*....|
gi 2218266673 554 HEELLAANERYRRlYHLDVP 573
Cdd:TIGR04521 227 PREVFSDVDELEK-IGLDVP 245
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
337-545 |
1.06e-37 |
|
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: 138.76 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSS---QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVEtallKDQIADAVA 413
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP----VTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPHLFD-TSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARI 486
Cdd:cd03293 77 YVFQQDALLPwLTVLDNVALGlelqgvPKAEARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 487 LLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAgvEA---ADKIVFLEN 545
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDID--EAvflADRVVVLSA 207
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
337-573 |
1.33e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 140.54 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVEtalLKDQ----IADA 411
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEEtvwdVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKP--HLFDTSILNNIRLG---NGEASDEDVRR---AAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIAL 483
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGlenIGVPREEMVERvdqALRQVGMEDFLNREPH-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELMETVFEVL--KGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAAN 561
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
250
....*....|..
gi 2218266673 562 ERYRRLyHLDVP 573
Cdd:PRK13635 232 HMLQEI-GLDVP 242
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
338-547 |
2.27e-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: 135.84 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 338 SFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIA-DAVAVLN 416
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELrRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QkphlfdtsilnnirlgngeasdedvrraakqvklhdyieslpdgyhtsvqetgirFSGGERQRIALARILLQDTPIIIL 496
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 497 DEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVE-AADKIVFLENGK 547
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
340-547 |
3.97e-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: 135.64 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIADAVAVLNQk 418
Cdd:cd03214 3 ENLSVGYGGR-TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSpKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 419 phlfdtsilnnirlgngeasdedvrrAAKQVKLHD----YIESLpdgyhtsvqetgirfSGGERQRIALARILLQDTPII 494
Cdd:cd03214 81 --------------------------ALELLGLAHladrPFNEL---------------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 495 ILDEPTVGLDPITERELMETVFEV--LKGKTILWITHHLA-GVEAADKIVFLENGK 547
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGR 175
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
25-312 |
4.01e-37 |
|
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: 139.15 E-value: 4.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 25 GAVTIFSAAFLMFTSGFLISKAATRPENILLI--YVPIVAVRTFGIARSVSRYVERLVGHHIILKIVSDMRVRLYNMLEP 102
Cdd:cd18585 1 GLLTLLASIGLLALSGWFISAAALAGLAAPTFnyFTPAAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 103 GALMLRSRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAILIALYLFVLVVLFPVVSLLVT 182
Cdd:cd18585 81 LAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 183 RARNAKLKSGRNVLYSRLTDAVMGVSDWMFSGRRHAFIDAYEKEEHDWFELERKKQRFTRWrDFAAQCLVAGLILLMLFW 262
Cdd:cd18585 161 KKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGL-SQALMILLSGLTVWLVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 263 -TAGQQADGELAKTMIAAFVLVVFPLTEAFLPLSDA---LGEVpgyQDSIKRMN 312
Cdd:cd18585 240 lGAPLVQNGALDGALLAMLVFAVLASFEAVAPLPLAfqyLGET---RAAARRLF 290
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
337-546 |
6.00e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.91 E-value: 6.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSY---DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETAllkdQIADAVA 413
Cdd:COG1116 8 LELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----GPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPHLFD-TSILNNIRLG---NGEASDEDVRRAA---KQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARI 486
Cdd:COG1116 84 VVFQEPALLPwLTVLDNVALGlelRGVPKAERRERARellELVGLAGFEDAYPH-----------QLSGGMRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 487 LLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAgvEA---ADKIVFLENG 546
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHDVD--EAvflADRVVVLSAR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
337-547 |
8.39e-37 |
|
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: 135.01 E-value: 8.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIAD---AVA 413
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrrRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPHLFDT-SILNNIRLGngeasdedvrraakqvklhdyieslpdgyhtsvqetgirFSGGERQRIALARILLQDTP 492
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 493 IIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEA-ADKIVFLENGK 547
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
337-547 |
1.11e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.71 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADAVAVL 415
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLFDTSILNNI----RLGNGEASDEDVRRAAKQVKLHDYIeslpdgYHTSVQetgiRFSGGERQRIALARILLQDT 491
Cdd:COG4619 80 PQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDI------LDKPVE----RLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 492 PIIILDEPTVGLDPiterELMETVFEVL------KGKTILWITHHLAGVEA-ADKIVFLENGK 547
Cdd:COG4619 150 DVLLLDEPTSALDP----ENTRRVEELLreylaeEGRAVLWVSHDPEQIERvADRVLTLEAGR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
353-501 |
1.15e-36 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 133.54 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGveTALLKDQIADA---VAVLNQKPHLF-DTSILN 428
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG--QDLTDDERKSLrkeIGYVFQDPQLFpRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 429 NIRLGngeASDEDVRRAAKQVKLHDYIE--SLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTV 501
Cdd:pfam00005 79 NLRLG---LLLKGLSKREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
337-573 |
3.12e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 141.96 E-value: 3.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSS-QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPD---SGSVTLNGVETALLKDQI-ADA 411
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALrGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKP--HLFDTSILNNIR--LGNGEASDED----VRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIAL 483
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGDQIAeaLENLGLSRAEararVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLAA 560
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
250
....*....|...
gi 2218266673 561 NERYRRLYHLDVP 573
Cdd:COG1123 234 PQALAAVPRLGAA 246
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
330-547 |
3.59e-36 |
|
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: 134.18 E-value: 3.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIA 409
Cdd:cd03259 1 LELKGLSKTYGSVR--------ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 DaVAVLNQKPHLFDT-SILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPDGyhtsvqetgirFSGGERQRIA 482
Cdd:cd03259 73 N-IGMVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 483 LARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAgvEA---ADKIVFLENGK 547
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQE--EAlalADRIAVMNEGR 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
337-547 |
8.25e-36 |
|
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: 131.95 E-value: 8.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADAVAV 414
Cdd:cd03246 1 LEVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADiSQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHLFDTSILNNIrlgngeasdedvrraakqvklhdyieslpdgyhtsvqetgirFSGGERQRIALARILLQDTPII 494
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 495 ILDEPTVGLDPITERELMETVFEV-LKGKTILWITHHLAGVEAADKIVFLENGK 547
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGR 172
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
337-562 |
1.33e-35 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 133.58 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETAL-----LKDQIADA 411
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqdpveLRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKPHLfdtSILNNIRLG---NGEASDEDVRRAAKQVKLHD-----YIESLPDgyhtsvqetgiRFSGGERQRIAL 483
Cdd:cd03295 81 IQQIGLFPHM---TVEENIALVpklLKWPKEKIRERADELLALVGldpaeFADRYPH-----------ELSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAgvEA---ADKIVFLENGKTEMEGTHEELL 558
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDID--EAfrlADRIAIMKNGEIVQVGTPDEIL 224
|
....*.
gi 2218266673 559 A--ANE 562
Cdd:cd03295 225 RspAND 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
337-547 |
1.59e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.87 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDqiaDAVAVLN 416
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR---REIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QK--------PHLFDTSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPdgyhtsvqetgIRFSGGERQRIA 482
Cdd:COG2884 79 RRigvvfqdfRLLPDRTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 483 LARILLQDTPIIILDEPTVGLDPITERELMEtVFEVL--KGKTILWITHHLAGVEAADK-IVFLENGK 547
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIME-LLEEInrRGTTVLIATHDLELVDRMPKrVLELEDGR 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
337-547 |
1.96e-35 |
|
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: 132.63 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSS---QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIA---- 409
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 --------DAVAVLNqkP-----HLFDTSILNNIRLGNGEASDEDVRRAAKQVKLH-DYIESLPDgyhtsvqetgiRFSG 475
Cdd:cd03257 82 keiqmvfqDPMSSLN--PrmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeEVLNRYPH-----------ELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 476 GERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEV--LKGKTILWITHHLAGVEA-ADKIVFLENGK 547
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGK 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
330-566 |
6.32e-35 |
|
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: 131.85 E-value: 6.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRdvtfSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG--VETALLKDQ 407
Cdd:COG1124 2 LEVRNLSVSYG----QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 408 iADAVAVLNQKP-------HLFDTSILNNIRLGNGEASDEDVRRAAKQVKLH-DYIESLPdgyHTsvqetgirFSGGERQ 479
Cdd:COG1124 78 -RRRVQMVFQDPyaslhprHTVDRILAEPLRIHGLPDREERIAELLEQVGLPpSFLDRYP---HQ--------LSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 480 RIALARILLQDTPIIILDEPTVGLDPITERELMEtVFEVLK---GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGT-- 553
Cdd:COG1124 146 RVAIARALILEPELLLLDEPTSALDVSVQAEILN-LLKDLReerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTva 224
|
250 260
....*....|....*....|...
gi 2218266673 554 -------HE---ELLAANERYRR 566
Cdd:COG1124 225 dllagpkHPytrELLAASLAFER 247
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
341-552 |
7.23e-35 |
|
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: 130.69 E-value: 7.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 341 DVTFSYDNSSQvldNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLkDQIADAVAVLNQKPH 420
Cdd:cd03298 5 KIRFSYGEQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA-PPADRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 421 LF-DTSILNNIRLGNG------EASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARILLQDTPI 493
Cdd:cd03298 81 LFaHLTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 494 IILDEPTVGLDPITERELMETVFEVL--KGKTILWITHHLAGVEA-ADKIVFLENGKTEMEG 552
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLDLHaeTKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
337-540 |
1.66e-34 |
|
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: 129.52 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLN 416
Cdd:COG4133 3 LEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLFDT-SILNNI----RLGNGEASDEDVRRAAKQVKLHDYiESLPDGYhtsvqetgirFSGGERQRIALARILLQDT 491
Cdd:COG4133 82 HADGLKPElTVRENLrfwaALYGLRADREAIDEALEAVGLAGL-ADLPVRQ----------LSAGQKRRVALARLLLSPA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2218266673 492 PIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVEAADKI 540
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLaRGGAVLLTTHQPLELAAARVL 200
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
337-568 |
2.53e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.18 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADA---V 412
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvTALRGRALRRLrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPHLFD-TSILNNI---RLGN--------GEASDEDVRRAAK---QVKLHDYIESLPDgyhtsvqetgiRFSGGE 477
Cdd:COG3638 83 GMIFQQFNLVPrLSVLTNVlagRLGRtstwrsllGLFPPEDRERALEaleRVGLADKAYQRAD-----------QLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 478 RQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILwITHH---LAgVEAADKIVFLENGKTEMEG 552
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVV-VNLHqvdLA-RRYADRIIGLRDGRVVFDG 229
|
250
....*....|....*.
gi 2218266673 553 THEELlaANERYRRLY 568
Cdd:COG3638 230 PPAEL--TDAVLREIY 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
337-547 |
2.60e-34 |
|
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: 129.61 E-value: 2.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSL-------ALIEGAlkPDSGSVTLNGVETALLKDQIA 409
Cdd:cd03260 1 IELRDLNVYYGDK-HALKDISLDIPKGEITALIGPSGCGKSTLLrllnrlnDLIPGA--PDEGEVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 D---AVAVLNQKPHLFDTSILNNIRLG-------NGEASDEDVRRAAKQVKLHDYIESLPDGYHtsvqetgirFSGGERQ 479
Cdd:cd03260 78 ElrrRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 480 RIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVE-AADKIVFLENGK 547
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGR 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
338-546 |
2.62e-34 |
|
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: 129.19 E-value: 2.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 338 SFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIAdavaVLNQ 417
Cdd:cd03235 1 EVEDLTVSYGGH-PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIG----YVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 418 KPHL---FDTSILNNIRLG----------NGEASDEDVRRAAKQVKLHDY----IESLpdgyhtsvqetgirfSGGERQR 480
Cdd:cd03235 76 RRSIdrdFPISVRDVVLMGlyghkglfrrLSKADKAKVDEALERVGLSELadrqIGEL---------------SGGQQQR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 481 IALARILLQDTPIIILDEPTVGLDPITERELMETVFEV-LKGKTILWITHHLAGVEA-ADKIVFLENG 546
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
337-568 |
3.81e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 138.62 E-value: 3.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQV--LDNFSFTLRQGEKMALLGRSGSGKSTSLALI------------------------------- 383
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 384 -----------------EGA------LKPDSGSVTLNGVETA--LLKDqIADAVAVLNQKPHLFDTSILNNIRLGNGEAS 438
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkEGGsgedstVFKNSGKILLDGVDICdyNLKD-LRNLFSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 439 DEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEV 518
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 519 LK--GKTILWITHHLAGVEAADKIVFLENGK-----TEMEGTHEELLAANERYRRLY 568
Cdd:PTZ00265 1405 KDkaDKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKKY 1461
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
335-574 |
2.78e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 127.58 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 335 VTLSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIADAVA 413
Cdd:PRK13548 1 AMLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPHL-FDTSILNNIRLG---NGEASDED---VRRAAKQVKLHDYIESLpdgYHTsvqetgirFSGGERQRIALARI 486
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGrapHGLSRAEDdalVAAALAQVDLAHLAGRD---YPQ--------LSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 487 LLQ------DTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITH--HLAgveA--ADKIVFLENGKTEMEGTH 554
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHerGLAVIVVLHdlNLA---AryADRIVLLHQGRLVADGTP 225
|
250 260
....*....|....*....|
gi 2218266673 555 EELLAAnERYRRLYHLDVPV 574
Cdd:PRK13548 226 AEVLTP-ETLRRVYGADVLV 244
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
341-548 |
5.72e-33 |
|
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: 125.06 E-value: 5.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 341 DVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQiaDAVAVLNQKP- 419
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR--KSIGYVMQDVd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 420 -HLFDTSILNNIRLGNGEASD--EDVRRAAKQVKLHDYIESLPdgyHTsvqetgirFSGGERQRIALARILLQDTPIIIL 496
Cdd:cd03226 82 yQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHP---LS--------LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 497 DEPTVGLDPITERELMETVFEV-LKGKTILWITHH---LAGVeaADKIVFLENGKT 548
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDyefLAKV--CDRVLLLANGAI 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
337-557 |
7.33e-33 |
|
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: 125.31 E-value: 7.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVL 415
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLFDT-SILNNIRL------GNGEASDEDVRRAAKQVKLHDYIeslpdgyHTSVQEtgirFSGGERQRIALARILL 488
Cdd:cd03263 81 PQFDALFDElTVREHLRFyarlkgLPKSEIKEEVELLLRVLGLTDKA-------NKRART----LSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 489 QDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEEL 557
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
337-568 |
7.57e-33 |
|
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: 126.14 E-value: 7.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKD----QIADAV 412
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPHLFD-TSILNNI---RLGN--------GEASDEDVRRAA---KQVKLHDYIESLPDgyhtsvqetgiRFSGGE 477
Cdd:cd03256 81 GMIFQQFNLIErLSVLENVlsgRLGRrstwrslfGLFPKEEKQRALaalERVGLLDKAYQRAD-----------QLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 478 RQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVL--KGKTILWITHHL-AGVEAADKIVFLENGKTEMEGTH 554
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreEGITVIVSLHQVdLAREYADRIVGLKDGRIVFDGPP 229
|
250
....*....|....
gi 2218266673 555 EELlaANERYRRLY 568
Cdd:cd03256 230 AEL--TDEVLDEIY 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
337-561 |
2.63e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 124.31 E-value: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQvldNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQiaDAVAVL 415
Cdd:PRK10771 2 LKLTDITWLYHHLPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhTTTPPSR--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLFD-TSILNNIRLG-------NGEASDEdVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARIL 487
Cdd:PRK10771 77 FQENNLFShLTVAQNIGLGlnpglklNAAQREK-LHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 488 LQDTPIIILDEPTVGLDPITERELMETVFEVLKGK--TILWITHHLagvEAADKI----VFLENGKTEMEGTHEELLAAN 561
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSL---EDAARIaprsLVVADGRIAWDGPTDELLSGK 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
337-547 |
1.09e-31 |
|
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: 121.87 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADavavLN 416
Cdd:cd03262 1 IEIKNLHKSFGDF-HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINE----LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QK-----------PHLfdtSILNNIRLG----NGEASDEDVRRAA---KQVKLHDYIESLPdgyhtsvqetgIRFSGGER 478
Cdd:cd03262 76 QKvgmvfqqfnlfPHL---TVLENITLApikvKGMSKAEAEERALellEKVGLADKADAYP-----------AQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLDPiterELMETVFEVLK-----GKTILWITHHLAGV-EAADKIVFLENGK 547
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDP----ELVGEVLDVMKdlaeeGMTMVVVTHEMGFArEVADRVIFMDDGR 212
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
356-552 |
1.13e-31 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 121.89 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 356 FSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQiaDAVAVLNQKPHLFD-TSILNNIRLG 433
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQShTGLAPYQ--RPVSMLFQENNLFAhLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 434 -------NGEaSDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLDPI 506
Cdd:TIGR01277 95 lhpglklNAE-QQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2218266673 507 TERELMETVFEVL--KGKTILWITHHLAGVEA-ADKIVFLENGKTEMEG 552
Cdd:TIGR01277 163 LREEMLALVKQLCseRQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
340-573 |
1.38e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 123.66 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYDNSSQ-----VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKD--QIADAV 412
Cdd:PRK13633 8 KNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPhlfDTSILNNI----------RLG-NGEASDEDVRRAAKQVKLHDYIESLPdgyHTsvqetgirFSGGERQRI 481
Cdd:PRK13633 88 GMVFQNP---DNQIVATIveedvafgpeNLGiPPEEIRERVDESLKKVGMYEYRRHAP---HL--------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 482 ALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLA 559
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
250
....*....|....
gi 2218266673 560 ANERYRRLyHLDVP 573
Cdd:PRK13633 234 EVEMMKKI-GLDVP 246
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
330-563 |
1.58e-31 |
|
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: 122.16 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQI 408
Cdd:cd03219 1 LEVRGLTKRFGGLV--------ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDiTGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 409 ADA-VAVLNQKPHLFDT-SILNNIRLG----------------NGEASDEDVRRAAKQVKLHDYIESLPDGyhtsvqetg 470
Cdd:cd03219 73 ARLgIGRTFQIPRLFPElTVLENVMVAaqartgsglllararrEEREARERAEELLERVGLADLADRPAGE--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 471 irFSGGERQRIALARILLQDTPIIILDEPTVGLDPiTERE-LMETVFEV-LKGKTILWITHHLAGV-EAADKIVFLENGK 547
Cdd:cd03219 144 --LSYGQQRRLEIARALATDPKLLLLDEPAAGLNP-EETEeLAELIRELrERGITVLLVEHDMDVVmSLADRVTVLDQGR 220
|
250
....*....|....*.
gi 2218266673 548 TEMEGTHEELLaANER 563
Cdd:cd03219 221 VIAEGTPDEVR-NNPR 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
330-573 |
1.86e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.18 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQ 407
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiSKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 408 IADAVAVLNQKPhlfDTSI------------LNNIRLGNGEASDEdVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSG 475
Cdd:PRK13632 81 IRKKIGIIFQNP---DNQFigatveddiafgLENKKVPPKKMKDI-IDDLAKKVGMEDYLDKEPQ-----------NLSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 476 GERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEAADKIVFLENGKTEMEGT 553
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
250 260
....*....|....*....|
gi 2218266673 554 HEELLaANERYRRLYHLDVP 573
Cdd:PRK13632 226 PKEIL-NNKEILEKAKIDSP 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
337-570 |
2.56e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.88 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-----TALLKdqIADA 411
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydkKSLLE--VRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKP--HLFDTSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPdgYHtsvqetgirFSGGERQRIAL 483
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPP--HH---------LSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELLA-- 559
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSdi 228
|
250
....*....|....*.
gi 2218266673 560 -----ANERYRRLYHL 570
Cdd:PRK13639 229 etirkANLRLPRVAHL 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
335-573 |
3.16e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.97 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 335 VTLSFRDVTFSYDNSS----QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKD--- 406
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITiTHKTKDkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 407 -QIADAVAVLNQKP--HLFDTSILNNIRLGngeasDEDVRRAAKQVKLHDYIESLPDGYHTSV-QETGIRFSGGERQRIA 482
Cdd:PRK13646 81 rPVRKRIGMVFQFPesQLFEDTVEREIIFG-----PKNFKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 483 LARILLQDTPIIILDEPTVGLDPITERELMETV--FEVLKGKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLA 559
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
250
....*....|....
gi 2218266673 560 ANERYRRlYHLDVP 573
Cdd:PRK13646 236 DKKKLAD-WHIGLP 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-547 |
9.04e-31 |
|
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: 119.05 E-value: 9.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 333 QDVTLSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIAD 410
Cdd:cd03369 3 EHGEIEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPlEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 AVAVLNQKPHLFDTSILNNIRLGNgEASDEDVRRAAKqvklhdyieslpdgyhtsVQETGIRFSGGERQRIALARILLQD 490
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 491 TPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGK 547
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGE 200
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
337-566 |
2.05e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 118.94 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADavavLN 416
Cdd:COG1126 2 IEIENLHKSFGDL-EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINK----LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QK-----------PHLfdtSILNNIRLG----NGEASDEDVRRAAK---QVKLHDYIESLPDgyhtsvqetgiRFSGGER 478
Cdd:COG1126 77 RKvgmvfqqfnlfPHL---TVLENVTLApikvKKMSKAEAEERAMElleRVGLADKADAYPA-----------QLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLDPiterelmETVFEVLK--------GKTILWITHHLA-GVEAADKIVFLENGKTE 549
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDP-------ELVGEVLDvmrdlakeGMTMVVVTHEMGfAREVADRVVFMDGGRIV 215
|
250
....*....|....*....
gi 2218266673 550 MEGTHEELLAA--NERYRR 566
Cdd:COG1126 216 EEGPPEEFFENpqHERTRA 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
355-566 |
4.74e-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: 118.90 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 355 NFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDqiADAVAVLNQK-----------PHLfd 423
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSR--KELRELRRKKismvfqsfallPHR-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 424 tSILNNIRLG---NGEASDEDVRRAAK---QVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARILLQDTPIIILD 497
Cdd:cd03294 118 -TVLENVAFGlevQGVPRAEREERAAEaleLVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 498 EPTVGLDPITERELMETVFEVLK--GKTILWITHHLAgvEA---ADKIVFLENGKTEMEGTHEELLA--ANERYRR 566
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLD--EAlrlGDRIAIMKDGRLVQVGTPEEILTnpANDYVRE 259
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
337-574 |
2.00e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 116.75 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIADAVAVL 415
Cdd:COG4559 2 LEAENLSVRLGGR-TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHL-FDTSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLpdgYHTsvqetgirFSGGERQRIALARILL 488
Cdd:COG4559 81 PQHSSLaFPFTVEEVVALGraphgsSAAQDRQIVREALALVGLAHLAGRS---YQT--------LSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 489 Q------DTP-IIILDEPTVGLDPITERELMETVFEVL-KGKTILWITH--HLAgveA--ADKIVFLENGKTEMEGTHEE 556
Cdd:COG4559 150 QlwepvdGGPrWLFLDEPTSALDLAHQHAVLRLARQLArRGGGVVAVLHdlNLA---AqyADRILLLHQGRLVAQGTPEE 226
|
250
....*....|....*...
gi 2218266673 557 LLAAnERYRRLYHLDVPV 574
Cdd:COG4559 227 VLTD-ELLERVYGADLRV 243
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
337-566 |
5.10e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 5.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVetallkdqiaDAVAVLN 416
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR----------DVTGLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QK-------------PHLfdtSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGE 477
Cdd:COG3842 75 EKrnvgmvfqdyalfPHL---TVAENVAFGlrmrgvPKAEIRARVAELLELVGLEGLADRYPH-----------QLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 478 RQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAgvEA---ADKIVFLENGKTEMEG 552
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQE--EAlalADRIAVMNDGRIEQVG 218
|
250
....*....|....
gi 2218266673 553 THEELlaanerYRR 566
Cdd:COG3842 219 TPEEI------YER 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
337-568 |
5.19e-29 |
|
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: 115.47 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKD----QIADAV 412
Cdd:TIGR02315 2 LEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklrKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPHLFD-TSILNNI---RLGN--------GEASDEDVRRAA---KQVKLHDYieslpdgYHTSVQEtgirFSGGE 477
Cdd:TIGR02315 82 GMIFQHYNLIErLTVLENVlhgRLGYkptwrsllGRFSEEDKERALsalERVGLADK-------AYQRADQ----LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 478 RQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLA-GVEAADKIVFLENGKTEMEGTH 554
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKedGITVIINLHQVDlAKKYADRIVGLKAGEIVFDGAP 230
|
250
....*....|....
gi 2218266673 555 EELlaANERYRRLY 568
Cdd:TIGR02315 231 SEL--DDEVLRHIY 242
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
350-556 |
8.86e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.92 E-value: 8.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 350 SQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGV----ETALLKDqIADAVAVLNQKP--HLFD 423
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVditdKKVKLSD-IRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 424 TSILNNIRLG--NGEASDED----VRRAAKQVKLhDYiESLPDgyhtsvqETGIRFSGGERQRIALARILLQDTPIIILD 497
Cdd:PRK13637 99 ETIEKDIAFGpiNLGLSEEEienrVKRAMNIVGL-DY-EDYKD-------KSPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 498 EPTVGLDPITERELMETVFEVLKGK--TILWITHHLAGV-EAADKIVFLENGKTEMEGTHEE 556
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
352-558 |
1.25e-28 |
|
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: 113.97 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 352 VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADaVAVLNQKPHLF-DTSILNNI 430
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-ISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 431 ------RLGNGEASDEDVRRAAKQVKlhdyIESLPDGYHTsvqetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLD 504
Cdd:cd03299 93 ayglkkRKVDKKEIERKVLEIAEMLG----IDHLLNRKPE-------TLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 505 PITERELMETVFEVLK--GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELL 558
Cdd:cd03299 162 VRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
340-574 |
2.46e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.51 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGveTALLKDQIADA---VAVLN 416
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG--EPITKENIREVrkfVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKP--HLFDTSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPdgYHtsvqetgirFSGGERQRIALARILL 488
Cdd:PRK13652 85 QNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVP--HH---------LSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 489 QDTPIIILDEPTVGLDPITERELMETV--FEVLKGKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLAANERYR 565
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
....*....
gi 2218266673 566 RLyHLDVPV 574
Cdd:PRK13652 234 RV-HLDLPS 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
330-552 |
3.05e-28 |
|
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: 112.46 E-value: 3.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsydNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIA 409
Cdd:cd03266 2 ITADALTKRFRDVK----KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 DAVAVLNQKPHLFD-TSILNNIRL-----G-NGEASDEDVRRAAKQVKLHDYIESLPDGyhtsvqetgirFSGGERQRIA 482
Cdd:cd03266 78 RRLGFVSDSTGLYDrLTARENLEYfaglyGlKGDELTARLEELADRLGMEELLDRRVGG-----------FSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 483 LARILLQDTPIIILDEPTVGLDPITERELMEtVFEVLK--GKTILWITHHLAGVEA-ADKIVFLENGKTEMEG 552
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALRE-FIRQLRalGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
337-559 |
3.19e-28 |
|
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: 112.53 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADA-VAV 414
Cdd:cd03224 1 LEVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHERARAgIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHLFDT-SILNNIRLGNGEASDEDVRRAAKQV-----KLHDYIESLpdgyhtsvqetGIRFSGGERQRIALARILL 488
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGAYARRRAKRKARLERVyelfpRLKERRKQL-----------AGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 489 QDTPIIILDEPTVGLDPItereLMETVFEVLK-----GKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLA 559
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPK----IVEEIFEAIRelrdeGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
334-573 |
4.17e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.74 E-value: 4.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 334 DVTLSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGS---VTLNGVE-TALLKDQI 408
Cdd:PRK13640 3 DNIVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITlTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 409 ADAVAVLNQKP--HLFDTSILNNIRLG--NGEASDED----VRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQR 480
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEmikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 481 IALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGK--TILWITHHLAGVEAADKIVFLENGKTEMEGTHEELL 558
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
250
....*....|....*
gi 2218266673 559 AANERYRRLyHLDVP 573
Cdd:PRK13640 232 SKVEMLKEI-GLDIP 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
251-545 |
4.21e-28 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 120.13 E-value: 4.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 251 LVAGLILLML---FW---------TAGQQADGELAKTMIAAFVLVVfpLTEAFLpLSDALGEVPGYQDSIKRMNR----V 314
Cdd:PTZ00265 286 MINGFILASYafgFWygtriiisdLSNQQPNNDFHGGSVISILLGV--LISMFM-LTIILPNITEYMKSLEATNSlyeiI 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 315 APQPEASQTESGAQTLDLQDVtlSFRDVTFSYDNSS--QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSG 392
Cdd:PTZ00265 363 NRKPLVENNDDGKKLKDIKKI--QFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 393 SVTLNgvETALLKD----QIADAVAVLNQKPHLFDTSILNNIRLG----------------NGEAS-------------- 438
Cdd:PTZ00265 441 DIIIN--DSHNLKDinlkWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSqenknkrnscrakc 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 439 ---------------------------DEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDT 491
Cdd:PTZ00265 519 agdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNP 598
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 492 PIIILDEPTVGLDPITERELMETVfEVLKGK----TILwITHHLAGVEAADKIVFLEN 545
Cdd:PTZ00265 599 KILILDEATSSLDNKSEYLVQKTI-NNLKGNenriTII-IAHRLSTIRYANTIFVLSN 654
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
337-568 |
9.95e-28 |
|
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: 111.23 E-value: 9.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIADA-VAV 414
Cdd:COG0410 4 LEVENLHAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHLFDT-SILNNIRLG-NGEASDEDVRRAAKQV-----KLHDYIESLpdgyhtsvqetGIRFSGGERQRIALARIL 487
Cdd:COG0410 83 VPEGRRIFPSlTVEENLLLGaYARRDRAEVRADLERVyelfpRLKERRRQR-----------AGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 488 LQDTPIIILDEPTVGLDPItereLMETVFEVLK-----GKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLaAN 561
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPL----IVEEIFEIIRrlnreGVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELL-AD 226
|
....*..
gi 2218266673 562 ERYRRLY 568
Cdd:COG0410 227 PEVREAY 233
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
335-574 |
1.26e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.62 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 335 VTLSFRDVTFSYDNSS----QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETAL------L 404
Cdd:PRK13641 1 MSIKFENVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 405 KDqIADAVAVLNQKP--HLFDTSILNNIRLG--NGEASDEDVRRAA----KQVKL-HDYIESLPdgyhtsvqetgIRFSG 475
Cdd:PRK13641 81 KK-LRKKVSLVFQFPeaQLFENTVLKDVEFGpkNFGFSEDEAKEKAlkwlKKVGLsEDLISKSP-----------FELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 476 GERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGV-EAADKIVFLENGKTEMEGT 553
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHAS 228
|
250 260
....*....|....*....|.
gi 2218266673 554 HEELLaANERYRRLYHLDVPV 574
Cdd:PRK13641 229 PKEIF-SDKEWLKKHYLDEPA 248
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
334-573 |
1.58e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.42 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 334 DVTlsFRDVTFSYDNSS----QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTL------NGVETAL 403
Cdd:PRK13634 2 DIT--FQKVEHRYQYKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 404 LKDqIADAVAVLNQKP--HLFDTSILNNIRLG--NGEASDEDV-RRAAKQVKL----HDYIESLPdgyhtsvqetgIRFS 474
Cdd:PRK13634 80 LKP-LRKKVGIVFQFPehQLFEETVEKDICFGpmNFGVSEEDAkQKAREMIELvglpEELLARSP-----------FELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 475 GGERQRIALARILLQDTPIIILDEPTVGLDPITERELMEtVFEVL---KGKTILWITHHLAGVEA-ADKIVFLENGKTEM 550
Cdd:PRK13634 148 GGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMME-MFYKLhkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
250 260
....*....|....*....|...
gi 2218266673 551 EGTHEELLAANERYRRLyHLDVP 573
Cdd:PRK13634 227 QGTPREIFADPDELEAI-GLDLP 248
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
339-547 |
3.13e-27 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 109.42 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 339 FRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQiadAVAVLNQK 418
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGR---AIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 419 --------PHLFDTSILNNIRLGNgEASDEDVRRAAKQVK-------LHDYIESLPDGyhtsvqetgirFSGGERQRIAL 483
Cdd:cd03292 80 igvvfqdfRLLPDRNVYENVAFAL-EVTGVPPREIRKRVPaalelvgLSHKHRALPAE-----------LSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELMETVFEV-LKGKTILWITHHLAGVEAADKIVF-LENGK 547
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIaLERGK 213
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
11-559 |
4.47e-27 |
|
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: 115.28 E-value: 4.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 11 IKQNARLFVLVIFLGAVT-IFSAAFLMFtsgflISKAATRPENILLIYVP--IVAVRTFGIARSVSRYVERLVGHHIILK 87
Cdd:COG4615 8 LRESRWLLLLALLLGLLSgLANAGLIAL-----INQALNATGAALARLLLlfAGLLVLLLLSRLASQLLLTRLGQHAVAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 88 ivsdMRVRLYNMLepgalmLRS------RFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLyAVSVIALGFFSWPF-- 159
Cdd:COG4615 83 ----LRLRLSRRI------LAAplerleRIGAARLLAALTEDVRTISQAFVRLPELLQSVALV-LGCLAYLAWLSPPLfl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 160 --AILIALYLFVLVVLFPVVSLLVTRARNAklksgRNVLYSRLTDAVMGVSDWMFS-GRRHAFIDAYEKEEHDwfELERK 236
Cdd:COG4615 152 ltLVLLGLGVAGYRLLVRRARRHLRRAREA-----EDRLFKHFRALLEGFKELKLNrRRRRAFFDEDLQPTAE--RYRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 237 KQRFTRWRDFA---AQCLVAGLILLMLFWtagQQADGELAKTMIAAFVLVVFplteaFL--PLSDALGEVPGY---QDSI 308
Cdd:COG4615 225 RIRADTIFALAnnwGNLLFFALIGLILFL---LPALGWADPAVLSGFVLVLL-----FLrgPLSQLVGALPTLsraNVAL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 309 KRMNRV-----APQPEASQTESGAQTLDLQdvTLSFRDVTFSYDNSSQ----VLDNFSFTLRQGEKMALLGRSGSGKSTS 379
Cdd:COG4615 297 RKIEELelalaAAEPAAADAAAPPAPADFQ--TLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 380 LALIEGALKPDSGSVTLNG--VETALL---KDQIAdavAVLNQkPHLFDtsilnniRL--GNGEASDEDVRRAAKQVKLH 452
Cdd:COG4615 375 AKLLTGLYRPESGEILLDGqpVTADNReayRQLFS---AVFSD-FHLFD-------RLlgLDGEADPARARELLERLELD 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 453 DyieslpdgyHTSVQE---TGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERelmetVF--EVL-----KGK 522
Cdd:COG4615 444 H---------KVSVEDgrfSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRR-----VFytELLpelkaRGK 509
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 2218266673 523 TILWITH-----HLagveaADKIVFLENGK-TEMEGTHEELLA 559
Cdd:COG4615 510 TVIAISHddryfDL-----ADRVLKMDYGKlVELTGPAALAAS 547
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
305-559 |
4.96e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 4.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 305 QDSIKRMNRVAPQPEASQ--------TESGAQTLDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGK 376
Cdd:COG0488 283 IKALEKLEREEPPRRDKTveirfpppERLGKKVLELEGLSKSYGDKT--------LLDDLSLRIDRGDRIGLIGPNGAGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 377 STSLALIEGALKPDSGSVTLN-GVEtallkdqiadaVAVLNQKPHLFDT--SILNNIRLGNGEASDEDVRraakqvklhD 453
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKLGeTVK-----------IGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVR---------G 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 454 YIESL---PDGYHTSVQetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITeRELMETVFEVLKGkTILWITH- 529
Cdd:COG0488 415 YLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET-LEALEEALDDFPG-TVLLVSHd 488
|
250 260 270
....*....|....*....|....*....|...
gi 2218266673 530 -HLagVEA-ADKIVFLENGK-TEMEGTHEELLA 559
Cdd:COG0488 489 rYF--LDRvATRILEFEDGGvREYPGGYDDYLE 519
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
337-552 |
6.82e-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: 108.43 E-value: 6.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGeKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLN 416
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLFD--TSI--LNNI-RLGNGEASDED--VRRAAKQVKLHDYieslpdgYHTSVQEtgirFSGGERQRIALARILLQ 489
Cdd:cd03264 79 QEFGVYPnfTVRefLDYIaWLKGIPSKEVKarVDEVLELVNLGDR-------AKKKIGS----LSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 490 DTPIIILDEPTVGLDPiTERELMETVF-EVLKGKTILWITHHLAGVEA-ADKIVFLENGKTEMEG 552
Cdd:cd03264 148 DPSILIVDEPTAGLDP-EERIRFRNLLsELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
337-548 |
1.00e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.57 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKdqIADA----V 412
Cdd:COG1129 5 LEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS--PRDAqaagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPHLFDT-SILNNIRLGN-----GEASDEDVRRAAKQVklhdyIESLpdGYHTSVQETGIRFSGGERQRIALARI 486
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGReprrgGLIDWRAMRRRAREL-----LARL--GLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 487 LLQDTPIIILDEPTVGLdpiTERELmETVFEVL-----KGKTILWITHHLAGVEA-ADKIVFLENGKT 548
Cdd:COG1129 155 LSRDARVLILDEPTASL---TEREV-ERLFRIIrrlkaQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
340-573 |
1.57e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.44 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYDNSSQ--VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVEtaLLKD---QIADAVAV 414
Cdd:PRK13650 8 KNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL--LTEEnvwDIRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKP--HLFDTSILNNIRLG---NGEASDEDVRR---AAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARI 486
Cdd:PRK13650 86 VFQNPdnQFVGATVEDDVAFGlenKGIPHEEMKERvneALELVGMQDFKEREPA-----------RLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 487 LLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERY 564
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
....*....
gi 2218266673 565 RRLyHLDVP 573
Cdd:PRK13650 235 LQL-GLDIP 242
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
337-559 |
2.30e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.54 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTsLAL-IEGALKPDSGSVTLNGVETALLK--DQIADAVA 413
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKST-LALhLNGLLRPQKGKVLVSGIDTGDFSklQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPhlfDTSILnnirlgnGEASDED------------------VRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSG 475
Cdd:PRK13644 81 IVFQNP---ETQFV-------GRTVEEDlafgpenlclppieirkrVDRALAEIGLEKYRHRSPK-----------TLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 476 GERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEV-LKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTH 554
Cdd:PRK13644 140 GQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEP 219
|
....*
gi 2218266673 555 EELLA 559
Cdd:PRK13644 220 ENVLS 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
340-574 |
2.54e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 107.86 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIADAVAVLNQK 418
Cdd:COG4604 5 KNVSKRYGGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsRELAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 419 PHLfdtsilnNIRL---------------GNGEASDED-VRRAAKQVKLHD----YIESLpdgyhtsvqetgirfSGGER 478
Cdd:COG4604 84 NHI-------NSRLtvrelvafgrfpyskGRLTAEDREiIDEAIAYLDLEDladrYLDEL---------------SGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLDPITERELMET----VFEvlKGKTILWITHHL--AGVeAADKIVFLENGKTEMEG 552
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLlrrlADE--LGKTVVIVLHDInfASC-YADHIVAMKDGRVVAQG 218
|
250 260
....*....|....*....|..
gi 2218266673 553 THEELLAAnERYRRLYHLDVPV 574
Cdd:COG4604 219 TPEEIITP-EVLSDIYDTDIEV 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
337-548 |
3.57e-26 |
|
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: 104.82 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALlkdqiadavavln 416
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 qkphlfdtsilnnirlgngeASDEDVRRAakqvklhdyieslpdgyhtsvqetGIRF----SGGERQRIALARILLQDTP 492
Cdd:cd03216 67 --------------------ASPRDARRA------------------------GIAMvyqlSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 493 IIILDEPTVGLDPiteRELmETVFEVLK-----GKTILWITHHLAGV-EAADKIVFLENGKT 548
Cdd:cd03216 103 LLILDEPTAALTP---AEV-ERLFKVIRrlraqGVAVIFISHRLDEVfEIADRVTVLRDGRV 160
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
332-547 |
5.92e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETallkdqiada 411
Cdd:COG0488 1 LENLSKSFGGRP--------LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKPHLFDT-SILNNIRLGNGE----------------ASDEDVRRAAkqvKLHDYIESLpDGY--HTSVQET--- 469
Cdd:COG0488 63 IGYLPQEPPLDDDlTVLDTVLDGDAElraleaeleeleaklaEPDEDLERLA---ELQEEFEAL-GGWeaEARAEEIlsg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 470 -GIR----------FSGGERQRIALARILLQDTPIIILDEPTVGLDpiterelMETVF---EVLKG--KTILWITH--H- 530
Cdd:COG0488 139 lGFPeedldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEwleEFLKNypGTVLVVSHdrYf 211
|
250
....*....|....*..
gi 2218266673 531 LAGVeaADKIVFLENGK 547
Cdd:COG0488 212 LDRV--ATRILELDRGK 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
336-543 |
6.50e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.87 E-value: 6.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYDNSSQ---VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQiada 411
Cdd:COG4525 3 MLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 vAVLNQKPHLFD-TSILNNIRLG---NGEASDEDVRRAA---KQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALA 484
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAFGlrlRGVPKAERRARAEellALVGLADFARRRIW-----------QLSGGMRQRVGIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 485 RILLQDTPIIILDEPTVGLDPITeRELM-ETVFEVLK--GKTILWITHhlaGVEAAdkiVFL 543
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALT-REQMqELLLDVWQrtGKGVFLITH---SVEEA---LFL 201
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
336-558 |
8.57e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 108.70 E-value: 8.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVetallkdqiadaVAVL 415
Cdd:COG1118 2 SIEVRNISKRFGSF-TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR------------DLFT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPH------------LF-DTSILNNIR--LGNGEASDEDVR-RAAKQVKLhdyieslpdgyhtsVQETGI--RF---- 473
Cdd:COG1118 69 NLPPRerrvgfvfqhyaLFpHMTVAENIAfgLRVRPPSKAEIRaRVEELLEL--------------VQLEGLadRYpsql 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 474 SGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLagVEA---ADKIVFLENGKT 548
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHDQ--EEAlelADRVVVMNQGRI 212
|
250
....*....|
gi 2218266673 549 EMEGTHEELL 558
Cdd:COG1118 213 EQVGTPDEVY 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
327-560 |
1.16e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 109.16 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 327 AQTLDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLK 405
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTT--------VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 406 DQIADAVAVLNQKPHL-FDTSILNNIRLGN----------GEASDEDVRRAAKQVKlhdyIESLPDGYHTSVqetgirfS 474
Cdd:PRK09536 73 RAASRRVASVPQDTSLsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTG----VAQFADRPVTSL-------S 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 475 GGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFE-VLKGKTILWITHHL-AGVEAADKIVFLENGKTEMEG 552
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRlVDDGKTAVAAIHDLdLAARYCDELVLLADGRVRAAG 221
|
....*...
gi 2218266673 553 THEELLAA 560
Cdd:PRK09536 222 PPADVLTA 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
336-557 |
1.37e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 108.24 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVEtallkdqIADA---- 411
Cdd:COG3839 3 SLELENVSKSYGGV-EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-------VTDLppkd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 --VAVLNQKPHLFDT-SILNNIRLG---NGEASDE---DVRRAAKQVKLHDYIESLPDGyhtsvqetgirFSGGERQRIA 482
Cdd:COG3839 75 rnIAMVFQSYALYPHmTVYENIAFPlklRKVPKAEidrRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 483 LARILLQDTPIIILDEPTVGLDPiterELMETVFEVLK------GKTILWITHHLagVEA---ADKIVFLENGKTEMEGT 553
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDA----KLRVEMRAEIKrlhrrlGTTTIYVTHDQ--VEAmtlADRIAVMNDGRIQQVGT 217
|
....
gi 2218266673 554 HEEL 557
Cdd:COG3839 218 PEEL 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
329-557 |
1.47e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 106.73 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 329 TLDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGvetallkdqi 408
Cdd:COG4152 1 MLELKGLTKRFGDKT--------AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 409 adavavlnqkpHLFDTSILNNI-----------------------RLgNGEASDEDVRRAA---KQVKLHDY----IESL 458
Cdd:COG4152 63 -----------EPLDPEDRRRIgylpeerglypkmkvgeqlvylaRL-KGLSKAEAKRRADewlERLGLGDRankkVEEL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 459 pdgyhtsvqetgirfSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFE-VLKGKTILWITHHLAGVEA- 536
Cdd:COG4152 131 ---------------SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRElAAKGTTVIFSSHQMELVEEl 195
|
250 260
....*....|....*....|.
gi 2218266673 537 ADKIVFLENGKTEMEGTHEEL 557
Cdd:COG4152 196 CDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
337-552 |
1.56e-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: 104.22 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDqiadavaVLN 416
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-------ALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLFDTSILNNIRLGNgeasdEDVRRAAKQVKL-HDYIESLPD--GYHTSVQETGIRFSGGERQRIALARILLQDTPI 493
Cdd:cd03268 73 RIGALIEAPGFYPNLTAR-----ENLRLLARLLGIrKKRIDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 494 IILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGVE-AADKIVFLENGKTEMEG 552
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDqGITVLISSHLLSEIQkVADRIGIINKGKLIEEG 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
337-568 |
1.72e-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: 104.93 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIA-DAVAV 414
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDiTKLPMHKRArLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHLF-DTSILNNIRLGNGEASDEDVRRAAKqvklhdyIESLPDGYH-TSVQET-GIRFSGGERQRIALARILLQDT 491
Cdd:cd03218 80 LPQEASIFrKLTVEENILAVLEIRGLSKKEREEK-------LEELLEEFHiTHLRKSkASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 492 PIIILDEPTVGLDPITERELMETVFEvLKGKTI-LWITHHLA--GVEAADKIVFLENGKTEMEGTHEElLAANERYRRLY 568
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKI-LKDRGIgVLITDHNVreTLSITDRAYIIYEGKVLAEGTPEE-IAANELVRKVY 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
332-560 |
1.73e-25 |
|
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: 104.97 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRDVtfsyDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIAD 410
Cdd:cd03258 4 LKNVSKVFGDT----GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDlTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 A---VAVLNQKPHLFDT-SILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQR 480
Cdd:cd03258 80 ArrrIGMIFQHFNLLSSrTVFENVALPleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 481 IALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEEL 557
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 2218266673 558 LAA 560
Cdd:cd03258 229 FAN 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
340-562 |
1.97e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 106.71 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYDNSS----QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLN-----------GVETALL 404
Cdd:PRK13651 6 KNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkEKEKVLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 405 KD--------------QIADAVAVLNQ--KPHLFDTSILNNIRLGN---GEASDEDVRRAAKQVKLHDyiesLPDGYhts 465
Cdd:PRK13651 86 KLviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPvsmGVSKEEAKKRAAKYIELVG----LDESY--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 466 VQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMEtVFEVL--KGKTILWITHHLAGV-EAADKIVF 542
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE-IFDNLnkQGKTIILVTHDLDNVlEWTKRTIF 237
|
250 260
....*....|....*....|
gi 2218266673 543 LENGKTEMEGTHEELLAANE 562
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSDNK 257
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
340-562 |
2.33e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.59 E-value: 2.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADAVAVLNQK 418
Cdd:PRK13647 8 EDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 419 P--HLFDTSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPdgYHTSVqetgirfsgGERQRIALARILLQD 490
Cdd:PRK13647 88 PddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPP--YHLSY---------GQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 491 TPIIILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHL-AGVEAADKIVFLENGKTEMEG-----THEELLAANE 562
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNqGKTVIVATHDVdLAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAG 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
332-570 |
3.45e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG-----VETALLKd 406
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidySRKGLMK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 407 qIADAVAVLNQKP--HLFDTSILNNIRLG--NGEASDEDVRRAAKQVKLHDYIESLPDG-YHTsvqetgirFSGGERQRI 481
Cdd:PRK13636 80 -LRESVGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDKpTHC--------LSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 482 ALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELL 558
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVF 230
|
250
....*....|....*....
gi 2218266673 559 A-------ANERYRRLYHL 570
Cdd:PRK13636 231 AekemlrkVNLRLPRIGHL 249
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
334-557 |
3.65e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.47 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 334 DVTLSFRDVTFSYD----NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSV-----------TLNG 398
Cdd:PRK13631 19 DIILRVKNLYCVFDekqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkkNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 399 VETALLKDQIADA------VAVLNQKP--HLFDTSILNNIRLG--NGEASDEDVRRAAKQvklhdYIESLPDGYhTSVQE 468
Cdd:PRK13631 99 LITNPYSKKIKNFkelrrrVSMVFQFPeyQLFKDTIEKDIMFGpvALGVKKSEAKKLAKF-----YLNKMGLDD-SYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 469 TGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGV-EAADKIVFLENG 546
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVlEVADEVIVMDKG 252
|
250
....*....|.
gi 2218266673 547 KTEMEGTHEEL 557
Cdd:PRK13631 253 KILKTGTPYEI 263
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
330-552 |
3.79e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 103.51 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGvetALLKDQIA 409
Cdd:cd03269 1 LEVENVTKRFGRVT--------ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 DAVAVLNQKPHLF-DTSILNNIR-------LGNGEASdEDVRRAAKQVKLHDYIESlpdgyhtSVQEtgirFSGGERQRI 481
Cdd:cd03269 70 NRIGYLPEERGLYpKMKVIDQLVylaqlkgLKKEEAR-RRIDEWLERLELSEYANK-------RVEE----LSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 482 ALARILLQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVEA-ADKIVFLENGKTEMEG 552
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
337-549 |
6.50e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 103.28 E-value: 6.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSS---QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIA--- 409
Cdd:COG4181 9 IELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDlFALDEDARArlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 -DAVAVLNQKPHLFDT-SILNNIRLGNGEASDEDVRRAAK----QVKLHDYIESLPDGyhtsvqetgirFSGGERQRIAL 483
Cdd:COG4181 89 aRHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARARalleRVGLGHRLDHYPAQ-----------LSGGEQQRVAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEAADKIVFLENGKTE 549
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRLV 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
337-563 |
9.22e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.83 E-value: 9.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETAllKDQIAD---AV 412
Cdd:PLN03130 1238 IKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIS--KFGLMDlrkVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPHLFDTSILNNIRLGNgEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTP 492
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDPFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 493 IIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLaANER 563
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL-SNEG 1464
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
346-529 |
1.03e-24 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 101.35 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 346 YDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADA---VAVLNQKP--H 420
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERrqrVGLVFQDPddQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 421 LFDTSILNNIRLG--NGEASDEDVRR----AAKQVKLHDYIESLPdgyHTsvqetgirFSGGERQRIALARILLQDTPII 494
Cdd:TIGR01166 81 LFAADVDQDVAFGplNLGLSEAEVERrvreALTAVGASGLRERPT---HC--------LSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 2218266673 495 ILDEPTVGLDPITERELMETVFE-VLKGKTILWITH 529
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRlRAEGMTVVISTH 185
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
337-557 |
1.10e-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: 102.70 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL---KDQiadaVA 413
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpphKRP----VN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQK----PHLfdtSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIAL 483
Cdd:cd03300 76 TVFQNyalfPHL---TVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDpiteRELMETVFEVLK------GKTILWITHHLAgvEA---ADKIVFLENGKTEMEGTH 554
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALD----LKLRKDMQLELKrlqkelGITFVFVTHDQE--EAltmSDRIAVMNKGKIQQIGTP 215
|
...
gi 2218266673 555 EEL 557
Cdd:cd03300 216 EEI 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-548 |
1.17e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 101.47 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 335 VTLSFRDVTFSYDNSS-----QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKP--DSGSVTLNGveTALLKDQ 407
Cdd:cd03213 2 VTLSFRNLTVTVKSSPsksgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLING--RPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 408 IADAVAVLNQKPHLFDTSILnnirlgngeasDEDVRRAAKqvklhdyIESLpdgyhtsvqetgirfSGGERQRIALARIL 487
Cdd:cd03213 80 FRKIIGYVPQDDILHPTLTV-----------RETLMFAAK-------LRGL---------------SGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 488 LQDTPIIILDEPTVGLDPITERELMETvfevLK-----GKTILWITHHLAG--VEAADKIVFLENGKT 548
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSL----LRrladtGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
329-548 |
1.64e-24 |
|
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: 101.96 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 329 TLDLQDVTLSFRDvtfsYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPD---SGSVTLNGVEtaLLK 405
Cdd:cd03234 3 VLPWWDVGLKAKN----WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQP--RKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 406 DQIADAVAVLNQK----PHLFDTSIL---NNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVqetgirfSGGER 478
Cdd:cd03234 77 DQFQKCVAYVRQDdillPGLTVRETLtytAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGI-------SGGER 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEA---ADKIVFLENGKT 548
Cdd:cd03234 150 RRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLfrlFDRILLLSSGEI 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
337-553 |
1.75e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDN----SSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE---TALLKD--Q 407
Cdd:PRK13649 3 INLQNVSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitsTSKNKDikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 408 IADAVAVLNQKP--HLFDTSILNNIRLGN---GEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqETGIRFSGGERQRIA 482
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVLKDVAFGPqnfGVSQEEAEALAREKLALVGISESLFE-------KNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 483 LARILLQDTPIIILDEPTVGLDPITERELMeTVFEVL--KGKTILWITHHLAGV-EAADKIVFLENGKTEMEGT 553
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELM-TLFKKLhqSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
343-574 |
1.79e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.78 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 343 TFSYDNSSqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKD-QIADAVAVLNQKpHL 421
Cdd:PRK11231 9 TVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLPQH-HL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 422 F--DTSILNNIRLGN-------GEASDED---VRRAAKQVKlhdyIESLPDGYHTSVqetgirfSGGERQRIALARILLQ 489
Cdd:PRK11231 87 TpeGITVRELVAYGRspwlslwGRLSAEDnarVNQAMEQTR----INHLADRRLTDL-------SGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 490 DTPIIILDEPTVGLDPITERELMETVFEV-LKGKTILWITHHL-AGVEAADKIVFLENGKTEMEGTHEELLAAnERYRRL 567
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTP-GLLRTV 234
|
....*..
gi 2218266673 568 YHLDVPV 574
Cdd:PRK11231 235 FDVEAEI 241
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
337-563 |
2.20e-24 |
|
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: 103.01 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDsGSVTLNGVE-TALLKDQIADAVAV 414
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSwNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHLFDTSILNNIRlGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPII 494
Cdd:cd03289 82 IPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 495 ILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLaaNER 563
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL--NEK 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
352-540 |
2.50e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 100.72 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 352 VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK--DQIA-----DAVavlnqKPHLfdt 424
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaEACHylghrNAM-----KPAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 425 SILNNIR-----LGNGEAsdeDVRRAAKQVKLHDyIESLPDGYhtsvqetgirFSGGERQRIALARILLQDTPIIILDEP 499
Cdd:PRK13539 89 TVAENLEfwaafLGGEEL---DIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2218266673 500 TVGLDPITERELMETVFEVLK-GKTILWITHHLAGVEAADKI 540
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAqGGIVIAATHIPLGLPGAREL 196
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
336-559 |
4.18e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 107.75 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYDNS-SQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETAL--LKDqIADAV 412
Cdd:PLN03232 1234 SIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgLTD-LRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPHLFDTSILNNIRLGNgEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTP 492
Cdd:PLN03232 1313 SIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 493 IIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLA 559
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
319-557 |
4.35e-24 |
|
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: 102.24 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 319 EASQTESGAQTLDLQDVTLSFRDVTFsydNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG 398
Cdd:cd03291 22 EKAKQENNDRKHSSDDNNLFFSNLCL---VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 399 vetallkdqiadAVAVLNQKPHLFDTSILNNIRLGngEASDE-DVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGE 477
Cdd:cd03291 99 ------------RISFSSQFSWIMPGTIKENIIFG--VSYDEyRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 478 RQRIALARILLQDTPIIILDEPTVGLDPITERELMET-VFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEE 556
Cdd:cd03291 165 RARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSE 244
|
.
gi 2218266673 557 L 557
Cdd:cd03291 245 L 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
337-546 |
5.10e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.39 E-value: 5.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIE--GALKPD---SGSVTLNG-------VETALL 404
Cdd:PRK14239 6 LQVSDLSVYY-NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGhniysprTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 405 KDQIAdavaVLNQKPHLFDTSILNNIRLG---NG----EASDEDVRRAAKQVKLHDYIEslpDGYHTSvqetGIRFSGGE 477
Cdd:PRK14239 85 RKEIG----MVFQQPNPFPMSIYENVVYGlrlKGikdkQVLDEAVEKSLKGASIWDEVK---DRLHDS----ALGLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 478 RQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHL-AGVEAADKIVFLENG 546
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqQASRISDRTGFFLDG 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
330-548 |
8.98e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.72 E-value: 8.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL--KDQ 407
Cdd:COG3845 6 LELRGITKRFGGVV--------ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRspRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 408 IADAVAVLNQKPHLFDT-SILNNIRLGNGEASDE--DVRRAAKQVK-----------LHDYIESLpdgyhtSVqetgirf 473
Cdd:COG3845 78 IALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGrlDRKAARARIRelserygldvdPDAKVEDL------SV------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 474 sgGERQRIALARILLQDTPIIILDEPTVGLDPITERELmetvFEVLK-----GKTILWITHHLAGV-EAADKIVFLENGK 547
Cdd:COG3845 145 --GEQQRVEILKALYRGARILILDEPTAVLTPQEADEL----FEILRrlaaeGKSIIFITHKLREVmAIADRVTVLRRGK 218
|
.
gi 2218266673 548 T 548
Cdd:COG3845 219 V 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
330-549 |
1.39e-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: 98.87 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIA 409
Cdd:cd03301 1 VELENVTKRFGNVT--------ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 DAVAVLNQ---KPHLfdtSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQR 480
Cdd:cd03301 73 DIAMVFQNyalYPHM---TVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 481 IALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHlaGVEA---ADKIVFLENGKTE 549
Cdd:cd03301 139 VALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHD--QVEAmtmADRIAVMNDGQIQ 210
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
337-547 |
1.47e-23 |
|
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: 98.96 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSY---DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDqiADAVA 413
Cdd:TIGR02211 2 LKCENLGKRYqegKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSS--NERAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQK-------PHLF-DTSILNNIR--LGNGEASDEDVRRAA----KQVKLHDYIESLPDgyhtsvqetgiRFSGGERQ 479
Cdd:TIGR02211 80 LRNKKlgfiyqfHHLLpDFTALENVAmpLLIGKKSVKEAKERAyemlEKVGLEHRINHRPS-----------ELSGGERQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 480 RIALARILLQDTPIIILDEPTVGLDPITERELMETVFEV--LKGKTILWITHHLAGVEAADKIVFLENGK 547
Cdd:TIGR02211 149 RVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELnrELNTSFLVVTHDLELAKKLDRVLEMKDGQ 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
336-557 |
1.53e-23 |
|
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: 99.72 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQiADAVAVL 415
Cdd:cd03296 2 SIEVRNVSKRFGDF-VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLF-DTSILNNIRLG----------NGEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALA 484
Cdd:cd03296 80 FQHYALFrHMTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 485 RILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLA-GVEAADKIVFLENGKTEMEGTHEEL 557
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
330-541 |
1.84e-23 |
|
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: 101.28 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRdvtfSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKP---DSGSVTLNGVE------ 400
Cdd:COG0444 2 LEVRNLKVYFP----TRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllklse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 401 -------------------TAL-----LKDQIADAVAVlnqkpHlfdtsilnniRLGNGEASDEDVRRAAKQVKLHD--- 453
Cdd:COG0444 78 kelrkirgreiqmifqdpmTSLnpvmtVGDQIAEPLRI-----H----------GGLSKAEARERAIELLERVGLPDper 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 454 YIESLPdgyHtsvqetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEvLK---GKTILWITHH 530
Cdd:COG0444 143 RLDRYP---H--------ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKD-LQrelGLAILFITHD 210
|
250
....*....|..
gi 2218266673 531 LAGV-EAADKIV 541
Cdd:COG0444 211 LGVVaEIADRVA 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
303-530 |
1.94e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.50 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 303 GYQDSIKRMnRVAPQPEASQTESGAQTLDLQDVTLSFRDvtfsydnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLAL 382
Cdd:COG4178 337 GFEEALEAA-DALPEAASRIETSEDGALALEDLTLRTPD-------GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 383 IEGALKPDSGSVTLNGVETALLkdqiadavavLNQKPHLfdtsILNNIR------LGNGEASDEDVRRAAKQVKLHDYIE 456
Cdd:COG4178 409 IAGLWPYGSGRIARPAGARVLF----------LPQRPYL----PLGTLReallypATAEAFSDAELREALEAVGLGHLAE 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 457 SLPDgyhtsVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHH 530
Cdd:COG4178 475 RLDE-----EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
352-557 |
2.55e-23 |
|
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: 104.99 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 352 VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGvetallkdqiadAVAVLNQKPHLFDTSILNNIR 431
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 432 LGngEASDE-DVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERE 510
Cdd:TIGR01271 509 FG--LSYDEyRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2218266673 511 LMET-VFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEEL 557
Cdd:TIGR01271 587 IFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
336-545 |
2.58e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.94 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPD---SGSVTLNGVETALLKDQiADAV 412
Cdd:COG4136 1 MLSLENLTITL-GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE-QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPHLFD-TSILNNIRLG-----NGEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARI 486
Cdd:COG4136 79 GILFQDDLLFPhLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 487 LLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTI--LWITHHLAGVEAADKIVFLEN 545
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTHDEEDAPAAGRVLDLGN 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
353-557 |
3.02e-23 |
|
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: 100.16 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLNQKPHLFD--TSILNNI 430
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEdlTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 431 RLGN--GEASDEDVRRAA---KQVKLHDYIESLPDGYhtsvqetgirfSGGERQRIALARILLQDTPIIILDEPTVGLDP 505
Cdd:TIGR01188 89 MMGRlyGLPKDEAEERAEellELFELGEAADRPVGTY-----------SGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 506 ITERELMETVFEVLK-GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEEL 557
Cdd:TIGR01188 158 RTRRAIWDYIRALKEeGVTILLTTHYMEEADKlCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
341-557 |
3.84e-23 |
|
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: 97.83 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 341 DVTFSYDNSSQVlDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLNQKPH 420
Cdd:cd03265 5 NLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 421 LFD--TSILNNIRLGN--GEASDEDVRRAAKqvkLHDYIEsLPDGYHTSVQetgiRFSGGERQRIALARILLQDTPIIIL 496
Cdd:cd03265 84 VDDelTGWENLYIHARlyGVPGAERRERIDE---LLDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 497 DEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEEL 557
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
336-568 |
4.07e-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: 98.50 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAV- 414
Cdd:TIGR04406 1 TLVAENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 -LNQKPHLF-DTSILNNIR--LgngEASdEDVRRAAKQVKLHDYIESLpdGYHTSVQETGIRFSGGERQRIALARILLQD 490
Cdd:TIGR04406 80 yLPQEASIFrKLTVEENIMavL---EIR-KDLDRAEREERLEALLEEF--QISHLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 491 TPIIILDEPTVGLDPITERELmETVFEVLKGKTI-LWITHHLA--GVEAADKIVFLENGKTEMEGTHEELLaANERYRRL 567
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAVGDI-KKIIKHLKERGIgVLITDHNVreTLDICDRAYIISDGKVLAEGTPAEIV-ANEKVRRV 231
|
.
gi 2218266673 568 Y 568
Cdd:TIGR04406 232 Y 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
327-547 |
4.72e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.57 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 327 AQTLDLQDVTLSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSL-------ALIEGALKpdSGSVTLNGV 399
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK-QALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGARV--EGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 400 EtaLLKDQIaDAVAV------LNQKPHLFDTSILNNIRLG---NGEAS----DEDVRRAAKQV--------KLHDYiesl 458
Cdd:COG1117 79 D--IYDPDV-DVVELrrrvgmVFQKPNPFPKSIYDNVAYGlrlHGIKSkselDEIVEESLRKAalwdevkdRLKKS---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 459 pdgyhtsvqetGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPI-TER--ELMETvfevLKGK-TILWITHHLAgv 534
Cdd:COG1117 152 -----------ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIsTAKieELILE----LKKDyTIVIVTHNMQ-- 214
|
250
....*....|....*.
gi 2218266673 535 EAA---DKIVFLENGK 547
Cdd:COG1117 215 QAArvsDYTAFFYLGE 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
337-547 |
5.66e-23 |
|
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: 94.82 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETallkdqiadaVAVLN 416
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK----------IGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QkphlfdtsilnnirlgngeasdedvrraakqvklhdyieslpdgyhtsvqetgirFSGGERQRIALARILLQDTPIIIL 496
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 497 DEPTVGLDpITERELMETVFEVLKGkTILWITH---HLAGVeaADKIVFLENGK 547
Cdd:cd03221 95 DEPTNHLD-LESIEALEEALKEYPG-TVILVSHdryFLDQV--ATKIIELEDGK 144
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
220-567 |
1.04e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 103.13 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 220 IDAYEKEEHDWFeleRKKQRFTRWRDFAAQCL--VAGLILLMLFWTAGQQADGELAKTMIAAFVLVVFPLTEaflpLSDA 297
Cdd:PLN03232 505 IQGIRNEELSWF---RKAQLLSAFNSFILNSIpvVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNM----LPNL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 298 LGEVPGYQDSIKRMNRVApqpeASQTESGAQTLDLQDVT--LSFRDVTFSYDN--SSQVLDNFSFTLRQGEKMALLGRSG 373
Cdd:PLN03232 578 LSQVVNANVSLQRIEELL----LSEERILAQNPPLQPGApaISIKNGYFSWDSktSKPTLSDINLEIPVGSLVAIVGGTG 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 374 SGKSTSLALIEGALKP-DSGSVTLNGvetallkdqiadAVAVLNQKPHLFDTSILNNIRLGNGEASdEDVRRAAKQVKLH 452
Cdd:PLN03232 654 EGKTSLISAMLGELSHaETSSVVIRG------------SVAYVPQVSWIFNATVRENILFGSDFES-ERYWRAIDVTALQ 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 453 DYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMET-VFEVLKGKTILWITHHL 531
Cdd:PLN03232 721 HDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQL 800
|
330 340 350
....*....|....*....|....*....|....*.
gi 2218266673 532 AGVEAADKIVFLENGKTEMEGTHEELLAANERYRRL 567
Cdd:PLN03232 801 HFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
337-560 |
1.06e-22 |
|
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: 103.10 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGRSGSGKST-SLALIEgALKPDSGSVTLNGVETALLK-DQIADAVA 413
Cdd:TIGR00957 1285 VEFRNYCLRYrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSlTLGLFR-INESAEGEIIIDGLNIAKIGlHDLRFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPHLFDTSILNNIRlGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPI 493
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 494 IILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAA 560
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
344-546 |
1.06e-22 |
|
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: 96.63 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 344 FSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADA-----VAVLNQK 418
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSrnrysVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 419 PHLFDTSILNNIRLGNgEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDE 498
Cdd:cd03290 88 PWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 499 PTVGLDPITERELM-ETVFEVLKG--KTILWITHHLAGVEAADKIVFLENG 546
Cdd:cd03290 167 PFSALDIHLSDHLMqEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
320-557 |
1.72e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 102.55 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 320 ASQTESGAQTLdlQDVTLSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG 398
Cdd:PTZ00243 1294 ASPTSAAPHPV--QAGSLVFEGVQMRYrEGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 399 VETAL-----LKDQIAdavaVLNQKPHLFDTSILNNIR--LgngEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGI 471
Cdd:PTZ00243 1372 REIGAyglreLRRQFS----MIPQDPVLFDGTVRQNVDpfL---EASSAEVWAALELVGLRERVASESEGIDSRVLEGGS 1444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 472 RFSGGERQRIALARILLQ-DTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEM 550
Cdd:PTZ00243 1445 NYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
|
....*..
gi 2218266673 551 EGTHEEL 557
Cdd:PTZ00243 1525 MGSPREL 1531
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
335-566 |
4.70e-22 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 95.64 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 335 VTLSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKD-----QIA 409
Cdd:COG4598 7 PALEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgelVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 DAVAV-------------LNQKPHLfdtSILNNIRLG----NGEASDEDVRRAAK---QVKLHDYIESLPdgyhtsvqet 469
Cdd:COG4598 86 DRRQLqrirtrlgmvfqsFNLWSHM---TVLENVIEApvhvLGRPKAEAIERAEAllaKVGLADKRDAYP---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 470 gIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPiterelmETVFEVLK--------GKTILWITHHLA-GVEAADKI 540
Cdd:COG4598 153 -AHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEVLKvmrdlaeeGRTMLVVTHEMGfARDVSSHV 224
|
250 260
....*....|....*....|....*...
gi 2218266673 541 VFLENGKTEMEGTHEELLAA--NERYRR 566
Cdd:COG4598 225 VFLHQGRIEEQGPPAEVFGNpkSERLRQ 252
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
337-557 |
6.82e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.59 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYD-NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG--VETALLKDqIADAVA 413
Cdd:PRK13648 8 IVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaITDDNFEK-LRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKP-HLFDTSILN-NIRLG--NGEASDED----VRRAAKQVKLHDYIESLPDGyhtsvqetgirFSGGERQRIALAR 485
Cdd:PRK13648 87 IVFQNPdNQFVGSIVKyDVAFGleNHAVPYDEmhrrVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 486 ILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGK--TILWITHHLAGVEAADKIVFLENGKTEMEGTHEEL 557
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
337-560 |
7.73e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLN 416
Cdd:PRK13537 8 IDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLF-DTSILNNIRLGN---GEASDEDVRRAAKQVKLHDyIESLPDGyhtSVQEtgirFSGGERQRIALARILLQDTP 492
Cdd:PRK13537 87 QFDNLDpDFTVRENLLVFGryfGLSAAAARALVPPLLEFAK-LENKADA---KVGE----LSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 493 IIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELLAA 560
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
337-573 |
1.02e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.57 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYD-NS---SQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQ----- 407
Cdd:PRK13643 2 IKFEKVNYTYQpNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 408 IADAVAVLNQKP--HLFDTSILNNIRLGN---GEASDEDVRRAAKQVKL----HDYIESLPdgyhtsvqetgIRFSGGER 478
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPqnfGIPKEKAEKIAAEKLEMvglaDEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLDPITERELMEtVFEVL--KGKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHE 555
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIhqSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPS 229
|
250
....*....|....*...
gi 2218266673 556 ELLAANErYRRLYHLDVP 573
Cdd:PRK13643 230 DVFQEVD-FLKAHELGVP 246
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
352-537 |
1.06e-21 |
|
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: 93.33 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 352 VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLNQKPHLFDT-SILNNI 430
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTlSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 431 RLGNGEASDEDVRRAAKQVKLHDYiESLPDGYhtsvqetgirFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERE 510
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|....*...
gi 2218266673 511 LMETVFEVL-KGKTILWITHHLAGVEAA 537
Cdd:cd03231 164 FAEAMAGHCaRGGMVVLTTHQDLGLSEA 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
337-556 |
1.17e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK-DQIADAVAVL 415
Cdd:PRK10247 8 LQLQNVGYLAG-DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLFDTSILNN------IRlgnGEASDEDvrraakqvKLHDYIE--SLPDgyhTSVQETGIRFSGGERQRIALARIl 487
Cdd:PRK10247 87 AQTPTLFGDTVYDNlifpwqIR---NQQPDPA--------IFLDDLErfALPD---TILTKNIAELSGGEKQRISLIRN- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 488 LQDTP-IIILDEPTVGLDPITERELMETVFEVLKGKTI--LWITHHLAGVEAADKIVFLENGKTEMEGTHEE 556
Cdd:PRK10247 152 LQFMPkVLLLDEITSALDESNKHNVNEIIHRYVREQNIavLWVTHDKDEINHADKVITLQPHAGEMQEARYE 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
218-561 |
1.22e-21 |
|
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: 100.02 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 218 AFIDAYEKEEHDWFELERKKQRFTRWRDFAAQC---LVAgLILLMLFWTAGQQ--ADGELAKTMIAAFVLVVFPLTeaFL 292
Cdd:TIGR00957 517 AFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCtpfLVA-LITFAVYVTVDENniLDAEKAFVSLALFNILRFPLN--IL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 293 PLsdALGEVPGYQDSIKRMNRVAPQPEASQTESGAQTL-DLQDVTLSFRDVTFSYDNS-SQVLDNFSFTLRQGEKMALLG 370
Cdd:TIGR00957 594 PM--VISSIVQASVSLKRLRIFLSHEELEPDSIERRTIkPGEGNSITVHNATFTWARDlPPTLNGITFSIPEGALVAVVG 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 371 RSGSGKSTSLALIEGALKPDSGSVTLNGvetallkdqiadAVAVLNQKPHLFDTSILNNIRLGngEASDEDVRRAAKQV- 449
Cdd:TIGR00957 672 QVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQAWIQNDSLRENILFG--KALNEKYYQQVLEAc 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 450 KLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVF---EVLKGKTILW 526
Cdd:TIGR00957 738 ALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpeGVLKNKTRIL 817
|
330 340 350
....*....|....*....|....*....|....*
gi 2218266673 527 ITHHLAGVEAADKIVFLENGKTEMEGTHEELLAAN 561
Cdd:TIGR00957 818 VTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRD 852
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
337-567 |
2.72e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 98.66 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQ--VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDS-GSVTLNGvetallkdqiadAVA 413
Cdd:PLN03130 615 ISIKNGYFSWDSKAErpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRG------------TVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPHLFDTSILNNIRLGNgEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPI 493
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGS-PFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 494 IILDEPTVGLDPITERELMETVF-EVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANERYRRL 567
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVFDKCIkDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
83-563 |
2.72e-21 |
|
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: 98.83 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 83 HIILKIVSDMRVRLYNMLEPGALMLRSRFRTGDMLGILSEDIEHLQDAFLKTIFPAISaLLLYAVSVIALGFFSWPFaIL 162
Cdd:TIGR01271 951 HTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQ-LTLIVLGAIFVVSVLQPY-IF 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 163 IALYLFVLVVLFPVVSLLVTRARNAKLKS-GRNVLYSRLTDAVMGVSDWMFSGRRHAFIDAYEK----EEHDWFELERKk 237
Cdd:TIGR01271 1029 IAAIPVAVIFIMLRAYFLRTSQQLKQLESeARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKalnlHTANWFLYLST- 1107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 238 qrfTRWRDFAAQCLVAGLILLMLFWTAGQQADGELAKTMIAAFVLVVfplTEAFLPLSDALGEVPGYQDSIKRMNRVAPQ 317
Cdd:TIGR01271 1108 ---LRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNI---LSTLQWAVNSSIDVDGLMRSVSRVFKFIDL 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 318 P-EASQTESGAQTLDLQDVT----------------LSFRDVTFSY-DNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTS 379
Cdd:TIGR01271 1182 PqEEPRPSGGGGKYQLSTVLvienphaqkcwpsggqMDVQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTL 1261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 380 LALIEGALKPDsGSVTLNGVE-TALLKDQIADAVAVLNQKPHLFDTSILNNIRlGNGEASDEDVRRAAKQVKLHDYIESL 458
Cdd:TIGR01271 1262 LSALLRLLSTE-GEIQIDGVSwNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQF 1339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 459 PDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAAD 538
Cdd:TIGR01271 1340 PDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQ 1419
|
490 500
....*....|....*....|....*
gi 2218266673 539 KIVFLENGKTEMEGTHEELLaaNER 563
Cdd:TIGR01271 1420 QFLVIEGSSVKQYDSIQKLL--NET 1442
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
251-561 |
2.94e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 97.35 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 251 LVAGLILLmLFWTAGQQadgELAKTMIAAfvlvVFPLTEAFL--PLSDALGEVPGYQ------DSIKRMNRVAPQPE--A 320
Cdd:PRK10522 242 MMLGAIGL-VFYMANSL---GWADTNVAA----TYSLTLLFLrtPLLSAVGALPTLLsaqvafNKLNKLALAPYKAEfpR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 321 SQTESGAQTLdlqdvtlSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG-- 398
Cdd:PRK10522 314 PQAFPDWQTL-------ELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkp 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 399 VETALLKDQIADAVAVLNQKpHLFDtSILNNirlGNGEASDEDVRRAAKQVKLHDYIEsLPDGyhtsvQETGIRFSGGER 478
Cdd:PRK10522 387 VTAEQPEDYRKLFSAVFTDF-HLFD-QLLGP---EGKPANPALVEKWLERLKMAHKLE-LEDG-----RISNLKLSKGQK 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEAADKIVFLENGK-TEMEGTHE 555
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQlSELTGEER 535
|
....*.
gi 2218266673 556 ELLAAN 561
Cdd:PRK10522 536 DAASRD 541
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
337-573 |
3.08e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.00 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQV--LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADAVA 413
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELlTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKP--HLFDTSILNNIRLG---NGEASDEDVRR---AAKQVKLHDYIESLPdgyhtsvqetgIRFSGGERQRIALAR 485
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGmenQGIPREEMIKRvdeALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 486 ILLQDTPIIILDEPTVGLDPITERELMETVFEVlKGK---TILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLAANE 562
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEI-KEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
250
....*....|.
gi 2218266673 563 RYRRLyHLDVP 573
Cdd:PRK13642 233 DMVEI-GLDVP 242
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
336-555 |
4.56e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.38 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVL 415
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQK-----------PHLfdtSILNN-----IRLGnGEASDEDVRRAAK---QVKLHDYIESLPdgyhtsvqetgIRFSGG 476
Cdd:COG4161 81 RQKvgmvfqqynlwPHL---TVMENlieapCKVL-GLSKEQAREKAMKllaRLRLTDKADRFP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 477 ERQRIALARILLQDTPIIILDEPTVGLDP-ITE------RELMETvfevlkGKTILWITHHlagVEAADKI----VFLEN 545
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPeITAqvveiiRELSQT------GITQVIVTHE---VEFARKVasqvVYMEK 216
|
250
....*....|
gi 2218266673 546 GKTEMEGTHE 555
Cdd:COG4161 217 GRIIEQGDAS 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
336-555 |
5.73e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 92.38 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKST---SLALIEGalkPDSGSVTLNGVETALLKDQIADAV 412
Cdd:PRK11124 2 SIQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLNIAGNHFDFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQK-----------PHLfdTSILNNIrlgngEA-------SDEDVRRAAKQV----KLHDYIESLPdgyhtsvqetg 470
Cdd:PRK11124 78 RELRRNvgmvfqqynlwPHL--TVQQNLI-----EApcrvlglSKDQALARAEKLlerlRLKPYADRFP----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 471 IRFSGGERQRIALARILLQDTPIIILDEPTVGLDP-ITE------RELMETvfevlkGKTILWITHHlagVEAADKI--- 540
Cdd:PRK11124 140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPeITAqivsiiRELAET------GITQVIVTHE---VEVARKTasr 210
|
250
....*....|....*.
gi 2218266673 541 -VFLENGKTEMEGTHE 555
Cdd:PRK11124 211 vVYMENGHIVEQGDAS 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
339-565 |
7.78e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 91.69 E-value: 7.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 339 FRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE---TALLKDQIADAVAVL 415
Cdd:PRK09493 4 FKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndPKVDERLIRQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLF-DTSILNNIRLGNGE---ASDEDVRRAAK----QVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARIL 487
Cdd:PRK09493 83 FQQFYLFpHLTALENVMFGPLRvrgASKEEAEKQARellaKVGLAERAHHYPS-----------ELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 488 LQDTPIIILDEPTVGLDPiterELMETVFEVLK-----GKTILWITHHLA-GVEAADKIVFLENGKTEMEGTHEELLAA- 560
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDP----ELRHEVLKVMQdlaeeGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIKNp 227
|
....*.
gi 2218266673 561 -NERYR 565
Cdd:PRK09493 228 pSQRLQ 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
341-562 |
8.28e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.76 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 341 DVTFSYDNSS----QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLN------GVETALLKDQIAD 410
Cdd:PRK13645 11 NVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 AVAVLNQKP--HLFDTSILNNIRLGN---GEASDEDVRRAAKQVKLhdyiESLPDGYhtsVQETGIRFSGGERQRIALAR 485
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAFGPvnlGENKQEAYKKVPELLKL----VQLPEDY---VKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 486 ILLQDTPIIILDEPTVGLDPITERELMeTVFEVL---KGKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLAAN 561
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFI-NLFERLnkeYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFSNQ 242
|
.
gi 2218266673 562 E 562
Cdd:PRK13645 243 E 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
352-547 |
8.67e-21 |
|
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: 91.63 E-value: 8.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 352 VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGV----ETALLKDQIAdavAVLNQKPHL-FDTSI 426
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwkRRKKFLRRIG---VVFGQKTQLwWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 427 LNNIRLgNGEASDEDVRRAAKQV-KLHDYIEsLPDGYHTSVQetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLDP 505
Cdd:cd03267 113 IDSFYL-LAAIYDLPPARFKKRLdELSELLD-LEELLDTPVR----QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2218266673 506 ITERELMETVFEV--LKGKTILWITHHLAGVEA-ADKIVFLENGK 547
Cdd:cd03267 187 VAQENIRNFLKEYnrERGTTVLLTSHYMKDIEAlARRVLVIDKGR 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
336-568 |
9.84e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 9.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADA-VA 413
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDiTHLPMHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPHLF-DTSILNNIR--LgngEASDEDvrRAAKQVKLHDYIESLpdgyH-TSVQET-GIRFSGGERQRIALARILL 488
Cdd:COG1137 82 YLPQEASIFrKLTVEDNILavL---ELRKLS--KKEREERLEELLEEF----GiTHLRKSkAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 489 QDTPIIILDEPTVGLDPITERELMETVFEvLKGKTI--LwITHHlaGVEAADKIV----FLENGKTEMEGTHEELLaANE 562
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKIIRH-LKERGIgvL-ITDH--NVRETLGICdrayIISEGKVLAEGTPEEIL-NNP 227
|
....*.
gi 2218266673 563 RYRRLY 568
Cdd:COG1137 228 LVRKVY 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
337-574 |
1.01e-20 |
|
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: 91.68 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSV------TLNGVETALLKDQIAD 410
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgeRRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 AVAVLNQKPH------------LFDTSILNNirlgngEASDEDVRRAA---KQVKLHDYIESLpdgYHTsvqetgirFSG 475
Cdd:COG1119 83 VSPALQLRFPrdetvldvvlsgFFDSIGLYR------EPTDEQRERARellELLGLAHLADRP---FGT--------LSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 476 GERQRIALARILLQDTPIIILDEPTVGLDPItERELMETVFEVL---KGKTILWITHHLA-GVEAADKIVFLENGKTEME 551
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLG-ARELLLALLDKLaaeGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAA 224
|
250 260
....*....|....*....|...
gi 2218266673 552 GTHEELLAAnERYRRLYHLDVPV 574
Cdd:COG1119 225 GPKEEVLTS-ENLSEAFGLPVEV 246
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
348-543 |
1.07e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.99 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 348 NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGvetallkdqiADAVAVLNQKPHLFDT--- 424
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPQRSEVPDSlpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 425 SILNNIRLGN----------GEASDEDVRRAAKQVKLHDYIeslpdgyHTSVQEtgirFSGGERQRIALARILLQDTPII 494
Cdd:NF040873 73 TVRDLVAMGRwarrglwrrlTRDDRAAVDDALERVGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2218266673 495 ILDEPTVGLDPITERELMETV-FEVLKGKTILWITHHLAGVEAADKIVFL 543
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-558 |
1.73e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 318 PEASQTESGAqtldLQDVTLSFRDVTFSYDNSSqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLN 397
Cdd:PRK13536 27 SEAKASIPGS----MSTVAIDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 398 GVETALLKDQIADAVAVLNQkphlFDTSILNNIRLGNGEASDEDVRRAAKQVK-----LHDY--IESLPDgyhTSVQEtg 470
Cdd:PRK13536 102 GVPVPARARLARARIGVVPQ----FDNLDLEFTVRENLLVFGRYFGMSTREIEavipsLLEFarLESKAD---ARVSD-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 471 irFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVEA-ADKIVFLENGKT 548
Cdd:PRK13536 173 --LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRK 250
|
250
....*....|
gi 2218266673 549 EMEGTHEELL 558
Cdd:PRK13536 251 IAEGRPHALI 260
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
337-559 |
1.83e-20 |
|
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: 91.12 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKST-SLALIEGALKPDsGSVTLNGVETALLKDQ-IADAVA 413
Cdd:cd03288 20 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSlSLAFFRMVDIFD-GKIVIDGIDISKLPLHtLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPHLFDTSILNNIRlGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPI 493
Cdd:cd03288 99 IILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 494 IILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLA 559
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
327-553 |
2.32e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.00 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 327 AQTLDLQDVTLSFRDVTFSYDNSSQVlDNFSFTLRQGEKMALLGRSGSGKSTSLA-------LIEGALKpdSGSVTLNGV 399
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAV-KNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 400 EtalLKDQIADAVAV------LNQKPHLFDTSILNNIRLG---NGEASDED--VRRAAKQVKLHDYIESlpdgyhtSVQE 468
Cdd:PRK14243 78 N---LYAPDVDPVEVrrrigmVFQKPNPFPKSIYDNIAYGariNGYKGDMDelVERSLRQAALWDEVKD-------KLKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 469 TGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHL-AGVEAADKIVFLeNGK 547
Cdd:PRK14243 148 SGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFF-NVE 226
|
....*.
gi 2218266673 548 TEMEGT 553
Cdd:PRK14243 227 LTEGGG 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
337-547 |
2.76e-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: 90.63 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSS--------QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQI 408
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 409 ADAV-----AVLNQKPHLFD--TSILNNIR--LGNGEASDEDvRRAAKQVKLHDYIESLPDGYHTSVQEtgirFSGGERQ 479
Cdd:TIGR02769 83 RRAFrrdvqLVFQDSPSAVNprMTVRQIIGepLRHLTSLDES-EQKARIAELLDMVGLRSEDADKLPRQ----LSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 480 RIALARILLQDTPIIILDEPTVGLDpiteRELMETVFEVLK------GKTILWITHHLAGVEA-ADKIVFLENGK 547
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRklqqafGTAYLFITHDLRLVQSfCQRVAVMDKGQ 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
337-540 |
2.77e-20 |
|
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: 88.95 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLN 416
Cdd:TIGR01189 1 LAARNLACSRG-ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHL-FDTSILNNIRLGN--GEASDEDVRRAAKQVKLHDYiESLPDGYhtsvqetgirFSGGERQRIALARILLQDTPI 493
Cdd:TIGR01189 80 HLPGLkPELSALENLHFWAaiHGGAQRTIEDALAAVGLTGF-EDLPAAQ----------LSAGQQRRLALARLWLSRRPL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2218266673 494 IILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVEAADKI 540
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRAHLaRGGIVLLTTHQDLGLVEAREL 196
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
353-546 |
4.46e-20 |
|
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: 89.45 E-value: 4.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVEtalLKDQIADAVAVLNQKPHLFDTSILNNIRL 432
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ---ITEPGPDRMVVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 433 GNGEASdEDVRRAAKQVKLHDYIESLpdGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELM 512
Cdd:TIGR01184 78 AVDRVL-PDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2218266673 513 ETVFEVLK--GKTILWITHHLAgvEA---ADKIVFLENG 546
Cdd:TIGR01184 155 EELMQIWEehRVTVLMVTHDVD--EAlllSDRVVMLTNG 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
332-568 |
5.06e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.55 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGV-----ETALLkd 406
Cdd:PRK11614 1 MEKVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwQTAKI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 407 qIADAVAVLNQKPHLFD-TSILNNIRLGNGEASDEDVRRAAKQVklhdyIESLPDGYHTSVQETGIrFSGGERQRIALAR 485
Cdd:PRK11614 78 -MREAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV-----YELFPRLHERRIQRAGT-MSGGEQQMLAIGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 486 ILLQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHL-AGVEAADKIVFLENGKTEMEGTHEELLaANER 563
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALL-ANEA 229
|
....*
gi 2218266673 564 YRRLY 568
Cdd:PRK11614 230 VRSAY 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
355-549 |
8.21e-20 |
|
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: 88.12 E-value: 8.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 355 NFSFTLrQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGveTALLKDQIA-------DAVAVLNQK----PHLfd 423
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSRKKinlppqqRKIGLVFQQyalfPHL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 424 tSILNNIRLG-NGEASDEDVRRAAKQVKLHDyIESLPDGYhtsVQEtgirFSGGERQRIALARILLQDTPIIILDEPTVG 502
Cdd:cd03297 91 -NVRENLAFGlKRKRNREDRISVDELLDLLG-LDHLLNRY---PAQ----LSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2218266673 503 LDPITERELMETVFEVLK--GKTILWITHHLAGVEA-ADKIVFLENGKTE 549
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQ 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
337-554 |
9.32e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQ----IADAV 412
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKPHLF-DTSILNN--IRLGNGEASDEDVRR----AAKQVKLHDYIESLPdgyhtsvqetgIRFSGGERQRIALAR 485
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNvaIPLIIAGASGDDIRRrvsaALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 486 ILLQDTPIIILDEPTVGLDPITERELMEtVFEVLK--GKTILWITHHLAGVEAAD-KIVFLENGKteMEGTH 554
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILR-LFEEFNrvGVTVLMATHDIGLISRRSyRMLTLSDGH--LHGGV 219
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
330-552 |
9.91e-20 |
|
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: 88.22 E-value: 9.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETA--LLKDq 407
Cdd:TIGR03740 1 LETKNLSKRFGKQT--------AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTrkDLHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 408 iadaVAVLNQKPHLFdtsilnnirlGNGEASDedvrraakQVKLHDYIESLPDGYHTSV------QETGIR----FSGGE 477
Cdd:TIGR03740 72 ----IGSLIESPPLY----------ENLTARE--------NLKVHTTLLGLPDSRIDEVlnivdlTNTGKKkakqFSLGM 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 478 RQRIALARILLQDTPIIILDEPTVGLDP--ITE-RELMETVFEvlKGKTILWITHHLAGVEA-ADKIVFLENGKTEMEG 552
Cdd:TIGR03740 130 KQRLGIAIALLNHPKLLILDEPTNGLDPigIQElRELIRSFPE--QGITVILSSHILSEVQQlADHIGIISEGVLGYQG 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
330-560 |
1.42e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVtfsydnssQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIA 409
Cdd:PRK15439 12 LCARSISKQYSGV--------EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 DAVAV--LNQKPHLF-DTSILNNIRLGNGeasdedvRRAAKQVKLHDYIESLpdGYHTSVQETGIRFSGGERQRIALARI 486
Cdd:PRK15439 84 HQLGIylVPQEPLLFpNLSVKENILFGLP-------KRQASMQKMKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 487 LLQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGV-EAADKIVFLENGKTEMEG-----THEELLA 559
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLaQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGktadlSTDDIIQ 234
|
.
gi 2218266673 560 A 560
Cdd:PRK15439 235 A 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
350-557 |
1.46e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 90.53 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 350 SQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL--KDQiadAVAVLNQKPHLF-DTSI 426
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLhaRDR---KVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 427 LNNIRLG----------NGEASDEDVRRAAKQVKLhdyiESLPDGYHTsvqetgiRFSGGERQRIALARILLQDTPIIIL 496
Cdd:PRK10851 92 FDNIAFGltvlprrerpNAAAIKAKVTQLLEMVQL----AHLADRYPA-------QLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 497 DEPTVGLDPITEREL---METVFEVLKgKTILWITH-HLAGVEAADKIVFLENGKTEMEGTHEEL 557
Cdd:PRK10851 161 DEPFGALDAQVRKELrrwLRQLHEELK-FTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
357-559 |
1.87e-19 |
|
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: 90.17 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 357 SFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVetaLLKDQIAD--------AVAVLNQKPHLF-DTSIL 427
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR---TLFDSRKGiflppekrRIGYVFQEARLFpHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 428 NNIRLGNgeasdEDVRRAAKQVKLHDYIESLPDGyHTSVQETGiRFSGGERQRIALARILLQDTPIIILDEPTVGLDPIT 507
Cdd:TIGR02142 94 GNLRYGM-----KRARPSERRISFERVIELLGIG-HLLGRLPG-RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 508 ERELMeTVFEVLKGKT---ILWITHHLAGVE-AADKIVFLENGKTEMEGTHEELLA 559
Cdd:TIGR02142 167 KYEIL-PYLERLHAEFgipILYVSHSLQEVLrLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
311-557 |
2.77e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.89 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 311 MNRVAPQPEAsQTESGAQTLdlqdvtLSFRDVTFSYDNSSQVlDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPD 390
Cdd:PRK11607 1 MNDAIPRPQA-KTRKALTPL------LEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 391 SGSVTLNGVETALLK------DQIADAVAVLnqkPHLfdtSILNNI-------RLGNGEASDEdVRRAAKQVKLHDYIES 457
Cdd:PRK11607 73 AGQIMLDGVDLSHVPpyqrpiNMMFQSYALF---PHM---TVEQNIafglkqdKLPKAEIASR-VNEMLGLVHMQEFAKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 458 LPdgyHtsvqetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITH-HLAGV 534
Cdd:PRK11607 146 KP---H--------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAM 214
|
250 260
....*....|....*....|...
gi 2218266673 535 EAADKIVFLENGKTEMEGTHEEL 557
Cdd:PRK11607 215 TMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
337-558 |
3.99e-19 |
|
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: 85.66 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEG--ALKPDSGSVTLNGVE-TALLKDQIAdava 413
Cdd:cd03217 1 LEIKDLHVSVGGK-EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDiTDLPPEERA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 vlnqkphlfdtsilnniRLGNGEASDEDVRRAAkqVKLHDYIESLPDGyhtsvqetgirFSGGERQRIALARILLQDTPI 493
Cdd:cd03217 76 -----------------RLGIFLAFQYPPEIPG--VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 494 IILDEPTVGLDpITERELMETVFEVLK--GKTILWITHH--LAGVEAADKIVFLENGKTEMEGTHEELL 558
Cdd:cd03217 126 AILDEPDSGLD-IDALRLVAEVINKLReeGKSVLIITHYqrLLDYIKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
333-556 |
4.82e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.24 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 333 QDVTLSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAV 412
Cdd:PRK09452 11 LSPLVELRGISKSFDGK-EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQK---PHLfdtSILNNIRLG-------NGEAsDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIA 482
Cdd:PRK09452 90 TVFQSYalfPHM---TVFENVAFGlrmqktpAAEI-TPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 483 LARILLQDTPIIILDEPTVGLDpITERELMETVFEVLK---GKTILWITHHLAgvEA---ADKIVFLENGKTEMEGTHEE 556
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALD-YKLRKQMQNELKALQrklGITFVFVTHDQE--EAltmSDRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
334-547 |
5.05e-19 |
|
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: 84.79 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 334 DVTLSFRDVTFSYdnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL--KDQIADA 411
Cdd:cd03215 2 EPVLEVRGLSVKG-----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRspRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKPH---LFDT-SILNNIRLGngeasdedvrraakqvklhdyieslpdgyhtsvqetgIRFSGGERQRIALARIL 487
Cdd:cd03215 77 IAYVPEDRKregLVLDlSVAENIALS-------------------------------------SLLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 488 LQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVEA-ADKIVFLENGK 547
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGlCDRILVMYEGR 181
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
353-559 |
5.33e-19 |
|
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: 90.25 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSV-----------TLNGVetaLLKDQIADAVAVLNQKPHL 421
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmTKPGP---DGRGRAKRYIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 422 F-DTSILNNIRLGNG-EASDEDVRRAA----KQVKL-HDYIESLPDGYHTSVqetgirfSGGERQRIALARILLQDTPII 494
Cdd:TIGR03269 377 YpHRTVLDNLTEAIGlELPDELARMKAvitlKMVGFdEEKAEEILDKYPDEL-------SEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 495 ILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLA 559
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
353-553 |
6.36e-19 |
|
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: 91.23 E-value: 6.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG--VETALlkDQIADAVAVLNQKPHLFD-----TS 425
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdIETNL--DAVRQSLGMCPQHNILFHhltvaEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 426 ILNNIRLgNGEASDEdvrraaKQVKLHDYIESlpDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDP 505
Cdd:TIGR01257 1024 ILFYAQL-KGRSWEE------AQLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2218266673 506 ITERELMETVFEVLKGKTILWITHHLAGVEA-ADKIVFLENGKTEMEGT 553
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
368-560 |
6.76e-19 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 87.93 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 368 LLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIAdAVAVLNQKPHLF-DTSILNNIRLG------NGEASDE 440
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR-HINMVFQSYALFpHMTVEENVAFGlkmrkvPRAEIKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 441 DVRRAAKQVKLHDYIESLPdgyhtsvqetgIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPiTERELMETVFEVLK 520
Cdd:TIGR01187 80 RVLEALRLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDK-KLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2218266673 521 ---GKTILWITHHLAgvEA---ADKIVFLENGKTEMEGTHEELLAA 560
Cdd:TIGR01187 148 eqlGITFVFVTHDQE--EAmtmSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
357-568 |
7.49e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.94 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 357 SFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKD---------QIADAVAVLNQKPHLfdtSIL 427
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrevrrkKIAMVFQSFALMPHM---TVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 428 NNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARILLQDTPIIILDEPTV 501
Cdd:PRK10070 125 DNTAFGmelagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 502 GLDPITERELMETV--FEVLKGKTILWITHHL-AGVEAADKIVFLENGKTEMEGTHEELL--AANERYRRLY 568
Cdd:PRK10070 194 ALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILnnPANDYVRTFF 265
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
357-559 |
8.20e-19 |
|
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: 88.23 E-value: 8.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 357 SFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGveTALLkdqiaDAVAVLNQKPH------------LFDT 424
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG--EVLQ-----DSARGIFLPPHrrrigyvfqearLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 425 -SILNNIRLGngeasdedVRRAAKQ---VKLHDYIESLpdgyhtsvqetGI-----RF----SGGERQRIALARILLQDT 491
Cdd:COG4148 92 lSVRGNLLYG--------RKRAPRAerrISFDEVVELL-----------GIghlldRRpatlSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 492 PIIILDEPTVGLDPITERELMEtVFEVLKGKT---ILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELLA 559
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILP-YLERLRDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
330-566 |
8.60e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.85 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIA 409
Cdd:PRK11432 7 VVLKNITKRFGSNT--------VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 DAVAVLNQK---PHLfdtSILNNIRLG---NGEASDEDVRRAAKQVKLHDyIESLPDGYHTSVqetgirfSGGERQRIAL 483
Cdd:PRK11432 79 DICMVFQSYalfPHM---SLGENVGYGlkmLGVPKEERKQRVKEALELVD-LAGFEDRYVDQI-------SGGQQQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAgvEA---ADKIVFLENGKTEMEGTHEELl 558
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQS--EAfavSDTVIVMNKGKIMQIGSPQEL- 224
|
....*...
gi 2218266673 559 aanerYRR 566
Cdd:PRK11432 225 -----YRQ 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
337-560 |
8.83e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.59 E-value: 8.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETAL--LKDQIADAVAV 414
Cdd:PRK11288 5 LSFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFasTTAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHLF-DTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLpdGYHTSVQETGIRFSGGERQRIALARILLQDTPI 493
Cdd:PRK11288 84 IYQELHLVpEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 494 IILDEPTVGLdpiTERELmETVFEVL-----KGKTILWITHHLAGV-EAADKIVFLENGK-----TEMEG-THEELLAA 560
Cdd:PRK11288 162 IAFDEPTSSL---SAREI-EQLFRVIrelraEGRVILYVSHRMEEIfALCDAITVFKDGRyvatfDDMAQvDRDQLVQA 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
352-529 |
9.70e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.91 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 352 VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVEtalLKDQIADAVAVLNQKPHLFDTSILNNIR 431
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP---VEGPGAERGVVFQNEGLLPWRNVQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 432 LG---NGEASDEDVRRAAKQVKLHDyieslpdgyhtsVQETGIRF----SGGERQRIALARILLQDTPIIILDEPTVGLD 504
Cdd:PRK11248 93 FGlqlAGVEKMQRLEIAHQMLKKVG------------LEGAEKRYiwqlSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*...
gi 2218266673 505 PITeRELMETVFEVL---KGKTILWITH 529
Cdd:PRK11248 161 AFT-REQMQTLLLKLwqeTGKQVLLITH 187
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
349-531 |
1.05e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 349 SSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGveTALLKDQIADAVAVLNQK-------PHL 421
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG--QPMSKLSSAAKAELRNQKlgfiyqfHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 422 F-DTSILNNIRL----GNgeasdedVRRAAKQVKLHDYIESLpdGYHTSVQETGIRFSGGERQRIALARILLQDTPIIIL 496
Cdd:PRK11629 99 LpDFTALENVAMplliGK-------KKPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 2218266673 497 DEPTVGLDPITERELMETVFE--VLKGKTILWITHHL 531
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDL 206
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
330-557 |
1.34e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 87.09 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFR----DVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKS-TSLALIeGALKPD---SGSVTLNGVET 401
Cdd:PRK09473 13 LDVKDLRVTFStpdgDVT--------AVNDLNFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANgriGGSATFNGREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 402 ALLKDQI-----ADAVAVLNQKP------------HLFDTSILNNiRLGNGEASDEDVRR--AAKQVKLHDYIESLPdgy 462
Cdd:PRK09473 84 LNLPEKElnklrAEQISMIFQDPmtslnpymrvgeQLMEVLMLHK-GMSKAEAFEESVRMldAVKMPEARKRMKMYP--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 463 HtsvqetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEvLK---GKTILWITHHLaGVEAA-- 537
Cdd:PRK09473 160 H--------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNE-LKrefNTAIIMITHDL-GVVAGic 229
|
250 260
....*....|....*....|.
gi 2218266673 538 DKIVFLENGKTeME-GTHEEL 557
Cdd:PRK09473 230 DKVLVMYAGRT-MEyGNARDV 249
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
353-567 |
2.23e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.29 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGV-----ETALLKdQIAdavAVLNQKPHLF-DTSI 426
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvpfkrRKEFAR-RIG---VVFGQRSQLWwDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 427 LNNIRLgNGE---ASDEDVRRaakqvKLHDYIE--SLPDGYHTSVQEtgirFSGGERQRIALARILLQDTPIIILDEPTV 501
Cdd:COG4586 114 IDSFRL-LKAiyrIPDAEYKK-----RLDELVEllDLGELLDTPVRQ----LSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 502 GLDPITErelmETVFEVLK------GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELLAANERYRRL 567
Cdd:COG4586 184 GLDVVSK----EAIREFLKeynrerGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTI 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
330-559 |
3.64e-18 |
|
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: 87.55 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVtfsydnssQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEG--ALKPDSGSV------------- 394
Cdd:TIGR03269 1 IEVKNLTKKFDGK--------EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvalcekcgyv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 395 ---------------TLNGVETAL------LKDQIADAVAVLNQKPHLF---DTSILNNIRLGN--GEASDEDVRRAA-- 446
Cdd:TIGR03269 73 erpskvgepcpvcggTLEPEEVDFwnlsdkLRRRIRKRIAIMLQRTFALygdDTVLDNVLEALEeiGYEGKEAVGRAVdl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 447 -KQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTI- 524
Cdd:TIGR03269 153 iEMVQLSHRITHIAR-----------DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIs 221
|
250 260 270
....*....|....*....|....*....|....*..
gi 2218266673 525 LWITHHLAGV--EAADKIVFLENGKTEMEGTHEELLA 559
Cdd:TIGR03269 222 MVLTSHWPEVieDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
327-569 |
4.86e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 327 AQTLDLQDVTLSFRDVTFSYDNSSQ--------------VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSG 392
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRSLKElllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 393 SVTLNGVETALLkdqiadAVAV-LNqkPHLfdtSILNNIRLgNGEA---SDEDVRRAAKQVK----LHDYIeslpdgyHT 464
Cdd:COG1134 82 RVEVNGRVSALL------ELGAgFH--PEL---TGRENIYL-NGRLlglSRKEIDEKFDEIVefaeLGDFI-------DQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 465 SVQetgiRFSGGERQRIALARILLQDTPIIILDEPT-VGLDPITER--ELMETVFEvlKGKTILWITHHLAGVEA-ADKI 540
Cdd:COG1134 143 PVK----TYSSGMRARLAFAVATAVDPDILLVDEVLaVGDAAFQKKclARIRELRE--SGRTVIFVSHSMGAVRRlCDRA 216
|
250 260
....*....|....*....|....*....
gi 2218266673 541 VFLENGKTEMEGTHEELLAAnerYRRLYH 569
Cdd:COG1134 217 IWLEKGRLVMDGDPEEVIAA---YEALLA 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-558 |
4.89e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.81 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVtfsydnssQVLDNFSFTLRQGEKMALLGRSGSGKSTSLA----LIEGALKPD-SGSVTLNG-----V 399
Cdd:PRK14247 4 IEIRDLKVSFGQV--------EVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGqdifkM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 400 ETALLKDQIADAVAVLNQKPHLfdtSILNNIRLG--------NGEASDEDVRRAAKQVKLHDYIESLPDGyhtsvqeTGI 471
Cdd:PRK14247 76 DVIELRRRVQMVFQIPNPIPNL---SIFENVALGlklnrlvkSKKELQERVRWALEKAQLWDEVKDRLDA-------PAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 472 RFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLA-GVEAADKIVFLENGKTEM 550
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQqAARISDYVAFLYKGQIVE 225
|
....*...
gi 2218266673 551 EGTHEELL 558
Cdd:PRK14247 226 WGPTREVF 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
332-559 |
4.96e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 85.51 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRdvtfSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIAD 410
Cdd:COG1135 4 LENLSKTFP----TKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDlTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 A---VAVLNQKPHLFDT-SILNNIRL---GNGEASDEDVRRAA---KQVKLHDYIESLPDgyhtsvqetgiRFSGGERQR 480
Cdd:COG1135 80 ArrkIGMIFQHFNLLSSrTVAENVALpleIAGVPKAEIRKRVAellELVGLSDKADAYPS-----------QLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 481 IALARILLQDTPIIILDEPTVGLDPITERElmetVFEVLK------GKTILWITHHLAGV-EAADKIVFLENGKTEMEGT 553
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRS----ILDLLKdinrelGLTIVLITHEMDVVrRICDRVAVLENGRIVEQGP 224
|
....*.
gi 2218266673 554 HEELLA 559
Cdd:COG1135 225 VLDVFA 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
351-567 |
6.14e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.87 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKD-----QIADAVAVLNQKPHLfdTS 425
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlKVADKNQLRLLRTRL--TM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 426 ILNNIRLGNGEASDEDVRRAAKQV----------KLHDYIESLpdGYHTSVQ-ETGIRFSGGERQRIALARILLQDTPII 494
Cdd:PRK10619 97 VFQHFNLWSHMTVLENVMEAPIQVlglskqeareRAVKYLAKV--GIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 495 ILDEPTVGLDPiterELMETVFEVLK-----GKTILWITHHLA-GVEAADKIVFLENGKTEMEGTHEELLaANERYRRL 567
Cdd:PRK10619 175 LFDEPTSALDP----ELVGEVLRIMQqlaeeGKTMVVVTHEMGfARHVSSHVIFLHQGKIEEEGAPEQLF-GNPQSPRL 248
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
332-547 |
7.52e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.57 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVtLNGveTALLkDQIADA 411
Cdd:PRK11247 8 NQGTPLLLNAVSKRYGER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG--TAPL-AEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKPHLFD-TSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGyhtsvqetgirFSGGERQRIALARILLQD 490
Cdd:PRK11247 83 TRLMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 491 TPIIILDEPTVGLDPITERElMETVFEVL---KGKTILWITHHLA-GVEAADKIVFLENGK 547
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIE-MQDLIESLwqqHGFTVLLVTHDVSeAVAMADRVLLIEEGK 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
351-546 |
1.05e-17 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 82.48 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLN--GVETALLKdqiADAVAVLnqkpHLFDTSI-- 426
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLAQ---ASPREIL----ALRRRTIgy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 427 ----LNNI-R-----------LGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSvqetgirFSGGERQRIALARILLQD 490
Cdd:COG4778 98 vsqfLRVIpRvsaldvvaeplLERGVDREEARARARELLARLNLPERLWDLPPAT-------FSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 491 TPIIILDEPTVGLDPITE---RELMETvfevLK--GKTILWITHHLAGVEA-ADKIVFLENG 546
Cdd:COG4778 171 PPLLLLDEPTASLDAANRavvVELIEE----AKarGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
313-560 |
1.64e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.84 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 313 RVAPQPEASQTESGAQTLDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKP--- 389
Cdd:PRK14271 5 RLGGQSGAADVDAAAPAMAAVNLTLGFAGKT--------VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 390 --DSGSVTLNGVETALLKD--QIADAVAVLNQKPHLFDTSILNNIRLG--NGEASDEDVRRAAKQVKLHDYieSLPDGYH 463
Cdd:PRK14271 77 yrYSGDVLLGGRSIFNYRDvlEFRRRVGMLFQRPNPFPMSIMDNVLAGvrAHKLVPRKEFRGVAQARLTEV--GLWDAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 464 TSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLA-GVEAADKIVF 542
Cdd:PRK14271 155 DRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAAL 234
|
250
....*....|....*...
gi 2218266673 543 LENGKTEMEGTHEELLAA 560
Cdd:PRK14271 235 FFDGRLVEEGPTEQLFSS 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
330-560 |
1.75e-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: 85.51 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDvtfsYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKS-TSLALI----EGALKPdSGSVTLNGVEtaLL 404
Cdd:COG4172 7 LSVEDLSVAFGQ----GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILrllpDPAAHP-SGSILFDGQD--LL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 405 KDQIA-------DAVAVLNQKPHlfdTSiLN-----------NIRLGNGeASDEDVRRAA----KQVKLHDyIESLPDGY 462
Cdd:COG4172 80 GLSERelrrirgNRIAMIFQEPM---TS-LNplhtigkqiaeVLRLHRG-LSGAAARARAlellERVGIPD-PERRLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 463 -HtsvqetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEvLK---GKTILWITHHLAGV-EAA 537
Cdd:COG4172 154 pH--------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKD-LQrelGMALLLITHDLGVVrRFA 224
|
250 260
....*....|....*....|...
gi 2218266673 538 DKIVFLENGKTEMEGTHEELLAA 560
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAA 247
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
351-529 |
2.46e-17 |
|
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: 81.28 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLN--GVETALLKDQIADAVAV-----------LNQ 417
Cdd:TIGR02324 22 PVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRheGAWVDLAQASPREVLEVrrktigyvsqfLRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 418 KPHLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSvqetgirFSGGERQRIALARILLQDTPIIILD 497
Cdd:TIGR02324 102 IPRVSALEVVAEPLLERGVPREAARARARELLARLNIPERLWHLPPAT-------FSGGEQQRVNIARGFIADYPILLLD 174
|
170 180 190
....*....|....*....|....*....|...
gi 2218266673 498 EPTVGLDPITERELMETVFEVL-KGKTILWITH 529
Cdd:TIGR02324 175 EPTASLDAANRQVVVELIAEAKaRGAALIGIFH 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
348-566 |
3.74e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.33 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 348 NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-------------TALLKDQIADAVAV 414
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarslsqqkglIRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 415 LNQKPHlfdTSILNNIRLG----NGEASDEDVRRAAK---QVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARIL 487
Cdd:PRK11264 94 FNLFPH---RTVLENIIEGpvivKGEPKEEATARAREllaKVGLAGKETSYPR-----------RLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 488 LQDTPIIILDEPTVGLDPITERELMETVFEVLKGK-TILWITHHLA-GVEAADKIVFLENGKTEMEGTHEELLAA--NER 563
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFADpqQPR 239
|
...
gi 2218266673 564 YRR 566
Cdd:PRK11264 240 TRQ 242
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-547 |
5.34e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 346 YDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSL------------ALIEGALKPDSGSVTLNGVETALLKDQIADAVA 413
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrllelneeARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQKPHLfdtSILNNIRLG---NG-----EASDEDVRRAAKQVKLHDYIESLPDGYHTSVqetgirfSGGERQRIALAR 485
Cdd:PRK14267 93 YPNPFPHL---TIYDNVAIGvklNGlvkskKELDERVEWALKKAALWDEVKDRLNDYPSNL-------SGGQRQRLVIAR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 486 ILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWITHHLA-GVEAADKIVFLENGK 547
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAqAARVSDYVAFLYLGK 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
351-568 |
1.05e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.94 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL--KDQIADAVAVLNQKPHLFDT-SIL 427
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplHARARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 428 NNIrlgngeASDEDVRRAAKQVKLHDYIESLPDGYHTS--VQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDP 505
Cdd:PRK10895 97 DNL------MAVLQIRDDLSAEQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 506 ITERELmETVFEVLK--GKTILWITHHL-AGVEAADKIVFLENGKTEMEGTHEELLaANERYRRLY 568
Cdd:PRK10895 171 ISVIDI-KRIIEHLRdsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL-QDEHVKRVY 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
348-558 |
1.30e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 348 NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPD---SGSVTLNGveTALLKDQIADAVAVLNQ------- 417
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNG--MPIDAKEMRAISAYVQQddlfipt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 418 ---KPHLFDTSILnniRLGNGEASDEdvRRAAKQVKLHDYieSLPDGYHTSVQETGIR--FSGGERQRIALARILLQDTP 492
Cdd:TIGR00955 114 ltvREHLMFQAHL---RMPRRVTKKE--KRERVDEVLQAL--GLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 493 IIILDEPTVGLDPITERELMETVFEV-LKGKTILWITH----HLagVEAADKIVFLENGKTEMEGTHEELL 558
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHqpssEL--FELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
351-566 |
1.36e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKSTS-LALIEgaLKPDSGSVTLNGVETALLKDQ----IADAVAVLNQKPHlfdtS 425
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTgLALLR--LINSQGEIWFDGQPLHNLNRRqllpVRHRIQVVFQDPN----S 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 426 ILNNiRLG----------------NGEASDEDVRRAAKQVKLHdyieslPDGYHTSVQEtgirFSGGERQRIALARILLQ 489
Cdd:PRK15134 374 SLNP-RLNvlqiieeglrvhqptlSAAQREQQVIAVMEEVGLD------PETRHRYPAE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 490 DTPIIILDEPTVGLDpiteRELMETVFEVLKG------KTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELLAA-N 561
Cdd:PRK15134 443 KPSLIILDEPTSSLD----KTVQAQILALLKSlqqkhqLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAApQ 518
|
....*
gi 2218266673 562 ERYRR 566
Cdd:PRK15134 519 QEYTR 523
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
351-546 |
2.08e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIAD--AVAVLNQKPHLFDT-SIL 427
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAqlGIGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 428 NNIRLGngeasdedvRRAAKQ---VKLHDYIE--------SLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIIL 496
Cdd:PRK09700 99 ENLYIG---------RHLTKKvcgVNIIDWREmrvraammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 497 DEPTVGLdpiTERELmETVFEVLK-----GKTILWITHHLAGVEA-ADKIVFLENG 546
Cdd:PRK09700 170 DEPTSSL---TNKEV-DYLFLIMNqlrkeGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
354-567 |
4.21e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 354 DNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIADAVAVLNQ----KPHLfdtSILNN 429
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHqpgiKTEL---TALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 430 IRL---GNGEASDEDVRRAAKQVKLHDYiESLPDGYhtsvqetgirFSGGERQRIALARILLQDTPIIILDEPTVGLDPi 506
Cdd:PRK13538 95 LRFyqrLHGPGDDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQRRVALARLWLTRAPLWILDEPFTAIDK- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 507 terelmetvfevlkgKTILWITHHLAGVEAADKIVFLengkTemegTHEELLAANERYRRL 567
Cdd:PRK13538 163 ---------------QGVARLEALLAQHAEQGGMVIL----T----THQDLPVASDKVRKL 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-560 |
6.86e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.50 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKST-SLALIegALKPDSGSVTLNGVETALLKD----------QIA--DAVAVLN--- 416
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlGLALL--RLIPSEGEIRFDGQDLDGLSRralrplrrrmQVVfqDPFGSLSprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 ------------QKPHLfdtsilnnirlgNGEASDEDVRRAAKQVKLHdyieslPDGYHtsvqetgiR----FSGGERQR 480
Cdd:COG4172 380 tvgqiiaeglrvHGPGL------------SAAERRARVAEALEEVGLD------PAARH--------RypheFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 481 IALARILLQDTPIIILDEPTVGLDpiteRELMETVFEVLK------GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGT 553
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALD----VSVQAQILDLLRdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
....*..
gi 2218266673 554 HEELLAA 560
Cdd:COG4172 510 TEQVFDA 516
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
337-555 |
9.47e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.03 E-value: 9.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEG--ALKPDSGSVTLNGVE-TALLKDQIADA-- 411
Cdd:COG0396 1 LEIKNLHVSVEGK-EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDiLELSPDERARAgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 ------------VAVLNqkphlFDTSILNNIRLGNGEASD--EDVRRAAKQVKL-HDYIE-SLPDGyhtsvqetgirFSG 475
Cdd:COG0396 80 flafqypveipgVSVSN-----FLRTALNARRGEELSAREflKLLKEKMKELGLdEDFLDrYVNEG-----------FSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 476 GERQRIALARILLQDTPIIILDEPTVGLDpIterELMETVFEVL-----KGKTILWITHH---LAGVEaADKIVFLENGK 547
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLD-I---DALRIVAEGVnklrsPDRGILIITHYqriLDYIK-PDFVHVLVDGR 218
|
....*...
gi 2218266673 548 TEMEGTHE 555
Cdd:COG0396 219 IVKSGGKE 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
351-552 |
1.26e-15 |
|
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: 76.03 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLkdqiaDAVAVLNqkPHLfdtSILNNI 430
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-----GLGGGFN--PEL---TGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 431 RLgNGEASdeDVRRAAKQVKLHDYIE--SLPDGYHTSVQEtgirFSGGERQRIALARILLQDTPIIILDEPT-VGlDPIT 507
Cdd:cd03220 106 YL-NGRLL--GLSRKEIDEKIDEIIEfsELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLaVG-DAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2218266673 508 ERELMETVFEVLK-GKTILWITHHLAGVEA-ADKIVFLENGKTEMEG 552
Cdd:cd03220 178 QEKCQRRLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
341-529 |
1.32e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.99 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 341 DVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTlngVETALlkdqiadAVAVLNQKPH 420
Cdd:PRK11147 324 NVNYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH---CGTKL-------EVAYFDQHRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 421 LFD--TSILNNIRLGNGEASDEDVRRAAKQVkLHDYIESlPDGYHTSVQEtgirFSGGERQRIALARILLQDTPIIILDE 498
Cdd:PRK11147 393 ELDpeKTVMDNLAEGKQEVMVNGRPRHVLGY-LQDFLFH-PKRAMTPVKA----LSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190
....*....|....*....|....*....|.
gi 2218266673 499 PTVGLDpITERELMETVFEVLKGkTILWITH 529
Cdd:PRK11147 467 PTNDLD-VETLELLEELLDSYQG-TVLLVSH 495
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
334-560 |
1.55e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 334 DVTLSFRDVTfsydnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKdqIADAVA 413
Cdd:COG1129 254 EVVLEVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS--PRDAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 ---------------VLNQkphlfdtSILNNIRLgngeASDEDVRRA-----AKQVKL-HDYIESL---PDGYHTSVQEt 469
Cdd:COG1129 327 agiayvpedrkgeglVLDL-------SIRENITL----ASLDRLSRGglldrRRERALaEEYIKRLrikTPSPEQPVGN- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 470 girFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFE-VLKGKTILWIT---HHLAGVeaADKIVFLEN 545
Cdd:COG1129 395 ---LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVISselPELLGL--SDRILVMRE 469
|
250 260
....*....|....*....|
gi 2218266673 546 GK--TEMEG---THEELLAA 560
Cdd:COG1129 470 GRivGELDReeaTEEAIMAA 489
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
348-568 |
1.77e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 348 NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSL----ALIEGALKPDS------GSVTLNGVETALLKDQIADAVAVLNQ 417
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGShiellgRTVQREGRLARDIRKSRANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 418 KPHLFDTSILNNI---RLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPII 494
Cdd:PRK09984 95 FNLVNRLSVLENVligALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 495 ILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHL-AGVEAADKIVFLENGKTEMEGTHEELlaANERYRRLY 568
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVdYALRYCERIVALRQGHVFYDGSSQQF--DNERFDHLY 249
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
330-547 |
2.36e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRdvtfSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTsLALIEGAL-KPDSGSVTLNGVETALLKDqi 408
Cdd:PRK10535 5 LELKDIRRSYP----SGEEQVEVLKGISLDIYAGEMVAIVGASGSGKST-LMNILGCLdKPTSGTYRVAGQDVATLDA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 409 aDAVAVLN--------QKPHLFD-TSILNNIRLGNGEASDEdvrRAAKQVKLHDYIESLPDGYHTSVQETgiRFSGGERQ 479
Cdd:PRK10535 78 -DALAQLRrehfgfifQRYHLLShLTAAQNVEVPAVYAGLE---RKQRLLRAQELLQRLGLEDRVEYQPS--QLSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 480 RIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVEAADKIVFLENGK 547
Cdd:PRK10535 152 RVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGE 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
340-566 |
3.07e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.96 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYDNSSqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVET-ALLKDQIADA---VAVL 415
Cdd:PRK11831 11 RGVSFTRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLYTVrkrMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLF-DTSILNNIRLGNGEASD--EDVRRAAKQVKLhdyiESLpdGYHTSVQETGIRFSGGERQRIALARILLQDTP 492
Cdd:PRK11831 90 FQSGALFtDMNVFDNVAYPLREHTQlpAPLLHSTVMMKL----EAV--GLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 493 IIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLAANERYRR 566
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQALQANPDPRVR 240
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
349-547 |
3.61e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.88 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 349 SSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDqiADAVAVLNQKPHLFDTSI-L 427
Cdd:PRK10419 24 HQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR--AQRKAFRRDIQMVFQDSIsA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 428 NNIRLGNGEASDEDVR------RAAKQVKLHDYIES--LPDGYhtsVQETGIRFSGGERQRIALARILLQDTPIIILDEP 499
Cdd:PRK10419 102 VNPRKTVREIIREPLRhllsldKAERLARASEMLRAvdLDDSV---LDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 500 TVGLDpiteRELMETVFEVLK------GKTILWITHHLAGVEA-ADKIVFLENGK 547
Cdd:PRK10419 179 VSNLD----LVLQAGVIRLLKklqqqfGTACLFITHDLRLVERfCQRVMVMDNGQ 229
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
328-560 |
3.79e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.51 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 328 QTLDLQDVTLSfrdvtfsydnSSQVL-DNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPD----SGSVTLNGVETA 402
Cdd:PRK10418 3 QQIELRNIALQ----------AAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 403 LlKDQIADAVAVLNQKPHlfdtSILNNIR----------LGNGEASDEDVRRAA-KQVKLHDyIESLPDGYhtsvqetGI 471
Cdd:PRK10418 73 P-CALRGRKIATIMQNPR----SAFNPLHtmhtharetcLALGKPADDATLTAAlEAVGLEN-AARVLKLY-------PF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 472 RFSGGERQRIALARILLQDTPIIILDEPTVGLDPITER---ELMETVFEVlKGKTILWITHHLaGVEA--ADKIVFLENG 546
Cdd:PRK10418 140 EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQArilDLLESIVQK-RALGMLLVTHDM-GVVArlADDVAVMSHG 217
|
250
....*....|....
gi 2218266673 547 KTEMEGTHEELLAA 560
Cdd:PRK10418 218 RIVEQGDVETLFNA 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
256-559 |
3.82e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.05 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 256 ILLMLFWTAGQQADGELAKTmiaafvlVVFPLTEAFLPLSDALGEVPGYQDSikrMNRVAPQPEASQTESGAQTLDLQDV 335
Cdd:PTZ00243 601 ALRMLCCEQCRPTKRHPSPS-------VVVEDTDYGSPSSASRHIVEGGTGG---GHEATPTSERSAKTPKMKTDDFFEL 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TlsfrdvtfsydnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVtlngvetallkdQIADAVAVL 415
Cdd:PTZ00243 671 E------------PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------------WAERSIAYV 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLFDTSILNNIrLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIII 495
Cdd:PTZ00243 727 PQQAWIMNATVRGNI-LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYL 805
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 496 LDEPTVGLDP-ITERELMETVFEVLKGKTILWITHHLAGVEAADKIVFLENGKTEMEGTHEELLA 559
Cdd:PTZ00243 806 LDDPLSALDAhVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-534 |
4.23e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.46 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYDnSSQVLDNFSFTLRQGEKMALLGRSGSGKST------SLALIEGALKPDsGSVTLNG---VETALLKDQIAD 410
Cdd:PRK14258 11 NNLSFYYD-TQKILEGVSMEIYQSKVTAIIGPSGCGKSTflkclnRMNELESEVRVE-GRVEFFNqniYERRVNLNRLRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 AVAVLNQKPHLFDTSILNNIRLGNGEAS-------DEDVRRAAKQVKLHDYIESlpdgyhtSVQETGIRFSGGERQRIAL 483
Cdd:PRK14258 89 QVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpkleiDDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELmETVFEVLKGK---TILWITHHLAGV 534
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRselTMVIVSHNLHQV 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-531 |
7.79e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 74.74 E-value: 7.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsyDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQI 408
Cdd:COG1101 2 LELKNLSKTFNPGT---VNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 409 ADAVAVLNQKPHL---FDTSILNN------------IRLGNGEASDEDVRRAAKQV------KLHDYIESLpdgyhtsvq 467
Cdd:COG1101 79 AKYIGRVFQDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLglglenRLDTKVGLL--------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 468 etgirfSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGK--TILWITHHL 531
Cdd:COG1101 150 ------SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNM 209
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
330-572 |
1.67e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.43 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRdvtfsydnssqvLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALkPDSGSVTLNGvetALLKDQIA 409
Cdd:PRK03695 1 MQLNDVAVSTR------------LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAG---QPLEAWSA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 DAVAVL------NQKP----HLFDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIeslpdgyHTSVQetgiRFSGGERQ 479
Cdd:PRK03695 65 AELARHraylsqQQTPpfamPVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKL-------GRSVN----QLSGGEWQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 480 RIALARILLQDTPII-------ILDEPTVGLDpITERELMETVFEVL--KGKTILWITHHLAGV-EAADKIVFLENGKTE 549
Cdd:PRK03695 134 RVRLAAVVLQVWPDInpagqllLLDEPMNSLD-VAQQAALDRLLSELcqQGIAVVMSSHDLNHTlRHADRVWLLKQGKLL 212
|
250 260
....*....|....*....|...
gi 2218266673 550 MEGTHEELLAAnERYRRLYHLDV 572
Cdd:PRK03695 213 ASGRRDEVLTP-ENLAQVFGVNF 234
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
337-530 |
2.01e-14 |
|
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: 71.03 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLkdqiadavavLN 416
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLF----------LP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLfdtsILNNIRlgngeasdEDVRRAAKQVklhdyieslpdgyhtsvqetgirFSGGERQRIALARILLQDTPIIIL 496
Cdd:cd03223 71 QRPYL----PLGTLR--------EQLIYPWDDV-----------------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....
gi 2218266673 497 DEPTVGLDPITERELMETVFEvlKGKTILWITHH 530
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
333-560 |
2.30e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 333 QDVTLSFRDVTFSYDNSSqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQ-IADA 411
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRT-LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQK-PHLFDTSILNNIRLGN----------GEASDEDVRRAAKQVKLHDYIESLPDGyhtsvqetgirFSGGERQR 480
Cdd:PRK10575 87 VAYLPQQlPAAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 481 IALARILLQDTPIIILDEPTVGLDPITERELMETVFEV--LKGKTILWITHHL-AGVEAADKIVFLENGKTEMEGTHEEL 557
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDInMAARYCDYLVALRGGEMIAQGTPAEL 235
|
...
gi 2218266673 558 LAA 560
Cdd:PRK10575 236 MRG 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
332-557 |
2.61e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG--VETALLKDQIA 409
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqpTRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 ---DAVAVLNQKPHLFDTSILNNiRLGN------GEASD-EDVRRAAKQVKLHDYieslpdgYHTSVQEtgirFSGGERQ 479
Cdd:PRK15056 82 yvpQSEEVDWSFPVLVEDVVMMG-RYGHmgwlrrAKKRDrQIVTAALARVDMVEF-------RHRQIGE----LSGGQKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 480 RIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGV-EAADKIVF-----LENGKTEMEG 552
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVtEFCDYTVMvkgtvLASGPTETTF 229
|
....*
gi 2218266673 553 THEEL 557
Cdd:PRK15056 230 TAENL 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
332-504 |
3.50e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFrdvtfsydNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVtlngvetallKDQIADA 411
Cdd:PRK09544 7 LENVSVSF--------GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKPHLFDT---SILNNIRLGNGeASDEDVRRAAKQVKLHDYIESlpdgyhtSVQetgiRFSGGERQRIALARILL 488
Cdd:PRK09544 69 IGYVPQKLYLDTTlplTVNRFLRLRPG-TKKEDILPALKRVQAGHLIDA-------PMQ----KLSGGETQRVLLARALL 136
|
170
....*....|....*.
gi 2218266673 489 QDTPIIILDEPTVGLD 504
Cdd:PRK09544 137 NRPQLLVLDEPTQGVD 152
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
342-570 |
8.36e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.94 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 342 VTFSYDNSSqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETA-LLKDQIADAVAVLNQkph 420
Cdd:PRK10253 13 LTLGYGKYT-VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASKEVARRIGLLAQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 421 lfdtsilNNIRLGNGEASDEDVR-RAAKQVKLHDYIESLPDGYHTSVQETGIR---------FSGGERQRIALARILLQD 490
Cdd:PRK10253 89 -------NATTPGDITVQELVARgRYPHQPLFTRWRKEDEEAVTKAMQATGIThladqsvdtLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 491 TPIIILDEPTVGLDPITERELMETVFEV--LKGKTILWITHHL-AGVEAADKIVFLENGKTEMEGTHEELLAAnERYRRL 567
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVTA-ELIERI 240
|
...
gi 2218266673 568 YHL 570
Cdd:PRK10253 241 YGL 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
351-504 |
8.41e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 72.69 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKST---SLALIEgalKPDSGSVTLNGVEtALLKDQIADA-----VAVLNQKPH-- 420
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTlarLLTMIE---TPTGGELYYQGQD-LLKADPEAQKllrqkIQIVFQNPYgs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 421 ---------LFDTSILNNIRLGNGEASdEDVRRAAKQVKLHdyieslPDGY----HTsvqetgirFSGGERQRIALARIL 487
Cdd:PRK11308 105 lnprkkvgqILEEPLLINTSLSAAERR-EKALAMMAKVGLR------PEHYdrypHM--------FSGGQRQRIAIARAL 169
|
170
....*....|....*..
gi 2218266673 488 LQDTPIIILDEPTVGLD 504
Cdd:PRK11308 170 MLDPDVVVADEPVSALD 186
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
353-504 |
8.47e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 72.46 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTsLA-LIEGALKPDSGSVTLNGVETALLKD----------QIA--DAVAVLNQKP 419
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKST-LGrLLLRLEEPTSGEILFDGQDITGLSGrelrplrrrmQMVfqDPYASLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 420 HLFDT---SILNNiRLGNGEASDEDVRRAAKQVKLH-DYIESLPdgyHTsvqetgirFSGGERQRIALARILLQDTPIII 495
Cdd:COG4608 113 TVGDIiaePLRIH-GLASKAERRERVAELLELVGLRpEHADRYP---HE--------FSGGQRQRIGIARALALNPKLIV 180
|
....*....
gi 2218266673 496 LDEPTVGLD 504
Cdd:COG4608 181 CDEPVSALD 189
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
330-548 |
1.13e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.42 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTsLALIEGALKPD---SGSVTLNG--VETALL 404
Cdd:PRK13549 6 LEMKNITKTFGGVK--------ALDNVSLKVRAGEIVSLCGENGAGKST-LMKVLSGVYPHgtyEGEIIFEGeeLQASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 405 KDQIADAVAVLNQK----PHLfdtSILNNIRLGNgEAS-------DEDVRRAAK---QVKLHdyIESlpdgyHTSVQETG 470
Cdd:PRK13549 77 RDTERAGIAIIHQElalvKEL---SVLENIFLGN-EITpggimdyDAMYLRAQKllaQLKLD--INP-----ATPVGNLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 471 irfsGGERQRIALARILLQDTPIIILDEPTVGLdpiTERElMETVFEVLK-----GKTILWITHHLAGVEA-ADKIVFLE 544
Cdd:PRK13549 146 ----LGQQQLVEIAKALNKQARLLILDEPTASL---TESE-TAVLLDIIRdlkahGIACIYISHKLNEVKAiSDTICVIR 217
|
....
gi 2218266673 545 NGKT 548
Cdd:PRK13549 218 DGRH 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
367-556 |
1.19e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 367 ALLGRSGSGKSTSLALIEGALKPDSGSVTLNGvetallkDQIADAVAVLNQKPH------------LF-DTSILNNIRLG 433
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-------RVLFDAEKGICLPPEkrrigyvfqdarLFpHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 434 NGEASDEDVrraAKQVKLHDyIESLPDGYhtsvqetGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELM- 512
Cdd:PRK11144 101 MAKSMVAQF---DKIVALLG-IEPLLDRY-------PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLp 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2218266673 513 --ETVFEVLKgKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEE 556
Cdd:PRK11144 170 ylERLAREIN-IPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
330-560 |
2.40e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRdvtfSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKS-TSLALIEgaLKPD------SGSVTLNG---- 398
Cdd:PRK15134 6 LAIENLSVAFR----QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILR--LLPSppvvypSGDIRFHGesll 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 399 -VETALLKDQIADAVAVLNQKP-------HLFDTSILNNIRLGNG---EASDED---------VRRAAKqvKLHDYIESL 458
Cdd:PRK15134 80 hASEQTLRGVRGNKIAMIFQEPmvslnplHTLEKQLYEVLSLHRGmrrEAARGEilncldrvgIRQAAK--RLTDYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 459 pdgyhtsvqetgirfSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEvLKGK---TILWITHHLAGV- 534
Cdd:PRK15134 158 ---------------SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRE-LQQElnmGLLFITHNLSIVr 221
|
250 260
....*....|....*....|....*.
gi 2218266673 535 EAADKIVFLENGKTEMEGTHEELLAA 560
Cdd:PRK15134 222 KLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
337-562 |
2.42e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSV-----TLNGVETALLKdqIADA 411
Cdd:PRK13638 2 LATSDLWFRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkPLDYSKRGLLA--LRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKP--HLFDTSILNNI--RLGN-GEASDEDVRRAakqvklhDYIESLPDGYHTSVQETGIrFSGGERQRIALARI 486
Cdd:PRK13638 79 VATVFQDPeqQIFYTDIDSDIafSLRNlGVPEAEITRRV-------DEALTLVDAQHFRHQPIQC-LSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 487 LLQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLAANE 562
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
337-504 |
2.99e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.95 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLkDQIADAVAvln 416
Cdd:PRK11701 7 LSVRGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR-DLYALSEA--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLFDT-----------------SILNNI--RL-GNGEASDEDVRRAAKQ----VKLH-DYIESLPDgyhtsvqetgi 471
Cdd:PRK11701 82 ERRRLLRTewgfvhqhprdglrmqvSAGGNIgeRLmAVGARHYGDIRATAGDwlerVEIDaARIDDLPT----------- 150
|
170 180 190
....*....|....*....|....*....|...
gi 2218266673 472 RFSGGERQRIALARILLQDTPIIILDEPTVGLD 504
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
331-560 |
3.87e-13 |
|
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: 71.78 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 331 DLQDVTLSFRDVT-FSYDNSS-QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPD-SGSVTLNG--VETALLK 405
Cdd:TIGR02633 252 EIGDVILEARNLTcWDVINPHrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 406 DQIADAVAVL--NQKPH--LFDTSILNNIRLG-----------NGEASDEDVRRAAKQVKLHDYIESLPDGyhtsvqetg 470
Cdd:TIGR02633 332 QAIRAGIAMVpeDRKRHgiVPILGVGKNITLSvlksfcfkmriDAAAELQIIGSAIQRLKVKTASPFLPIG--------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 471 iRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFE-VLKGKTILWITHHLAGVEA-ADKIVFLENGKT 548
Cdd:TIGR02633 403 -RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
250
....*....|....*..
gi 2218266673 549 E-----MEGTHEELLAA 560
Cdd:TIGR02633 482 KgdfvnHALTQEQVLAA 498
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
355-567 |
5.08e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.43 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 355 NFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG---------VETALLKDQIADAVAVLNQKP---HLF 422
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysYRSQRIRMIFQDPSTSLNPRQrisQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 423 DTSILNNIRLgNGEASDEDVRRAAKQVKLhdyiesLPD--GYHTSVqetgirFSGGERQRIALARILLQDTPIIILDEPT 500
Cdd:PRK15112 111 DFPLRLNTDL-EPEQREKQIIETLRQVGL------LPDhaSYYPHM------LAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 501 VGLDPITERELMETVFEVLKGKTI--LWITHHLAGVE-AADKIVFLENGKTEMEGTHEELLAA--NERYRRL 567
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVLASplHELTKRL 249
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
358-560 |
6.45e-13 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 68.34 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 358 FTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQIAdavAVLNQKPHLFDTSI-----LNNIRL 432
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIG---YVPQRHEFAWDFPIsvahtVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 433 GN-------GEASDEDVRRAAKQVKLHDyIESLPDGyhtsvqetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLDP 505
Cdd:TIGR03771 78 GHigwlrrpCVADFAAVRDALRRVGLTE-LADRPVG----------ELSGGQRQRVLVARALATRPSVLLLDEPFTGLDM 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 506 ITERELMEtVFEVL--KGKTILWITHHLA-GVEAADKIVFLeNGKTEMEGTHEELLAA 560
Cdd:TIGR03771 147 PTQELLTE-LFIELagAGTAILMTTHDLAqAMATCDRVVLL-NGRVIADGTPQQLQDP 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
330-556 |
8.31e-13 |
|
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: 70.62 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVTfsydnssqVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGaLKPD---SGSVTLNGVE--TALL 404
Cdd:TIGR02633 2 LEMKGIVKTFGGVK--------ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPlkASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 405 KDQIADAVAVLNQKPHLF-DTSILNNIRLGN-----GEASDED--VRRAAK---QVKLHDYIESLPdgyhtsVQETGirf 473
Cdd:TIGR02633 73 RDTERAGIVIIHQELTLVpELSVAENIFLGNeitlpGGRMAYNamYLRAKNllrELQLDADNVTRP------VGDYG--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 474 sGGERQRIALARILLQDTPIIILDEPTVGLDPiTERELMETVFEVLKGKTI--LWITHHLAGVEA-ADKIVFLENGK--- 547
Cdd:TIGR02633 144 -GGQQQLVEIAKALNKQARLLILDEPSSSLTE-KETEILLDIIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQhva 221
|
250
....*....|
gi 2218266673 548 -TEMEGTHEE 556
Cdd:TIGR02633 222 tKDMSTMSED 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
338-529 |
8.96e-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: 70.73 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 338 SFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSvtlngvetALLKDQIAdaVAVLNQ 417
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQPGIK--VGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 418 KPHLFDT-SILNNIRLGNGEA--------------SDEDV---RRAAKQVKLHDYIES------------------LPDG 461
Cdd:TIGR03719 76 EPQLDPTkTVRENVEEGVAEIkdaldrfneisakyAEPDAdfdKLAAEQAELQEIIDAadawdldsqleiamdalrCPPW 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 462 yHTSVQEtgirFSGGERQRIALARILLQDTPIIILDEPTVGLDPIT----ERELMEtvfevLKGkTILWITH 529
Cdd:TIGR03719 156 -DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE-----YPG-TVVAVTH 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
286-535 |
1.17e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 286 PLTEAFLPLSDALGEVPGyQDSIKRMNRV-APQPEASQTESGAQTLDLQDVTLSFRDVTFSYDNSSQVL----------D 354
Cdd:PRK10261 263 PYTRALLAAVPQLGAMKG-LDYPRRFPLIsLEHPAKQEPPIEQDTVVDGEPILQVRNLVTRFPLRSGLLnrvtrevhavE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 355 NFSFTLRQGEKMALLGRSGSGKSTS----LALIEGalkpDSGSVTLNGVETALLKDQ------------IADAVAVLNQK 418
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTgralLRLVES----QGGEIIFNGQRIDTLSPGklqalrrdiqfiFQDPYASLDPR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 419 pHLFDTSILNNIR---LGNGEASDEDVRRAAKQVKLhdyiesLPDGYHTSVQEtgirFSGGERQRIALARILLQDTPIII 495
Cdd:PRK10261 418 -QTVGDSIMEPLRvhgLLPGKAAAARVAWLLERVGL------LPEHAWRYPHE----FSGGQRQRICIARALALNPKVII 486
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2218266673 496 LDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGVE 535
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVE 528
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
330-547 |
1.57e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.03 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVtfsydnssQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALL--KDQ 407
Cdd:PRK10762 5 LQLKGIDKAFPGV--------KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 408 IADAVAVLNQK----PHLfdtSILNNIRLGNgeasdEDVRR--AAKQVKLHDYIESL------PDGYHTSVQETGIrfsg 475
Cdd:PRK10762 77 QEAGIGIIHQElnliPQL---TIAENIFLGR-----EFVNRfgRIDWKKMYAEADKLlarlnlRFSSDKLVGELSI---- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 476 GERQRIALARILLQDTPIIILDEPTvglDPITERElMETVFEVLK-----GKTILWITHHLAGV-EAADKIVFLENGK 547
Cdd:PRK10762 145 GEQQMVEIAKVLSFESKVIIMDEPT---DALTDTE-TESLFRVIRelksqGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
330-560 |
1.82e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVtLSFRDVTFSYDNSSQVLD---NFSFTLRQGEKMALLGRSGSGKS-TSLALIEgaLKPDSGS------------ 393
Cdd:PRK10261 7 LDARDV-LAVENLNIAFMQEQQKIAavrNLSFSLQRGETLAIVGESGSGKSvTALALMR--LLEQAGGlvqcdkmllrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 394 ----VTLNGVETALLKDQIADAVAVLNQKPHlfdTS----------ILNNIRLGNGEASDEDVRRAAK---QVKLHDYIE 456
Cdd:PRK10261 84 srqvIELSEQSAAQMRHVRGADMAMIFQEPM---TSlnpvftvgeqIAESIRLHQGASREEAMVEAKRmldQVRIPEAQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 457 SLPDGYHtsvqetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVfEVLKGKT---ILWITHHLAG 533
Cdd:PRK10261 161 ILSRYPH--------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLI-KVLQKEMsmgVIFITHDMGV 231
|
250 260
....*....|....*....|....*...
gi 2218266673 534 V-EAADKIVFLENGKTEMEGTHEELLAA 560
Cdd:PRK10261 232 VaEIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
356-563 |
1.86e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 356 FSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETAL--LKDQI----------------------ADA 411
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIrsPRDAIragimlcpedrkaegiipvhsvADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKPHLFDTSILNNIRlgngEASDEDVRRAAKQVKlhdyieslpdgyhTSVQETGIRF-SGGERQRIALARILLQD 490
Cdd:PRK11288 352 INISARRHHLRAGCLINNRW----EAENADRFIRSLNIK-------------TPSREQLIMNlSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 491 TPIIILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEEllaANER 563
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ---ATER 486
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-560 |
2.27e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.38 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 344 FSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKD-------QIADAVAVLN 416
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifqidaiKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHLF-DTSILNNIRLGNGEASDEDVRRAAKQVKLHDYIESLPDGYHTSVQETGIRFSGGERQRIALARILLQDTPIII 495
Cdd:PRK14246 97 QQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 496 LDEPTVGLDPITERELMETVFEVLKGKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLAA 560
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
339-547 |
4.62e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.52 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 339 FRDVTFSYDNSS---QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVE-TALLKDQIADA--- 411
Cdd:PRK11153 4 LKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDlTALSEKELRKArrq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 412 VAVLNQKPHL------FDtsilnNIRLG---NGEASDEDVRRAA---KQVKLHDYIESLPDgyhtsvqetgiRFSGGERQ 479
Cdd:PRK11153 84 IGMIFQHFNLlssrtvFD-----NVALPlelAGTPKAEIKARVTellELVGLSDKADRYPA-----------QLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 480 RIALARILLQDTPIIILDEPTVGLDPITERelmeTVFEVLK------GKTILWITHHLAGV-EAADKIVFLENGK 547
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTR----SILELLKdinrelGLTIVLITHEMDVVkRICDRVAVIDAGR 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
344-514 |
4.67e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.28 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 344 FSYDNSSQVLDNFSF-----TLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQI-ADAVAVLNQ 417
Cdd:cd03237 1 YTYPTMKKTLGEFTLeveggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIkADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 418 kphlFDTSILNNirLGNGEASDEDVrraAKQVKLHDYIES-LPDgyhtsvqetgirFSGGERQRIALARILLQDTPIIIL 496
Cdd:cd03237 81 ----LLSSITKD--FYTHPYFKTEI---AKPLQIEQILDReVPE------------LSGGELQRVAIAACLSKDADIYLL 139
|
170
....*....|....*...
gi 2218266673 497 DEPTVGLDpiTERELMET 514
Cdd:cd03237 140 DEPSAYLD--VEQRLMAS 155
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
332-567 |
5.14e-12 |
|
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: 68.42 E-value: 5.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRDVTFSYDnSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNgvETALLK--DQIA 409
Cdd:TIGR03719 318 LGDKVIEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKLAyvDQSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 DAvavLNQKPHLFD--TSILNNIRLGNGEASDedvrRAakqvklhdYIESLpdGYHTSVQETGI-RFSGGERQRIALARI 486
Cdd:TIGR03719 395 DA---LDPNKTVWEeiSGGLDIIKLGKREIPS----RA--------YVGRF--NFKGSDQQKKVgQLSGGERNRVHLAKT 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 487 LLQDTPIIILDEPTVGLDPITERELmETVFEVLKGKTILwITH----------HLAGVEAADKIVFLENGKTEMEGTHEE 556
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRAL-EEALLNFAGCAVV-ISHdrwfldriatHILAFEGDSHVEWFEGNFSEYEEDKKR 535
|
250
....*....|....*..
gi 2218266673 557 LLAANE------RYRRL 567
Cdd:TIGR03719 536 RLGEDAdqphriKYKKL 552
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
337-505 |
9.37e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.87 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSyDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETAllKDQIADAVAVLN 416
Cdd:PRK13543 12 LAAHALAFS-RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--RGDRSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHL-FDTSILNNIRLGNGEASdedvRRAAKQVKLHDYIESLPDGYHTSVQEtgirFSGGERQRIALARILLQDTPIII 495
Cdd:PRK13543 89 HLPGLkADLSTLENLHFLCGLHG----RRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWL 160
|
170
....*....|
gi 2218266673 496 LDEPTVGLDP 505
Cdd:PRK13543 161 LDEPYANLDL 170
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
305-504 |
1.34e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.12 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 305 QDSIK---RMNRVAP------------QPEAsqtesgaqtldLQDVTLSFRDVTFSYDNSSqVLDNFSFTLRQGEKMALL 369
Cdd:PRK10636 277 QSRIKmleRMELIAPahvdnpfhfsfrAPES-----------LPNPLLKMEKVSAGYGDRI-ILDSIKLNLVPGSRIGLL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 370 GRSGSGKSTSLALIEGALKPDSGSVTL-NGVetallkdqiadavavlnqKPHLFDTSILNNIRLgnGEASDEDVRRAAKQ 448
Cdd:PRK10636 345 GRNGAGKSTLIKLLAGELAPVSGEIGLaKGI------------------KLGYFAQHQLEFLRA--DESPLQHLARLAPQ 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 449 V---KLHDYIESLpdGYH-TSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLD 504
Cdd:PRK10636 405 EleqKLRDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
352-558 |
1.49e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 352 VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPD--------SGSVTLNGVETALLK-DQIADAVAVLNQKPH-L 421
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 422 FDTSILNNIRLG-------NGEASDEDVRRAAKQVKLHdyieslpdGYHTSVQETGIRFSGGERQRIALARILLQ----- 489
Cdd:PRK13547 96 FAFSAREIVLLGrypharrAGALTHRDGEIAWQALALA--------GATALVGRDVTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 490 ----DTPIIILDEPTVGLDPITERELMETVFEVLKGKTI--LWITH--HLAGvEAADKIVFLENGKTEMEGTHEELL 558
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHdpNLAA-RHADRIAMLADGAIVAHGAPADVL 243
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
363-562 |
1.72e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 363 GEKMALLGRSGSGKSTSLALIEGALKPDS--GSVTLNGVEtalLKDQIADAVAVLNQK----PHLFDTSIL---NNIRLG 433
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK---PTKQILKRTGFVTQDdilyPHLTVRETLvfcSLLRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 434 NGEASDEDVRRAAKQVKLHdyieSLPDGYHTSVQETGIR-FSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELM 512
Cdd:PLN03211 171 KSLTKQEKILVAESVISEL----GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 513 ETVFEVL-KGKTILWITHHLAG--VEAADKIVFLENGKTEMEGTHEELLAANE 562
Cdd:PLN03211 247 LTLGSLAqKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMAYFE 299
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
319-557 |
1.75e-11 |
|
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: 67.35 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 319 EASQTESGAQTLDLqdvtLSFRDVTFSYD-NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLN 397
Cdd:TIGR01257 1924 ERQRIISGGNKTDI----LRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVA 1999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 398 G--VETALLK-----------DQIADavaVLNQKPHLFDTSILNNIrlgngeaSDEDVRRAA----KQVKLHDYIESLPD 460
Cdd:TIGR01257 2000 GksILTNISDvhqnmgycpqfDAIDD---LLTGREHLYLYARLRGV-------PAEEIEKVAnwsiQSLGLSLYADRLAG 2069
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 461 GYhtsvqetgirfSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGVEA-AD 538
Cdd:TIGR01257 2070 TY-----------SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSHSMEECEAlCT 2138
|
250
....*....|....*....
gi 2218266673 539 KIVFLENGKTEMEGTHEEL 557
Cdd:TIGR01257 2139 RLAIMVKGAFQCLGTIQHL 2157
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
461-543 |
2.73e-11 |
|
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: 62.34 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 461 GYHTSVQETGIrFSGGERQRIALARILLQDTP--IIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVEAA 537
Cdd:cd03238 77 GYLTLGQKLST-LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSA 155
|
....*.
gi 2218266673 538 DKIVFL 543
Cdd:cd03238 156 DWIIDF 161
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
352-551 |
2.94e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 352 VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQI-----ADAVAVLNQKPHLFDT-S 425
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrAKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 426 ILNNIRLG---NGEASDEDVRRAA---KQVKLHDYIESLPdgyhtsvqetgIRFSGGERQRIALARILLQDTPIIILDEP 499
Cdd:PRK10584 105 ALENVELPallRGESSRQSRNGAKallEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 500 TVGLDPITERELMETVFEVLK--GKTILWITHHLAGVEAADKIVFLENGKTEME 551
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
330-530 |
7.04e-11 |
|
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: 62.66 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFRDVtfsydnssQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEG--ALKPDSGSVTLNGVE-TALLKD 406
Cdd:TIGR01978 1 LKIKDLHVSVEDK--------EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDlLELEPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 407 QIADAVAVLN-QKP--------HLFDTSILNNIRLGNGEasdEDVRRAAKQVKLHDYIESL---PDGYHTSVQETgirFS 474
Cdd:TIGR01978 73 ERARAGLFLAfQYPeeipgvsnLEFLRSALNARRSARGE---EPLDLLDFEKLLKEKLALLdmdEEFLNRSVNEG---FS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 475 GGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHH 530
Cdd:TIGR01978 147 GGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLRePDRSFLIITHY 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
354-557 |
9.46e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.31 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 354 DNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQ-IADAVAVLN-QKPHLF-DTSILNNI 430
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqIARMGVVRTfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 431 ------RLGNG------------EASDEDVRRAA---KQVKLHDYIEslpdgyhtsvQETGiRFSGGERQRIALARILLQ 489
Cdd:PRK11300 102 lvaqhqQLKTGlfsgllktpafrRAESEALDRAAtwlERVGLLEHAN----------RQAG-NLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 490 DTPIIILDEPTVGLDPITERELMETVFEVLK--GKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEEL 557
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
353-560 |
9.60e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKS-TSLA---LIEGALKPDSGSVTLNGVETALLKD----QIADA-VAVLNQKPHlfd 423
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAimgLIDYPGRVMAEKLEFNGQDLQRISEkerrNLVGAeVAMIFQDPM--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 424 TS----------ILNNIRLGNGEASDEDVRRAA---KQVKLHDYIESLpDGY-HtsvqetgiRFSGGERQRIALARILLQ 489
Cdd:PRK11022 100 TSlnpcytvgfqIMEAIKVHQGGNKKTRRQRAIdllNQVGIPDPASRL-DVYpH--------QLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 490 DTPIIILDEPTVGLDPITERELMETVFEVLKGK--TILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLAA 560
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
334-547 |
1.25e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.51 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 334 DVTLsfRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSV-----TLNGVETAllkdqi 408
Cdd:PRK11000 3 SVTL--RNVTKAYGDV-VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekRMNDVPPA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 409 ADAVAVLNQK----PHLfdtSILNNIRLG------NGEASDEDVRRAAKQVKLHDYIESLPDGyhtsvqetgirFSGGER 478
Cdd:PRK11000 74 ERGVGMVFQSyalyPHL---SVAENMSFGlklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLDPITeRELMETvfEVLK-----GKTILWITHHlaGVEA---ADKIVFLENGK 547
Cdd:PRK11000 140 QRVAIGRTLVAEPSVFLLDEPLSNLDAAL-RVQMRI--EISRlhkrlGRTMIYVTHD--QVEAmtlADKIVVLDAGR 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
338-542 |
1.79e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 338 SFRDVTFSYDNSSQVLDNFSF-----TLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNgVETA-----LLKDQ 407
Cdd:PRK13409 335 SERETLVEYPDLTKKLGDFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISykpqyIKPDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 408 IADAVAVLNQKPHLFDTSILNNirlgngeasdEDVRRaakqVKLHDYIESlpdgyhtSVQEtgirFSGGERQRIALARIL 487
Cdd:PRK13409 414 DGTVEDLLRSITDDLGSSYYKS----------EIIKP----LQLERLLDK-------NVKD----LSGGELQRVAIAACL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 488 LQDTPIIILDEPTVGLDpiTE---------RELMETvfevlKGKTILWITHHLAGVE-AADK-IVF 542
Cdd:PRK13409 469 SRDADLYLLDEPSAHLD--VEqrlavakaiRRIAEE-----REATALVVDHDIYMIDyISDRlMVF 527
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
353-504 |
2.61e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG--VETALLKDQIADAVAVLNQKPH----LFDTSI 426
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQDGLANGIVYISEDRKrdglVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 427 LNNIRLgngEASDE------DVRRAAKQVKLHDYIESLpdGYHTSVQETGIRF-SGGERQRIALARILLQDTPIIILDEP 499
Cdd:PRK10762 348 KENMSL---TALRYfsraggSLKHADEQQAVSDFIRLF--NIKTPSMEQAIGLlSGGNQQKVAIARGLMTRPKVLILDEP 422
|
....*
gi 2218266673 500 TVGLD 504
Cdd:PRK10762 423 TRGVD 427
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
340-504 |
3.88e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYDNSSQVLDNFSFT-----LRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLN----------------G 398
Cdd:COG1245 338 EETLVEYPDLTKSYGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyispdydgT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 399 VEtALLKDQIADAvavlnqkphlFDTSILNNirlgngeasdEDVRRAAKQvKLHD-YIESLpdgyhtsvqetgirfSGGE 477
Cdd:COG1245 418 VE-EFLRSANTDD----------FGSSYYKT----------EIIKPLGLE-KLLDkNVKDL---------------SGGE 460
|
170 180
....*....|....*....|....*..
gi 2218266673 478 RQRIALARILLQDTPIIILDEPTVGLD 504
Cdd:COG1245 461 LQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
338-532 |
5.02e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 338 SFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLngvetallkdqiADAVAV--L 415
Cdd:PRK11819 8 TMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------------APGIKVgyL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 416 NQKPHLFDT-SILNNIRLGNGEA--------------SDEDVRR---AAKQVKLHDYIES------------------LP 459
Cdd:PRK11819 76 PQEPQLDPEkTVRENVEEGVAEVkaaldrfneiyaayAEPDADFdalAAEQGELQEIIDAadawdldsqleiamdalrCP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 460 DGyhtsvqETGI-RFSGGERQRIALARILLQDTPIIILDEPTVGLDPiterelmETVfevlkgktiLWITHHLA 532
Cdd:PRK11819 156 PW------DAKVtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-------ESV---------AWLEQFLH 207
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
341-559 |
5.33e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 341 DVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNgvETALL----KDQIADavavln 416
Cdd:PRK15064 324 NLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS--ENANIgyyaQDHAYD------ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 qkphlF--DTSILNNIRLGNGEASDEDVRRAA------------KQVKLhdyieslpdgyhtsvqetgirFSGGERQRIA 482
Cdd:PRK15064 395 -----FenDLTLFDWMSQWRQEGDDEQAVRGTlgrllfsqddikKSVKV---------------------LSGGEKGRML 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 483 LARILLQDTPIIILDEPTVGLDpiterelMETV------FEVLKGkTILWITHHLAGVEA-ADKIV-FLENGKTEMEGTH 554
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMD-------MESIeslnmaLEKYEG-TLIFVSHDREFVSSlATRIIeITPDGVVDFSGTY 520
|
....*
gi 2218266673 555 EELLA 559
Cdd:PRK15064 521 EEYLR 525
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
314-504 |
6.01e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.58 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 314 VAPQPEASQTESGAQTLDLQDvtLSFRDvtfsyDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGS 393
Cdd:COG3845 242 VLLRVEKAPAEPGEVVLEVEN--LSVRD-----DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 394 VTLNGVE-TALLKDQIADA-VAVLNQKPH---------LFDTSILNNIRLG--------NGEASDEDVRRAAKQ--VKlh 452
Cdd:COG3845 315 IRLDGEDiTGLSPRERRRLgVAYIPEDRLgrglvpdmsVAENLILGRYRRPpfsrggflDRKAIRAFAEELIEEfdVR-- 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 453 dyieslPDGYHTSVQetgiRFSGGERQRIALARILLQDTPIIILDEPTVGLD 504
Cdd:COG3845 393 ------TPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
353-547 |
7.59e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETAL--LKDQIADAVAVLNQKPHLF-DTSILNN 429
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFksSKEALENGISMVHQELNLVlQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 430 IRLG----NGEASDEDvrraakqvKLHDYIESLPDGYHTSV--QETGIRFSGGERQRIALARILLQDTPIIILDEPTVGL 503
Cdd:PRK10982 94 MWLGryptKGMFVDQD--------KMYRDTKAIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2218266673 504 dpiTEREL--METVFEVLK--GKTILWITHHLAGV-EAADKIVFLENGK 547
Cdd:PRK10982 166 ---TEKEVnhLFTIIRKLKerGCGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
333-560 |
8.04e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 8.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 333 QDVTLSFRDVTfSYDNSSqvLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLK--DQIAD 410
Cdd:PRK09700 262 HETVFEVRNVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 AVAVL--NQKPHLF--------DTSILNNIRLGN-----GEASDEDVRRAAKQVKlhdyiESLPDGYHtSVQETGIRFSG 475
Cdd:PRK09700 339 GMAYIteSRRDNGFfpnfsiaqNMAISRSLKDGGykgamGLFHEVDEQRTAENQR-----ELLALKCH-SVNQNITELSG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 476 GERQRIALARILLQDTPIIILDEPTVGLDPITERE---LMETVFEvlKGKTILWITHHLAGVEAA-DKIVFLENGK-TEM 550
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEiykVMRQLAD--DGKVILMVSSELPEIITVcDRIAVFCEGRlTQI 490
|
250
....*....|....*
gi 2218266673 551 -----EGTHEELLAA 560
Cdd:PRK09700 491 ltnrdDMSEEEIMAW 505
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
354-557 |
9.11e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 60.49 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 354 DNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDQ------------IADAVAVLNQKPHL 421
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewravrsdiqmiFQDPLASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 422 FDTsILNNIRLGNGEASDEDVRRAAKQVKLHdyIESLPDGYHTSVQEtgirFSGGERQRIALARILLQDTPIIILDEPTV 501
Cdd:PRK15079 118 GEI-IAEPLRTYHPKLSRQEVKDRVKAMMLK--VGLLPNLINRYPHE----FSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 502 GLDPITERELMETVFEVLK--GKTILWITHHLAGVE-AADKIVFLENGKtEME-GTHEEL 557
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVMYLGH-AVElGTYDEV 249
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
352-504 |
1.09e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.34 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 352 VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVEtallkdqiadAVAVLNQKPHLFDTSILNNIR 431
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNW----------QLAWVNQETPALPQPALEYVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 432 LGNGEASDEDVRRAAKQVK--------LH---DYIE---------SLPDGY---HTSVQETGIRFSGGERQRIALARILL 488
Cdd:PRK10636 86 DGDREYRQLEAQLHDANERndghaiatIHgklDAIDawtirsraaSLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALI 165
|
170
....*....|....*.
gi 2218266673 489 QDTPIIILDEPTVGLD 504
Cdd:PRK10636 166 CRSDLLLLDEPTNHLD 181
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
352-530 |
1.35e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 352 VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALK--PDSGSVTL---------NGVETALLKDQIADAVAVLNqkph 420
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVpdnqfgreaSLIDAIGRKGDFKDAVELLN---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 421 lfdtsilnnirlgngeasdedvrraakQVKLHDyieslPDGYHTSVQEtgirFSGGERQRIALARILLQDTPIIILDEPT 500
Cdd:COG2401 121 ---------------------------AVGLSD-----AVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|..
gi 2218266673 501 VGLDPITERELMETVFEVLK--GKTILWITHH 530
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARraGITLVVATHH 196
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
18-287 |
1.70e-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: 58.81 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 18 FVLVIFLGAVTIFSAAFLMFTSGFLISKAATRPENILLIYVPIVAvrtFGIARSVSRYVERLVGHHIILKIVSDMRVRLY 97
Cdd:pfam00664 5 ILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLL---LGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 98 NmlepgALMLRS-----RFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAILIALYLFVLVV 172
Cdd:pfam00664 82 K-----KILRQPmsffdTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 173 LFPVVSLLVTRARNAKLKSgRNVLYSRLTDAVMGVSDWMFSGRRHAFIDAYEKEEHDWFELERKKQRFTRWRDFAAQCLV 252
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKA-VAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIG 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 2218266673 253 AGLILLMLFWTAGQQADGEL----AKTMIAAFVLVVFPL 287
Cdd:pfam00664 236 YLSYALALWFGAYLVISGELsvgdLVAFLSLFAQLFGPL 274
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
336-557 |
1.98e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 59.47 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 336 TLSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG--VETALLKDQiadAVA 413
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEPADR---DIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 VLNQK----PHLfdtSILNN------IRlGNGEAS-DEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIA 482
Cdd:PRK11650 80 MVFQNyalyPHM---SVRENmayglkIR-GMPKAEiEERVAEAARILELEPLLDRKPR-----------ELSGGQRQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 483 LARILLQDTPIIILDEPTVGLDP---------ITE--RELmetvfevlkGKTILWITHHlaGVEA---ADKIVFLENGKT 548
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAklrvqmrleIQRlhRRL---------KTTSLYVTHD--QVEAmtlADRVVVMNGGVA 213
|
....*....
gi 2218266673 549 EMEGTHEEL 557
Cdd:PRK11650 214 EQIGTPVEV 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
359-532 |
2.34e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 359 TLRQGEKMALLGRSGSGKSTSLALIEGALKPDsgsvtLNGVETALLKDQIADAvavlnqkphlFDTSILNNI--RLGNGE 436
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEEEPSWDEVLKR----------FRGTELQNYfkKLYNGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 437 asdedVRRAAK-QvklhdYIESLPDGYHTSVQ-------ETGIR-------------------FSGGERQRIALARILLQ 489
Cdd:PRK13409 160 -----IKVVHKpQ-----YVDLIPKVFKGKVRellkkvdERGKLdevverlglenildrdiseLSGGELQRVAIAAALLR 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2218266673 490 DTPIIILDEPTVGLDpITERELM-ETVFEVLKGKTILWITHHLA 532
Cdd:PRK13409 230 DADFYFFDEPTSYLD-IRQRLNVaRLIRELAEGKYVLVVEHDLA 272
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
353-548 |
2.90e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDS--GSVTLNGVETAL--LKDQIADAVAVLNQK----PHLfdt 424
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFkdIRDSEALGIVIIHQElaliPYL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 425 SILNNIRLGNGEAS------DEDVRRAA---KQVKLHDyiesLPDgyhTSVQETGIrfsgGERQRIALARILLQDTPIII 495
Cdd:NF040905 94 SIAENIFLGNERAKrgvidwNETNRRARellAKVGLDE----SPD---TLVTDIGV----GKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 496 LDEPTVGLDPITERELMETVFEvLKGK--TILWITHHLAGVEA-ADKIVFLENGKT 548
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLE-LKAQgiTSIIISHKLNEIRRvADSITVLRDGRT 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
337-504 |
3.27e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.87 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVtlngVETALLKdqiadaVAVLN 416
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV----FRSAKVR------MAVFS 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QkpHLFD------TSILNNIRLGNGeasdedvrraAKQVKLHDYIESLPDGYHTSVQETgIRFSGGERQRIALARILLQD 490
Cdd:PLN03073 579 Q--HHVDgldlssNPLLYMMRCFPG----------VPEQKLRAHLGSFGVTGNLALQPM-YTLSGGQKSRVAFAKITFKK 645
|
170
....*....|....
gi 2218266673 491 TPIIILDEPTVGLD 504
Cdd:PLN03073 646 PHILLLDEPSNHLD 659
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
331-504 |
4.61e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 331 DLQDVTLSFRDVT-FSYDNSS-QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDS-GSVTLNG--VETALLK 405
Cdd:PRK13549 254 TIGEVILEVRNLTaWDPVNPHiKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGkpVKIRNPQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 406 DQIADAVAVL--NQKPH--LFDTSILNNI------RLGNGEASDEdvrrAAKQVKLHDYIESLPdgYHTSVQETGI-RFS 474
Cdd:PRK13549 334 QAIAQGIAMVpeDRKRDgiVPVMGVGKNItlaaldRFTGGSRIDD----AAELKTILESIQRLK--VKTASPELAIaRLS 407
|
170 180 190
....*....|....*....|....*....|
gi 2218266673 475 GGERQRIALARILLQDTPIIILDEPTVGLD 504
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
332-513 |
5.44e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRDVTFSYDNssQVL-DNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNgvETALLK--DQI 408
Cdd:PRK11819 320 LGDKVIEAENLSKSFGD--RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETVKLAyvDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 409 ADAvavLNQKPHLFDTsI---LNNIRLGNGEASDedvrRAakqvklhdYIESLpdGYHTSVQE--TGIrFSGGERQRIAL 483
Cdd:PRK11819 396 RDA---LDPNKTVWEE-IsggLDIIKVGNREIPS----RA--------YVGRF--NFKGGDQQkkVGV-LSGGERNRLHL 456
|
170 180 190
....*....|....*....|....*....|
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELME 513
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVETLRALEE 486
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
18-165 |
5.90e-09 |
|
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: 57.56 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 18 FVLVIFLGAVTIFSAAFLMFTSGFLISKAATRPENILLIYVPIVAVrTFGIARSVSRYVERLVGHHIILKIVSDMRVRLY 97
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLL-LLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 98 NMLEpgALMLR--SRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAILIAL 165
Cdd:cd07346 80 RHLQ--RLSLSffDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALL 147
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
351-560 |
6.03e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.99 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKpDSGSVT-----LNGVEtaLLK-------DQIADAVAVLNQK 418
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTadrfrWNGID--LLKlsprerrKIIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 419 PhlfdTSILN-NIRLGNG--EASDEDV------------RRAAKQ------VKLH-DYIESLPdgyHtsvqetgiRFSGG 476
Cdd:COG4170 98 P----SSCLDpSAKIGDQliEAIPSWTfkgkwwqrfkwrKKRAIEllhrvgIKDHkDIMNSYP---H--------ELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 477 ERQRIALARILLQDTPIIILDEPTVGLDPITERELME--TVFEVLKGKTILWITHHLAGV-EAADKIVFLENGKTEMEGT 553
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRllARLNQLQGTSILLISHDLESIsQWADTITVLYCGQTVESGP 242
|
....*..
gi 2218266673 554 HEELLAA 560
Cdd:COG4170 243 TEQILKS 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
335-547 |
6.43e-09 |
|
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: 56.12 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 335 VTLSFRDVTF---SYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPD---SGSVTLNGVETALLKdQI 408
Cdd:cd03233 2 STLSWRNISFttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA-EK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 409 ADAVAVLNQKPHLFDTSILnnirlgngeasdedVRR---AAKQVKLHDYIEslpdgyhtsvqetGIrfSGGERQRIALAR 485
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLT--------------VREtldFALRCKGNEFVR-------------GI--SGGERKRVSIAE 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 486 ILLQDTPIIILDEPTVGLDPITEREL---METVFEVLKGKTILWITHhlAGVEAA---DKIVFLENGK 547
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEIlkcIRTMADVLKTTTFVSLYQ--ASDEIYdlfDKVLVLYEGR 197
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
39-296 |
7.80e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 57.29 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 39 SGFLISKAATR---PENILLIYVPIVAVRTFGIARSVSRYVERLVGHHIILKIVSDMRVRLYNMLEPGALMLRSRFRTGD 115
Cdd:cd18561 15 QAWLLARALARifaGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 116 MLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAILIALYLFVLVVLFPVVSLLVTRArNAKLKSGRNV 195
Cdd:cd18561 95 LQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDT-GRRHWAAYGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 196 LYSRLTDAVMGVSDWMFSGRRHAFIDAYEKEEHDWFELERKKQRFTRWR----DFAAQCLVAGLILLMLFWTAGqqadGE 271
Cdd:cd18561 174 LSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSsgimGLATALGTALALGVGALRVLG----GQ 249
|
250 260
....*....|....*....|....*
gi 2218266673 272 LAktmIAAFVLVVFPLTEAFLPLSD 296
Cdd:cd18561 250 LT---LSSLLLILFLSREFFRPLRD 271
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
342-538 |
1.46e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 342 VTFSYDNSSQ-VLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGveTALLKDQIA--DAVAVLNQK 418
Cdd:PRK13540 5 IELDFDYHDQpLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER--QSIKKDLCTyqKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 419 ----PHL-FDTSILNNIRLGNGEASDEDVRRAAKQVKLHDYieslPDGYhtsvqetgirFSGGERQRIALARILLQDTPI 493
Cdd:PRK13540 83 sginPYLtLRENCLYDIHFSPGAVGITELCRLFSLEHLIDY----PCGL----------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2218266673 494 IILDEPTVGLDPITERELMETVFE-VLKGKTILWITHHLAGVEAAD 538
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
472-550 |
1.57e-08 |
|
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: 54.92 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 472 RFSGGERQ------RIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKT---ILWITHHLAGVEAADKIVF 542
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKnfqLIVITHDEELVDAADHIYR 194
|
....*...
gi 2218266673 543 LENGKTEM 550
Cdd:cd03240 195 VEKDGRQK 202
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
474-541 |
4.33e-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: 52.75 E-value: 4.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 474 SGGERQRIALARIL----LQDTPIIILDEPTVGLDPITERELMETVFE-VLKGKTILWITHHLAGVEAADKIV 541
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
353-547 |
4.94e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNG-VETALLK------------DQIADAVAVLNQK- 418
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdLIVARLQqdpprnvegtvyDFVAEGIEEQAEYl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 419 ------PHLFDTsilnnirlgngEASDEDVRRAAK-QVKL------------HDYIESLPDGYHTSVQEtgirFSGGERQ 479
Cdd:PRK11147 99 kryhdiSHLVET-----------DPSEKNLNELAKlQEQLdhhnlwqlenriNEVLAQLGLDPDAALSS----LSGGWLR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 480 RIALARILLQDTPIIILDEPTVGLDpITERELMETVFEVLKGkTILWITHHLAGVEA-ADKIVFLENGK 547
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLD-IETIEWLEGFLKTFQG-SIIFISHDRSFIRNmATRIVDLDRGK 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
361-532 |
9.05e-08 |
|
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: 53.52 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 361 RQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLN-----------GVE-----TALLKDQIADAVAV--LNQKPHLF 422
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPpdwdeildefrGSElqnyfTKLLEGDVKVIVKPqyVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 423 DTSILNNIrlgngEASDEdvrraakQVKLHDYIESLPdgyHTSVQETGI-RFSGGERQRIALARILLQDTPIIILDEPTV 501
Cdd:cd03236 104 KGKVGELL-----KKKDE-------RGKLDELVDQLE---LRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|...
gi 2218266673 502 GLDpITER-ELMETVFEVLK-GKTILWITHHLA 532
Cdd:cd03236 169 YLD-IKQRlNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
472-557 |
9.24e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 472 RFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLK-GKTILWITHHLAGVEA-ADKIVFLENGKTE 549
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHELTVIDRGRVI 223
|
....*...
gi 2218266673 550 MEGTHEEL 557
Cdd:NF000106 224 ADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
340-530 |
1.02e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 340 RDVTFSYdNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGalkpD-----SGSVTLNGV-----ETALlkdQIA 409
Cdd:PRK10938 264 NNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpqgySNDLTLFGRrrgsgETIW---DIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 410 DAVAVLNQKPHL---FDTSILNNI------RLGNGEASDEDVRRAAKQvklhdYIESLpdGYHTSVQETGIR-FSGGErQ 479
Cdd:PRK10938 336 KHIGYVSSSLHLdyrVSTSVRNVIlsgffdSIGIYQAVSDRQQKLAQQ-----WLDIL--GIDKRTADAPFHsLSWGQ-Q 407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 480 RIAL-ARILLQDTPIIILDEPTVGLDPITeRELMETVFEVL--KGKT-ILWITHH 530
Cdd:PRK10938 408 RLALiVRALVKHPTLLILDEPLQGLDPLN-RQLVRRFVDVLisEGETqLLFVSHH 461
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
344-547 |
1.74e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 344 FSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALI----EGALKPDSGSVTLNGVETALLKDQIADAVAVLNQK- 418
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETd 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 419 ---PHL-----FDTSILNNIRLGNGEASDEDVRrAAKQVKLHDYIESLPDGYHTSVQETGIR-FSGGERQRIALARILLQ 489
Cdd:TIGR00956 148 vhfPHLtvgetLDFAARCKTPQNRPDGVSREEY-AKHIADVYMATYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 490 DTPIIILDEPTVGLDPiterelmETVFEVLKG-KTILWITHHLAGV----------EAADKIVFLENGK 547
Cdd:TIGR00956 227 GAKIQCWDNATRGLDS-------ATALEFIRAlKTSANILDTTPLVaiyqcsqdayELFDKVIVLYEGY 288
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
474-541 |
2.95e-07 |
|
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: 51.85 E-value: 2.95e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 474 SGGERQRIALARILLQDTP---IIILDEPTVGLDPITERELMEtVFEVL--KGKTILWITHHLAGVEAADKIV 541
Cdd:cd03271 171 SGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLE-VLQRLvdKGNTVVVIEHNLDVIKCADWII 242
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-532 |
2.99e-07 |
|
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: 53.25 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 359 TLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVtlngvETALLKDQIADAvavlnqkphlFDTSILNNI--RLGNGE 436
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-----DEEPSWDEVLKR----------FRGTELQDYfkKLANGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 437 asdedVRRAAK-QvklhdYIESLPDGYH-------TSVQETGI-------------------RFSGGERQRIALARILLQ 489
Cdd:COG1245 160 -----IKVAHKpQ-----YVDLIPKVFKgtvrellEKVDERGKldelaeklglenildrdisELSGGELQRVAIAAALLR 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 490 DTPIIILDEPTVGLDpITER--------ELMEtvfevlKGKTILWITHHLA 532
Cdd:COG1245 230 DADFYFFDEPSSYLD-IYQRlnvarlirELAE------EGKYVLVVEHDLA 273
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
348-530 |
3.19e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 348 NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEG--ALKPDSGSVTLNGvetallkDQIADAVAvlNQKPHLfdts 425
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKG-------ESILDLEP--EERAHL---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 426 ilnNIRLG-------NGeASDEDVRRAA---KQVKLH----DYIESL-------------PDGYHTSVQETgirFSGGER 478
Cdd:CHL00131 85 ---GIFLAfqypieiPG-VSNADFLRLAynsKRKFQGlpelDPLEFLeiineklklvgmdPSFLSRNVNEG---FSGGEK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHH 530
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHY 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
474-557 |
3.46e-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: 53.48 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 474 SGGERQRIALARILLQ-DT--PIIILDEPTVGL--DPIteRELMETVFE-VLKGKTILWITHHLAGVEAADKIVFL---- 543
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKrSTgrTLYILDEPTTGLhfDDI--KKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIIDLgpeg 908
|
90
....*....|....*.
gi 2218266673 544 --ENGKTEMEGTHEEL 557
Cdd:TIGR00630 909 gdGGGTVVASGTPEEV 924
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
387-573 |
4.39e-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: 53.09 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 387 LKPDSGSVTLNGVEtallkdqIADAVAVLNQKPHLFdtsiLNNIRLGNGEAsdedvrRAAKQVkLHDYIESLpdgyhTSV 466
Cdd:TIGR00630 416 LKPEALAVTVGGKS-------IADVSELSIREAHEF----FNQLTLTPEEK------KIAEEV-LKEIRERL-----GFL 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 467 QETGIRF----------SGGERQRIALA-RILLQDTPII-ILDEPTVGLDPITERELMETVfEVLK--GKTILWITHHLA 532
Cdd:TIGR00630 473 IDVGLDYlslsraagtlSGGEAQRIRLAtQIGSGLTGVLyVLDEPSIGLHQRDNRRLINTL-KRLRdlGNTLIVVEHDED 551
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 533 GVEAADKIVFL------ENGKTEMEGTHEELLAANERYRRLY-----HLDVP 573
Cdd:TIGR00630 552 TIRAADYVIDIgpgageHGGEVVASGTPEEILANPDSLTGQYlsgrkKIEVP 603
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
337-546 |
1.07e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.16 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYD---NSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIegALKPDSGSVTlngvetallkdqiadava 413
Cdd:cd03232 4 LTWKNLNYTVPvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL--AGRKTAGVIT------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 414 vlnqkphlfdtsilNNIRLgNGEASDEDVRRA---AKQVKLHdyIESLpdgyhtSVQETgIRFSG-------GERQRIAL 483
Cdd:cd03232 64 --------------GEILI-NGRPLDKNFQRStgyVEQQDVH--SPNL------TVREA-LRFSAllrglsvEQRKRLTI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELMETVFEV-LKGKTILWITHHLAGV--EAADKIVFLENG 546
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
354-506 |
1.17e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 354 DNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGvetallkdQIADA--------VAVLNQKPHLF-DT 424
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG--------QPVDAgdiatrrrVGYMSQAFSLYgEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 425 SILNNI----RLGN--GEASDEDVRRAAKQVKLHDYIESLPDgyhtsvqetgiRFSGGERQRIALARILLQDTPIIILDE 498
Cdd:NF033858 355 TVRQNLelhaRLFHlpAAEIAARVAEMLERFDLADVADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDE 423
|
....*...
gi 2218266673 499 PTVGLDPI 506
Cdd:NF033858 424 PTSGVDPV 431
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
474-563 |
1.25e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.57 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 474 SGGERQRIALARILLQ-DTP--IIILDEPTVGL--DPIteRELMEtVFEVL--KGKTILWITHHLAGVEAAD-------- 538
Cdd:COG0178 828 SGGEAQRVKLASELSKrSTGktLYILDEPTTGLhfHDI--RKLLE-VLHRLvdKGNTVVVIEHNLDVIKTADwiidlgpe 904
|
90 100 110
....*....|....*....|....*....|.
gi 2218266673 539 ------KIVFlengktemEGTHEElLAANER 563
Cdd:COG0178 905 ggdgggEIVA--------EGTPEE-VAKVKA 926
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
353-564 |
1.62e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.81 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLKDqiadavAVLNQKphlfdTSILNNIR- 431
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAIS------AGLSGQ-----LTGIENIEf 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 432 --LGNGEASDEDVRRAAKQVKLHDyiesLPDGYHTSVQetgiRFSGGERQRIALARILLQDTPIIILDEP-TVGLDPITE 508
Cdd:PRK13546 109 kmLCMGFKRKEIKAMTPKIIEFSE----LGEFIYQPVK----KYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 509 RELmETVFEVL-KGKTILWITHHLAGV-EAADKIVFLENGKTEMEGTHEELLAANERY 564
Cdd:PRK13546 181 KCL-DKIYEFKeQNKTIFFVSHNLGQVrQFCTKIAWIEGGKLKDYGELDDVLPKYEAF 237
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
474-541 |
1.68e-06 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 1.68e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2218266673 474 SGGERQRIALARILLQD-TPII-ILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVEAADKIV 541
Cdd:cd03270 139 SGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVI 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
334-564 |
2.65e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 334 DVTLSFRDVTFSYDNSSQvldNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVET------------ 401
Cdd:PRK10982 248 EVILEVRNLTSLRQPSIR---DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhnaneainhg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 402 -ALLKDQ-----------IADAVAVLNQKPHLFDTSILNNIRLgngeASDEDVRRAAKQVKlhdyieslpdgyhTSVQET 469
Cdd:PRK10982 325 fALVTEErrstgiyayldIGFNSLISNIRNYKNKVGLLDNSRM----KSDTQWVIDSMRVK-------------TPGHRT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 470 GI-RFSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVL-KGKTILWITH---HLAGVeaADKIVFLE 544
Cdd:PRK10982 388 QIgSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSempELLGI--TDRILVMS 465
|
250 260
....*....|....*....|....*
gi 2218266673 545 NGKT-----EMEGTHEELLAANERY 564
Cdd:PRK10982 466 NGLVagivdTKTTTQNEILRLASLH 490
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
362-530 |
3.50e-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: 46.98 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 362 QGEKMALLGRSGSGKSTSLALIEGALKPDSGSVtlngvetallkdqiadavavlnqkphlfdtsilnnIRLgNGEASDED 441
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------------------------IYI-DGEDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 442 VRRAAKQVKLHDYIESLpdgyhtsvqetgirfSGGERQRIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVL-- 519
Cdd:smart00382 45 VLDQLLLIIVGGKKASG---------------SGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170
....*....|....*.
gi 2218266673 520 -----KGKTILWITHH 530
Cdd:smart00382 110 llkseKNLTVILTTND 125
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
292-529 |
4.33e-06 |
|
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: 49.75 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 292 LPLSDALG----------EVPGYQDSIKRMNRV-----------APQPEASQTESGAQTLDL---------QDVTLSFRD 341
Cdd:TIGR00954 377 LKAADALGrlmlagrdmtRLAGFTARVDTLLQVlddvksgnfkrPRVEEIESGREGGRNSNLvpgrgiveyQDNGIKFEN 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 342 VTFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKStSLALIEGALKPdsgsvTLNGVETALLKDQIAdavaVLNQKPHL 421
Cdd:TIGR00954 457 IPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKS-SLFRILGELWP-----VYGGRLTKPAKGKLF----YVPQRPYM 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 422 ----------FDTSILNNIRLGngeASDEDVRRAAKQVKLHDYIESlpDGYHTSVQETGIRFSGGERQRIALARILLQDT 491
Cdd:TIGR00954 527 tlgtlrdqiiYPDSSEDMKRRG---LSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKP 601
|
250 260 270
....*....|....*....|....*....|....*...
gi 2218266673 492 PIIILDEPTVGLDPITERELMETVFEVlkGKTILWITH 529
Cdd:TIGR00954 602 QFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSH 637
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
55-165 |
4.72e-06 |
|
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: 48.66 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 55 LIYVPIVAVRtfGIARSVSRYVERLVGHHIilkiVSDMRVRLYNMLEpgALMLR--SRFRTGDMLGILSEDIEHLQDAFL 132
Cdd:cd18564 58 AALVGIALLR--GLASYAGTYLTALVGQRV----VLDLRRDLFAHLQ--RLSLSfhDRRRTGDLLSRLTGDVGAIQDLLV 129
|
90 100 110
....*....|....*....|....*....|...
gi 2218266673 133 KTIFPAISALLLYAVSVIALGFFSWPFAiLIAL 165
Cdd:cd18564 130 SGVLPLLTNLLTLVGMLGVMFWLDWQLA-LIAL 161
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
330-560 |
5.17e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 330 LDLQDVTLSFrdvtFSYDNSSQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKpDSGSVT-----LNGVETALL 404
Cdd:PRK15093 4 LDIRNLTIEF----KTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTadrmrFDDIDLLRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 405 KDQ-----IADAVAVLNQKPH-LFDTS------ILNNI-----------RLGNGEasdedvRRAAK-----QVKLH-DYI 455
Cdd:PRK15093 79 SPRerrklVGHNVSMIFQEPQsCLDPServgrqLMQNIpgwtykgrwwqRFGWRK------RRAIEllhrvGIKDHkDAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 456 ESLPdgyhtsvqetgIRFSGGERQRIALArILLQDTP-IIILDEPTVGLDPITERElmetVFEVL------KGKTILWIT 528
Cdd:PRK15093 153 RSFP-----------YELTEGECQKVMIA-IALANQPrLLIADEPTNAMEPTTQAQ----IFRLLtrlnqnNNTTILLIS 216
|
250 260 270
....*....|....*....|....*....|...
gi 2218266673 529 HHLAGVEA-ADKIVFLENGKTEMEGTHEELLAA 560
Cdd:PRK15093 217 HDLQMLSQwADKINVLYCGQTVETAPSKELVTT 249
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
474-575 |
5.54e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 474 SGGERQRIALARILLQDTPII--ILDEPTVGLDPITERELMEtVFEVLK--GKTILWITHHLAGVEAADKIVFLE----- 544
Cdd:PRK00635 478 SGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLIN-VIKKLRdqGNTVLLVEHDEQMISLADRIIDIGpgagi 556
|
90 100 110
....*....|....*....|....*....|....*..
gi 2218266673 545 -NGKTEMEGTHEELLAANE----RY-RRLYHLDVPVK 575
Cdd:PRK00635 557 fGGEVLFNGSPREFLAKSDsltaKYlRQELTIPIPEK 593
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
351-504 |
6.06e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 351 QVLDNFSFTLRQGEKMALLGRSGSGKsTSLAL----------IegalkpdSGSVTLNG--VETALLKDQIADAVA-VLNQ 417
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGR-TELAMsvfgrsygrnI-------SGTVFKDGkeVDVSTVSDAIDAGLAyVTED 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 418 KPHL---FDTSILNNIRLGN-GEASDEDVRRAAKQVKL-HDYIESLPDGYHTSVQETGiRFSGGERQRIALARILLQDTP 492
Cdd:NF040905 346 RKGYglnLIDDIKRNITLANlGKVSRRGVIDENEEIKVaEEYRKKMNIKTPSVFQKVG-NLSGGNQQKVVLSKWLFTDPD 424
|
170
....*....|..
gi 2218266673 493 IIILDEPTVGLD 504
Cdd:NF040905 425 VLILDEPTRGID 436
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
474-563 |
8.39e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.92 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 474 SGGERQRIALARILL-QDT--PIIILDEPTVGL--DPIteRELMetvfEVL-----KGKTILWITHHLAGVEAADKIVFL 543
Cdd:PRK00349 832 SGGEAQRVKLAKELSkRSTgkTLYILDEPTTGLhfEDI--RKLL----EVLhrlvdKGNTVVVIEHNLDVIKTADWIIDL 905
|
90 100
....*....|....*....|....*.
gi 2218266673 544 ------ENGKTEMEGTHEElLAANER 563
Cdd:PRK00349 906 gpeggdGGGEIVATGTPEE-VAKVEA 930
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
355-529 |
1.12e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 355 NFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTL-NGVETALLK-DQIA-DAVAVLnqkphlfDTSILNNIR 431
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRqDQFAfEEFTVL-------DTVIMGHTE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 432 L-----------GNGEASDEDVRRAAK-QVKLHDYieslpDGYHTSVQ------ETGI----------RFSGGERQRIAL 483
Cdd:PRK15064 92 LwevkqerdriyALPEMSEEDGMKVADlEVKFAEM-----DGYTAEARagelllGVGIpeeqhyglmsEVAPGWKLRVLL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2218266673 484 ARILLQDTPIIILDEPTVGLDPITERELMETVFEvlKGKTILWITH 529
Cdd:PRK15064 167 AQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
353-569 |
1.15e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGveTALLkdqIADAvAVLNQKPHLFDTSILNNIRL 432
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--SAAL---IAIS-SGLNGQLTGIENIELKGLMM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 433 GngeASDEDVRRAAKQVklhdyIESLPDG--YHTSVQEtgirFSGGERQRIALARILLQDTPIIILDEP-TVGLDPITER 509
Cdd:PRK13545 114 G---LTKEKIKEIIPEI-----IEFADIGkfIYQPVKT----YSSGMKSRLGFAISVHINPDILVIDEAlSVGDQTFTKK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2218266673 510 EL--METVFEvlKGKTILWITHHLAGVEA-ADKIVFLENGKTEMEGTHEELLAANERYRRLYH 569
Cdd:PRK13545 182 CLdkMNEFKE--QGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYN 242
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
332-559 |
1.63e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 332 LQDVTLSFRDVtfsydnssQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVT-LNGvetallkdQIAD 410
Cdd:NF033858 4 LEGVSHRYGKT--------VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGG--------DMAD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 411 AV---AVL------------NQKPHLfdtSILNNI----RLgNGEASDEDVRRaakqvklhdyIESLpdgyhtsVQETGI 471
Cdd:NF033858 68 ARhrrAVCpriaympqglgkNLYPTL---SVFENLdffgRL-FGQDAAERRRR----------IDEL-------LRATGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 472 -RF--------SGGERQRIALARILLQDTPIIILDEPTVGLDPITER---ELMETVFEVLKGKTILWITHHLAgvEAA-- 537
Cdd:NF033858 127 aPFadrpagklSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRqfwELIDRIRAERPGMSVLVATAYME--EAErf 204
|
250 260
....*....|....*....|..
gi 2218266673 538 DKIVFLENGKTEMEGTHEELLA 559
Cdd:NF033858 205 DWLVAMDAGRVLATGTPAELLA 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
355-504 |
3.50e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 355 NFSFTLRQGEKMALLGRSGSGKsTSLA-LIEGALKPDSGSVTLNGVETALL--KDQIADAVAVL---NQKPHLF-DTSIL 427
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGR-TELAeTLYGLRPARGGRIMLNGKEINALstAQRLARGLVYLpedRQSSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 428 NNI-RLGNGEASDEdVRRAAKQVKLhdyieslpDGYHTSVqetGIRF----------SGGERQRIALARILLQDTPIIIL 496
Cdd:PRK15439 360 WNVcALTHNRRGFW-IKPARENAVL--------ERYRRAL---NIKFnhaeqaartlSGGNQQKVLIAKCLEASPQLLIV 427
|
....*...
gi 2218266673 497 DEPTVGLD 504
Cdd:PRK15439 428 DEPTRGVD 435
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
17-281 |
3.73e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 45.94 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 17 LFVLVIFLGAVTIFSAAFLMftsGFLISKAATRPeNILLIYVPIVAVRTFGIARSVSRYVERLVGHHIILKIVSDMRVRL 96
Cdd:cd18550 3 LVLLLILLSALLGLLPPLLL---REIIDDALPQG-DLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 97 YNMLEPGALMLRSRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSW----------PFAILIALY 166
Cdd:cd18550 79 YAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWrlallslvllPLFVLPTRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 167 LFvlvvlfpvvsllvtrARNAKLKSGRNVLYSRLTDAV---MGVSDWMFS---GRRHAFIDAYEKEEHDWFELERKKQRF 240
Cdd:cd18550 159 VG---------------RRRRKLTREQQEKLAELNSIMqetLSVSGALLVklfGREDDEAARFARRSRELRDLGVRQALA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2218266673 241 TRWRdFAAQCLVAGLILLMLFWTAGQQA-DGELAKTMIAAFV 281
Cdd:cd18550 224 GRWF-FAALGLFTAIGPALVYWVGGLLViGGGLTIGTLVAFT 264
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
357-504 |
3.84e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 357 SFTLRQGEKMALLGRSGSGKST-----SLALIEGALKpdsgSVTLNGVETALLKDQIADAVAVLN--------------- 416
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTflrymAMHAIDGIPK----NCQILHVEQEVVGDDTTALQCVLNtdiertqlleeeaql 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 --QKPHLFDTSILNNIRLGNGEASDEDV--RRAAKQVKLHDYIeslpDGYHTSVQETGI----------------RFSGG 476
Cdd:PLN03073 273 vaQQRELEFETETGKGKGANKDGVDKDAvsQRLEEIYKRLELI----DAYTAEARAASIlaglsftpemqvkatkTFSGG 348
|
170 180
....*....|....*....|....*...
gi 2218266673 477 ERQRIALARILLQDTPIIILDEPTVGLD 504
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-165 |
4.29e-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: 45.49 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 18 FVLVIFLGAVTIFSAAFLMFTSGFLISKAATRPENILLIYVPIVAVRTFgIARSVSRYVERLVGHHIILKIVSDMRVRLY 97
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLF-LLRGLASYLQTYLMAYVGQRVVRDLRNDLF 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2218266673 98 NMLepgaLMLRSRF----RTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAiLIAL 165
Cdd:cd18552 80 DKL----LRLPLSFfdrnSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLT-LIAL 146
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
434-544 |
1.33e-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: 42.94 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 434 NGEASDEDVRRAAKQVKLHDYIESLpDGYHTSVQETGIRFSGGERQRIALARILLQDTPIIILDEPTVGLDpITERELME 513
Cdd:cd03222 34 NGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD-IEQRLNAA 111
|
90 100 110
....*....|....*....|....*....|....*
gi 2218266673 514 TVFEVL---KGKTILWITHHLAGVE-AADKIVFLE 544
Cdd:cd03222 112 RAIRRLseeGKKTALVVEHDLAVLDyLSDRIHVFE 146
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
474-543 |
1.47e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 1.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 474 SGGERQRIALARILLQDTP---IIILDEPTVGLDPITERELMETVFEVL-KGKTILWITHHLAGVEAADKIVFL 543
Cdd:PRK00635 811 SGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
337-504 |
2.03e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNSsQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGA--LKPDSGSVTLNGVETALL--KDQIADAV 412
Cdd:PRK09580 2 LSIKDLHVSVEDK-AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELspEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 413 AVLNQKP--------HLFDTSILNNIRLGNGEAsdedvrrAAKQVKLHDYIE------SLPDGYHTSVQETGirFSGGER 478
Cdd:PRK09580 81 FMAFQYPveipgvsnQFFLQTALNAVRSYRGQE-------PLDRFDFQDLMEekiallKMPEDLLTRSVNVG--FSGGEK 151
|
170 180
....*....|....*....|....*.
gi 2218266673 479 QRIALARILLQDTPIIILDEPTVGLD 504
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLD 177
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
17-165 |
2.51e-04 |
|
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: 43.17 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 17 LFVLVIFLGAVTIFSAAFLmftsGFLISKAATRPENILLIYVPIVAVRTFGIARSVSRYVERLVGHHIILKIVSDMRVRL 96
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLL----ARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 97 YNMLEPGALMLRSRFRTGDMLGILSEDIEHLqDAFLKTIFPA-ISALLLYAVSVIALGFFSWPFAILIAL 165
Cdd:cd18584 77 LARLLALGPALLRRQSSGELATLLTEGVDAL-DGYFARYLPQlVLAAIVPLLILVAVFPLDWVSALILLV 145
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
18-165 |
2.54e-04 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 43.19 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 18 FVLVIFLGAV-TIFSAAFLMFTSGfLISKAATRPENILLIYVPIVAVRTFGIARSVSRYVERLVGHhiilKIVSDMRVRL 96
Cdd:cd18551 1 LILALLLSLLgTAASLAQPLLVKN-LIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGE----RVVLDLRRRL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2218266673 97 YNMLepgaLMLR----SRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWP-FAILIAL 165
Cdd:cd18551 76 WRRL----LRLPvsffDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVlTLVTLAV 145
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
18-165 |
3.40e-04 |
|
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: 42.80 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 18 FVLVIFLgavTIFSAAFLMFT---SGFLISKA--ATRPENILLIYVPIVAVrtfGIARSVSRYVERLVGHHIILKIVSDM 92
Cdd:cd18542 1 YLLAILA---LLLATALNLLIpllIRRIIDSVigGGLRELLWLLALLILGV---ALLRGVFRYLQGYLAEKASQKVAYDL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 93 RVRLYNMLEpgALMLR--SRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAiLIAL 165
Cdd:cd18542 75 RNDLYDHLQ--RLSFSfhDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLT-LISL 146
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
353-572 |
3.64e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.07 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 353 LDNFSFTLRQGeKMALLGRSGSGKSTSLALIEGALKPDSG---------------------SVTLNGVETALLK------ 405
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeieiELTFGSLLSRLLRlllkee 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 406 --DQIADAVAVLNQKPHLFDTSILNNIR-LGNGEASDEDVRRAAKQVKLHDYIESL----PDGYHTSVQETGIrfsgGER 478
Cdd:COG3593 93 dkEELEEALEELNEELKEALKALNELLSeYLKELLDGLDLELELSLDELEDLLKSLslriEDGKELPLDRLGS----GFQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 479 QRI--ALARILLQ-----DTPIIILDEPTVGLDPITERELMETVFEVLKGKTILWI-TH--HLAGVEAADKIVFLENGKT 548
Cdd:COG3593 169 RLIllALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIItTHspHLLSEVPLENIRRLRRDSG 248
|
250 260
....*....|....*....|....
gi 2218266673 549 EMEGTHEELLAANERYRRLYHLDV 572
Cdd:COG3593 249 GTTSTKLIDLDDEDLRKLLRYLGV 272
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
467-551 |
4.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 467 QETGIRF-SGGERQ------RIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKG--KTILwITHHLAGVEAA 537
Cdd:PRK03918 782 KERPLTFlSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKipQVII-VSHDEELKDAA 860
|
90
....*....|....*.
gi 2218266673 538 DKIVF--LENGKTEME 551
Cdd:PRK03918 861 DYVIRvsLEGGVSKVE 876
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-165 |
9.33e-04 |
|
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: 41.32 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 21 VIFLGAVTIFSAAFLMFTsGFLISKAATRPENILLIYVPIVAVRTFgIARSVSRYVERLVGHHIILKIVSDMRVRLYNML 100
Cdd:cd18576 2 LILLLLSSAIGLVFPLLA-GQLIDAALGGGDTASLNQIALLLLGLF-LLQAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2218266673 101 epgaLMLRSRF----RTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAILIAL 165
Cdd:cd18576 80 ----QRLPLSFfherRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLA 144
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
87-301 |
1.08e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 41.39 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 87 KIVSDMRVRLYnmlepGALMLRS-----RFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSW---- 157
Cdd:cd18557 66 RIVARLRRDLF-----SSLLRQEiaffdKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWkltl 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 158 -------PFAILIALYlfvlvvlfpvvsllvtrarNAKLKsgrnVLYSRLTDAV---MGVSDWMFSGRR--HAF------ 219
Cdd:cd18557 141 vlllvipLLLIASKIY-------------------GRYIR----KLSKEVQDALakaGQVAEESLSNIRtvRSFsaeeke 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 220 IDAYEKEEHDWFELERKKqrfTRWRDF---AAQCLVAGLILLMLFWTAGQQADGELAKTMIAAFVLVVFPLTEAFLPLSD 296
Cdd:cd18557 198 IRRYSEALDRSYRLARKK---ALANALfqgITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSS 274
|
....*
gi 2218266673 297 ALGEV 301
Cdd:cd18557 275 LLADI 279
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
337-529 |
3.19e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 337 LSFRDVTFSYDNssQVLDNFSFTLRQGEKMALLGRSGSGKSTSLALIEGALKPDSGSVTLNGVETALLkdqiadavavln 416
Cdd:PRK13541 2 LSLHQLQFNIEQ--KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 417 QKPHL----------FDTSILNNIRL-GNGEASDEDVRRAAKQVKLHDYIEslpdgyhtsvqETGIRFSGGERQRIALAR 485
Cdd:PRK13541 68 AKPYCtyighnlglkLEMTVFENLKFwSEIYNSAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIAR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2218266673 486 ILLQDTPIIILDEPTVGLDPiTERELMET--VFEVLKGKTILWITH 529
Cdd:PRK13541 137 LIACQSDLWLLDEVETNLSK-ENRDLLNNliVMKANSGGIVLLSSH 181
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
54-165 |
3.28e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 39.77 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 54 LLIYVPIVAVrtFGIARSVSRYVERLVGHHIILKIVSDMRVRLYNMLE--PGAlmLRSRFRTGDMLGILSEDIEHLQdAF 131
Cdd:cd18543 38 LWPLVLLLLA--LGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQrlDGA--FHDRWQSGQLLSRATSDLSLVQ-RF 112
|
90 100 110
....*....|....*....|....*....|....
gi 2218266673 132 LKTIFPAISALLLYAVSVIALGFFSWPFAiLIAL 165
Cdd:cd18543 113 LAFGPFLLGNLLTLVVGLVVMLVLSPPLA-LVAL 145
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
474-538 |
3.90e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 3.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2218266673 474 SGGERQ------RIALARILLQDTPIIILDEPTVGLDPITERELMETVFEVLKGKT----ILWITHHLAGVEAAD 538
Cdd:PRK01156 803 SGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipqVIMISHHRELLSVAD 877
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
26-166 |
7.06e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 38.67 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 26 AVTIFSAAFLMFTS-------GFLISKAATRPENI-LLIYVPIVAVRTFgIARSVSRYVERLVGHHIILKIVSDMRVRLY 97
Cdd:cd18778 2 ILTLLCALLSTLLGlvppwliRELVDLVTIGSKSLgLLLGLALLLLGAY-LLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 98 NMLEpgALMLR--SRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSW----------PFAILIAL 165
Cdd:cd18778 81 DKLQ--RLSLRyfDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPklalltlipiPFLALGAW 158
|
.
gi 2218266673 166 Y 166
Cdd:cd18778 159 L 159
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
18-165 |
7.39e-03 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 38.54 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2218266673 18 FVLVIFLgavTIFSAAFLMFTSGFL------ISKAATRPENILLIYVPIVAVRTFGI--ARSVSRYVERLVGHHIILKIV 89
Cdd:cd18547 1 LILVIIL---AIISTLLSVLGPYLLgkaidlIIEGLGGGGGVDFSGLLRILLLLLGLylLSALFSYLQNRLMARVSQRTV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2218266673 90 SDMRVRLYNMLEpgALMLR--SRFRTGDMLGILSEDIEHLQDAFLKTIFPAISALLLYAVSVIALGFFSWPFAILIAL 165
Cdd:cd18547 78 YDLRKDLFEKLQ--RLPLSyfDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLV 153
|
|
| |
