|
Name |
Accession |
Description |
Interval |
E-value |
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
70-295 |
9.99e-121 |
|
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: 358.89 E-value: 9.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 70 QFKIPW----RSHSSQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMKSGQIWINGQPSTPQLVR 145
Cdd:cd03234 1 QRVLPWwdvgLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 146 KCVAHVRQHDQLLPNLTVRETLAFIAQMRLPRTFSQAQRDKRVEDViaelRLRQCANTRVGNTYVRGVSGGERRRVSIGV 225
Cdd:cd03234 81 KCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDV----LLRDLALTRIGGNLVKGISGGERRRVSIAV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 226 QLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
88-663 |
2.29e-110 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 345.88 E-value: 2.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMKSGQIWINGQPSTPQLVRKCVAHVRQHDQLLPNLTVRETL 167
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNT-YVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 246
Cdd:TIGR00955 121 MFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 247 TAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQYFTSIGHPCPRYSNPADFYVDLTS 326
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 327 IDRRSKEREVATVEKaqslaalfleKVQGFDDFLWKAEAKELNTSTHTVSLTLTQDTDCGTAVEL-PGMIEQFSTLIRRQ 405
Cdd:TIGR00955 281 VIPGSENESRERIEK----------ICDSFAVSDIGRDMLVNTNLWSGKAGGLVKDSENMEGIGYnASWWTQFYALLKRS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 406 ISNDFRDLPTLLIHGSEACLMSLIIGFLYYGHGAKQLSFMDTAALLFMIGALIPFNVILDVVSKCHSERSMLYYELEDGL 485
Cdd:TIGR00955 351 WLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 486 YTAGPYFFAKILGELPEHCAYVIIYAMPIYWLTNLRPVPELFLLHFLLVWLVVFCCRTMALAASAMLPTFHMSSFFCNAL 565
Cdd:TIGR00955 431 YRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPF 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 566 YNSFYLTAGFMINLDNLWIVPAWISKLSFLRWCFSGLMQIQFNGH-----LYTTQIGNFTFSilGDTMISAMDLNSHPLY 640
Cdd:TIGR00955 511 VIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVdniecTSANTTGPCPSS--GEVILETLSFRNADLY 588
|
570 580
....*....|....*....|...
gi 1105531442 641 AIYLIVIGISYGFLFLYYLSLKL 663
Cdd:TIGR00955 589 LDLIGLVILIFFFRLLAYFALRI 611
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
98-665 |
2.12e-79 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 265.59 E-value: 2.12e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 98 GQMLAIIGSSGCGRASLLDVITGRGHGGKMkSGQIWINGQPSTPQLVRKcVAHVRQHDQLLPNLTVRETLAFIAQMRLPR 177
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNF-TGTILANNRKPTKQILKR-TGFVTQDDILYPHLTVRETLVFCSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 178 TFSQAQRDKRVEDVIAELRLRQCANTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSR 257
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 258 LAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQYFTSIGHPCPRYSNPADFYVDLTS----IDRRSkE 333
Cdd:PLN03211 252 LAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANgvcqTDGVS-E 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 334 REVATVEKA--QSLAALFLEKVQGFDDFLWKAEAKElntstHTVSLTLTQDTDCGTAVELPGMIEQFSTLIRRQISN-DF 410
Cdd:PLN03211 331 REKPNVKQSlvASYNTLLAPKVKAAIEMSHFPQANA-----RFVGSASTKEHRSSDRISISTWFNQFSILLQRSLKErKH 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 411 RDLPTLLIhgSEACLMSLIIGFLYYgHgAKQLSFMDTAALLFMI----GALIPFNVILDVvskcHSERSMLYYELEDGLY 486
Cdd:PLN03211 406 ESFNTLRV--FQVIAAALLAGLMWW-H-SDFRDVQDRLGLLFFIsifwGVFPSFNSVFVF----PQERAIFVKERASGMY 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 487 TAGPYFFAKILGELPEHCAYVIIYAMPIYWLTNLRPVPELFLLHFLLVWLVVFCCRTMALAASAMLPTFHMSSFFCNALY 566
Cdd:PLN03211 478 TLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTM 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 567 NSFYLTAGFMINldNLWIVPAWISKLSFLRWCFSGLMQIQFNGhlyttqiGNFTFSILGDTMISAMDLNS---------- 636
Cdd:PLN03211 558 LAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYRLLINVQYGE-------GKRISSLLGCSLPHGSDRASckfveedvag 628
|
570 580 590
....*....|....*....|....*....|.
gi 1105531442 637 --HPLYAIYLIVIgISYGFLFLYYLSLKLIK 665
Cdd:PLN03211 629 qiSPATSVSVLIF-MFVGYRLLAYLALRRIK 658
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
60-295 |
3.73e-79 |
|
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: 250.16 E-value: 3.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 60 SQVPWFEQLAQFKIPWRShssqDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMkSGQIWINGQPS 139
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPS----KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV-SGEVLINGRPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 140 TPQLVRKCVAHVRQHDQLLPNLTVRETLAFIAQMRlprtfsqaqrdkrvedviaelrlrqcantrvgntyvrGVSGGERR 219
Cdd:cd03213 76 DKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGERK 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1105531442 220 RVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-606 |
4.70e-55 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 203.80 E-value: 4.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 18 QDASGLQDSLFSSESDNSLYFTYSGQSNTLEVRDLTYQVDIASQVpwfEQLaqfkipwrshssqdscelgIRNLSFKVRS 97
Cdd:TIGR00956 731 EVLGSTDLTDESDDVNDEKDMEKESGEDIFHWRNLTYEVKIKKEK---RVI-------------------LNNVDGWVKP 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 98 GQMLAIIGSSGCGRASLLDVITGRGHGGKMKSGQIWINGQPSTPQLVRKcVAHVRQHDQLLPNLTVRETLAFIAQMRLPR 177
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRS-IGYVQQQDLHLPTSTVRESLRFSAYLRQPK 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 178 TFSQAQRDKRVEDVIAELRLRQCANTRVGnTYVRGVSGGERRRVSIGVQLLWNPGILI-LDEPTSGLDSFTAHNLVTTLS 256
Cdd:TIGR00956 868 SVSKSEKMEYVEEVIKLLEMESYADAVVG-VPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMR 946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 257 RLAKGNRLVLISLHQPRSDIFRLFD-LVLLMTSGTPIYLG----AAQQMVQYFTSIG-HPCPRYSNPADFYVDLTSIDRR 330
Cdd:TIGR00956 947 KLADHGQAILCTIHQPSAILFEEFDrLLLLQKGGQTVYFGdlgeNSHTIINYFEKHGaPKCPEDANPAEWMLEVIGAAPG 1026
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 331 SK-EREVATVEKAQSLAALFLEKVQGFDDFLWKAEAKELNTSTHTVSLTLtqdtdcgtavelpgmIEQFSTLIRRQISND 409
Cdd:TIGR00956 1027 AHaNQDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDALSKYAASL---------------WYQFKLVLWRTFQQY 1091
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 410 FRDLPTLLIHGSEACLMSLIIGFLYY--GHGAKQLsfmdTAALLFMIGALIPFNVILD--VVSKCHSERSMLYYELEDGL 485
Cdd:TIGR00956 1092 WRTPDYLYSKFFLTIFAALFIGFTFFkvGTSLQGL----QNQMFAVFMATVLFNPLIQqyLPPFVAQRDLYEVRERPSRT 1167
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 486 YTAGPYFFAKILGELPEHC-----AYVIIYA-MPIYW-LTNLRPVPELFLLHFLLVWLVVFCCRTMALAASAMLPTFHMS 558
Cdd:TIGR00956 1168 FSWLAFIAAQITVEIPYNLvagtiFFFIWYYpVGFYWnASKTGQVHERGVLFWLLSTMFFLYFSTLGQMVISFNPNADNA 1247
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1105531442 559 SFFCNALYNSFYLTAGFMINLDNL---WIvpaWISKLSFLRWCFSGLMQIQ 606
Cdd:TIGR00956 1248 AVLASLLFTMCLSFCGVLAPPSRMpgfWI---FMYRCSPFTYLVQALLSTG 1295
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
88-609 |
2.39e-51 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 192.63 E-value: 2.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHG-GKMKSGQIWINGQPS---TPQLvRKCVAHVRQHDQLLPNLTV 163
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfHIGVEGVITYDGITPeeiKKHY-RGDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFIAQMRLPRT----FSQAQRDKRVEDVI-AELRLRQCANTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:TIGR00956 156 GETLDFAARCKTPQNrpdgVSREEYAKHIADVYmATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRLAK-GNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQYFTSIGHPCPRYSNP 317
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTT 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 318 ADFyvdLTSIDRRSKER--------------EVATVEKAQSLAALFLEKVQGFDDFLWKAEAKE--------------LN 369
Cdd:TIGR00956 316 ADF---LTSLTSPAERQikpgyekkvprtpqEFETYWRNSPEYAQLMKEIDEYLDRCSESDTKEayreshvakqskrtRP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 370 TSTHTVSLTltqdtdcgtavelpgmiEQFSTLIRRQISNDFRDLPTLLIHGSEACLMSLIIGFLYYGhgakqlSFMDTAA 449
Cdd:TIGR00956 393 SSPYTVSFS-----------------MQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYN------LPKNTSD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 450 LLFMIGAL---IPFNVI--LDVVSKCHSERSMLYYELEDGLYTAGPYFFAKILGELPEHCAYVIIYAMPIYWLTNLRPVP 524
Cdd:TIGR00956 450 FYSRGGALffaILFNAFssLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTA 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 525 ELFLLHFLLVWLVVFC-----------CRTMALaasAMLPtfhmSSFFCNALynSFYltAGFMINLDNLWIVPAWISKLS 593
Cdd:TIGR00956 530 GRFFFYLLILFICTLAmshlfrsigavTKTLSE---AMTP----AAILLLAL--SIY--TGFAIPRPSMLGWSKWIYYVN 598
|
570
....*....|....*.
gi 1105531442 594 FLRWCFSGLMQIQFNG 609
Cdd:TIGR00956 599 PLAYAFESLMVNEFHG 614
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
88-607 |
2.35e-46 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 177.73 E-value: 2.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMKsGQIWINGQPSTPQLVRKCVAHVRQHDQLLPNLTVRETL 167
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIE-GDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 247
Cdd:PLN03140 975 IYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 248 AHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMT-SGTPIYLGA----AQQMVQYFTSI-GHP-CPRYSNPADF 320
Cdd:PLN03140 1055 AAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSGPlgrnSHKIIEYFEAIpGVPkIKEKYNPATW 1134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 321 YVDLTSIDRRSK-EREVATVEKAQSLAALFLEKVQGFDdfLWKAEAKELNTSTHTVSLTLTQDTDCgtavelpgMIEQFS 399
Cdd:PLN03140 1135 MLEVSSLAAEVKlGIDFAEHYKSSSLYQRNKALVKELS--TPPPGASDLYFATQYSQSTWGQFKSC--------LWKQWW 1204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 400 TLIRRQISNDFRDLPTLlihgseacLMSLIIGFLYYGHGAKQLSFMDtaaLLFMIGALIPfNVILDVVSKCHS------- 472
Cdd:PLN03140 1205 TYWRSPDYNLVRFFFTL--------AAALMVGTIFWKVGTKRSNAND---LTMVIGAMYA-AVLFVGINNCSTvqpmvav 1272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 473 ERSMLYYELEDGLYTAGPYFFAKILGELPehcaYV---------IIYAMPIYWLTNLRPVPELFLLHFLLVWLVVFCCRT 543
Cdd:PLN03140 1273 ERTVFYRERAAGMYSALPYAIAQVVCEIP----YVliqttyytlIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMT 1348
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 544 MALAasamlPTFHMSSFFCNALYNSFYLTAGFMI---NLDNLWIVPAWISKLSflrWCFSGLMQIQF 607
Cdd:PLN03140 1349 VSLT-----PNQQVAAIFAAAFYGLFNLFSGFFIprpKIPKWWVWYYWICPVA---WTVYGLIVSQY 1407
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
90-295 |
3.91e-43 |
|
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: 153.94 E-value: 3.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMKsGQIWINGQPSTPQLVRKcVAHVRQHDQLLPNLTVRETLAF 169
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVIT-GEILINGRPLDKNFQRS-TGYVEQQDVHSPNLTVREALRF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 170 IAqmrlprtfsqaqrdkrvedviaelrlrqcantrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAH 249
Cdd:cd03232 103 SA-------------------------------------LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1105531442 250 NLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTS-GTPIYLG 295
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
88-304 |
3.47e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 138.66 E-value: 3.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkMK--SGQIWINGQP--STPQLVRKCVAHVRQHDQLLPNLTV 163
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL-----LRptSGEVRVLGEDvaRDPAEVRRRIGYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCANTRVGnTYvrgvSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:COG1131 91 RENLRFFARLYgLPR----KEARERIDELLELFGLTDAADRKVG-TL----SGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 243 LDSFTAHNLVTTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSGTPIYLGAAQQMVQYF 304
Cdd:COG1131 162 LDPEARRELWELLRELAAEGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
88-241 |
3.79e-37 |
|
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: 135.85 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkmKSGQIWINGQPSTP---QLVRKCVAHVRQHDQLLPNLTVR 164
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP---TEGTILLDGQDLTDderKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 165 ETLAFIAQMRLPrtfSQAQRDKRVEDVIAELRLRQCANTRVGNtYVRGVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:pfam00005 78 ENLRLGLLLKGL---SKREKDARAEEALEKLGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
88-295 |
2.22e-35 |
|
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: 132.77 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMKSGQIWINGQPS--TPQLVRKCVAHVRQHDQLLPNLTVRE 165
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYkeFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAQMRlprtfsqaqrdkrvedviaelrlrqcantrvGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 245
Cdd:cd03233 103 TLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1105531442 246 FTAHNLVTTLSRLAKGNRLV-LISLHQPRSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:cd03233 152 STALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
401-605 |
6.18e-35 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 131.24 E-value: 6.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 401 LIRRQISNDFRDLPTLLIHGSEACLMSLIIGFLYYGHGaKQLSFMDTAALLFMIGALIPFNVILDVVSKCHSERSMLYYE 480
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG-NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 481 LEDGLYTAGPYFFAKILGELPEHCAYVIIYAMPIYWLTNLRPVPELFLLHFLLVWLVVFCCRTMALAASAMLPTFHMSSF 560
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1105531442 561 FCNALYNSFYLTAGFMINLDNLWIVPAWISKLSFLRWCFSGLMQI 605
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
88-299 |
8.63e-34 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 128.78 E-value: 8.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP--STPQLVRKCVAHVRQHDQLLPNLTVRE 165
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL---RPTSGTAYINGYSirTDRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAQMR-LPRTfsqaQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:cd03263 95 HLRFYARLKgLPKS----EIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1105531442 245 SFTAHNLVTTLSRLaKGNRLVLISLHQPRsDIFRLFDLVLLMTSGTPIYLGAAQQ 299
Cdd:cd03263 166 PASRRAIWDLILEV-RKGRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
87-299 |
2.40e-33 |
|
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: 128.05 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPST--PQLVRKCVAHVRQHDQLLPNLTVR 164
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL---KPDSGSILIDGEDVRkePREARRQIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIA-QMRLPRtfsqAQRDKRVEDVIAELRLRQCANTRVGntyvrGVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:COG4555 93 ENIRYFAeLYGLFD----EELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1105531442 244 DSFTAHNLVTTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSGTPIYLGAAQQ 299
Cdd:COG4555 164 DVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
77-290 |
5.13e-32 |
|
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: 123.35 E-value: 5.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 77 SHSSQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP---STPQLVRKCVAHVRQ 153
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL---GPTSGEVLVDGKDltkLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 154 H--DQLLpNLTVRETLAF-IAQMRLPRtfsqAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWN 230
Cdd:cd03225 83 NpdDQFF-GPTVEEEVAFgLENLGLPE----EEIEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 231 PGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSGT 290
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
88-290 |
1.64e-29 |
|
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: 114.26 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPqlvrkcvahvrqhdqlLPNLTVRETL 167
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL---KPTSGEILIDGKDIAK----------------LPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMrlprtfsqaqrdkrvedviaelrlrqcantrvgntyvrgvSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 247
Cdd:cd00267 76 GYVPQL----------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1105531442 248 AHNLVTTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSGT 290
Cdd:cd00267 116 RERLLELLRELAEEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
88-289 |
3.07e-29 |
|
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: 115.69 E-value: 3.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRK-CVAHVRQHDQLLPNLTVRET 166
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE---RPDSGEILIDGRDVTGVPPERrNIGMVFQDYALFPHLTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 LAFiaQMRLpRTFSQAQRDKRVEDVIAELRLRqcantRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 246
Cdd:cd03259 93 IAF--GLKL-RGVPKAEIRARVRELLELVGLE-----GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1105531442 247 TAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSG 289
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
88-301 |
8.09e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 115.53 E-value: 8.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP----STPQLVRKcVAHVRQHDQLLPNLTV 163
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLL---KPSSGEVLLDGRDlaslSRRELARR-IAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAF--IAQMRLPRTFSQAQRDKrVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIG---VQllwNPGILILDE 238
Cdd:COG1120 93 RELVALgrYPHLGLFGRPSAEDREA-VEEALERTGLEHLADRPVDE-----LSGGERQRVLIAralAQ---EPPLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRLAKG-NRLVLISLHqprsDI---FRLFDLVLLMTSGTPIYLGAAQQMV 301
Cdd:COG1120 164 PTSHLDLAHQLEVLELLRRLARErGRTVVMVLH----DLnlaARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
88-299 |
1.21e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.80 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggKMK--SGQIWINGQPstPQLVRKCVAHVRQH---DQLLPnLT 162
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG-----LLPptSGTVRLFGKP--PRRARRRIGYVPQRaevDWDFP-IT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLA--FIAQMRLPRTFSQAQRDkRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:COG1121 94 VRDVVLmgRYGRRGLFRRPSRADRE-AVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 241 SGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMtSGTPIYLGAAQQ 299
Cdd:COG1121 168 AGVDAATEEALYELLRELRREGKTILVVTHDL-GAVREYFDRVLLL-NRGLVAHGPPEE 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
88-295 |
1.25e-28 |
|
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: 113.83 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGqMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPST--PQLVRKCVAHVRQHDQLLPNLTVRE 165
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLT---PPSSGTIRIDGQDVLkqPQKLRRRIGYLPQEFGVYPNFTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQCANTRVGntyvrGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 245
Cdd:cd03264 92 FLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1105531442 246 FTAHNLVTTLSRLAKgNRLVLISLHQpRSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:cd03264 164 EERIRFRNLLSELGE-DRIVILSTHI-VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
88-299 |
5.17e-28 |
|
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: 112.43 E-value: 5.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKMKSGQIWINGQPstpqLVRKCVAHVRQH---------DQLL 158
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG---LLKPTSGEVLVDGKD----ITKKNLRELRRKvglvfqnpdDQLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 pNLTVRETLAF-IAQMRLPRtfsqAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSI-GVqLLWNPGILIL 236
Cdd:COG1122 90 -APTVEEDVAFgPENLGLPR----EEIRERVEEALELVGLEHLADRPPHE-----LSGGQKQRVAIaGV-LAMEPEVLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1105531442 237 DEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRsDIFRLFDLVLLMTSGTPIYLGAAQQ 299
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDDGRIVADGTPRE 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
89-272 |
5.21e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.80 E-value: 5.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP--STPQLVRKCVAHVRQHDQLLPNLTVRET 166
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLL---PPSAGEVLWNGEPirDAREDYRRRLAYLGHADGLKPELTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 LAFIAQMRlprtfSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 246
Cdd:COG4133 96 LRFWAALY-----GLRADREAIDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180
....*....|....*....|....*.
gi 1105531442 247 TAHNLVTTLSRLAKGNRLVLISLHQP 272
Cdd:COG4133 166 GVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
88-295 |
1.40e-27 |
|
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: 110.70 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPstPQLVRKCVAHVRQHDQLLPN--LTVRE 165
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLL---KPTSGSIRVFGKP--LEKERKRIGYVPQRRSIDRDfpISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 T--LAFIAQMRLPRTFSQAQRDKrVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:cd03235 90 VvlMGLYGHKGLFRRLSKADKAK-VDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 244 DSFTAHNLVTTLSRLAKGNRLVLISLHQPRSdIFRLFDLVLLMTsGTPIYLG 295
Cdd:cd03235 164 DPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
90-295 |
4.84e-27 |
|
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: 109.31 E-value: 4.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVrSGQMLAIIGSSGCGRASLLDVITG--RGHGGKMK-SGQIWINGQPS--TPQLVRKcVAHVRQHDQLLPNLTVR 164
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGleKPDGGTIVlNGTVLFDSRKKinLPPQQRK-IGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAqmrlpRTFSQAQRDKRVEDVIAELRLRQcantrVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:cd03297 94 ENLAFGL-----KRKRNREDRISVDELLDLLGLDH-----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 245 SFTAHNLVTTLSRLAKG-NRLVLISLHQPrSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:cd03297 164 RALRLQLLPELKQIKKNlNIPVIFVTHDL-SEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
88-289 |
2.29e-26 |
|
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: 107.58 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPST-------PQLVRKCVAHVRQHDQLLPN 160
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLD---RPTSGEVRVDGTDISklsekelAAFRRRHIGFVFQSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:cd03255 97 LTALENVELPLLLA---GVPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1105531442 241 SGLDSFTAHNLVTTLSRLAKG-NRLVLISLHQPrsDIFRLFDLVLLMTSG 289
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEaGTTIVVVTHDP--ELAEYADRIIELRDG 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
88-299 |
2.74e-26 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 107.91 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggKMK--SGQIWINGQPSTP----QLVRKCVAHVRQHDQLLPNL 161
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISG-----FLRptSGSVLFDGEDITGlpphEIARLGIGRTFQIPRLFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFIAQMRLPRTFSQAQR-------DKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGIL 234
Cdd:cd03219 91 TVLENVMVAAQARTGSGLLLARArreereaRERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 235 ILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHqprsD---IFRLFDLVLLMTSGTPIYLGAAQQ 299
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEH----DmdvVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
88-289 |
2.82e-26 |
|
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: 105.56 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkMK--SGQIWINGQP--STPQLVRKCVAHVRQHDQLLPNLTV 163
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL-----LKpdSGEIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFiaqmrlprtfsqaqrdkrvedviaelrlrqcantrvgntyvrgvSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:cd03230 91 RENLKL--------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1105531442 244 DSFTAHNLVTTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSG 289
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHIL-EEAERLCDRVAILNNG 171
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
88-289 |
3.59e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 107.05 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGG--KMKSGQIWINGQP----STPQLV---RKCVAHVRQHDQLL 158
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL-----GGldRPTSGEVLIDGQDisslSERELArlrRRHIGFVFQFFNLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 PNLTVRETLAFIAqmrLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:COG1136 99 PELTALENVALPL---LLAGVSRKERRERARELLERVGLGDRLDHRPSQ-----LSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRLAK-GNRLVLISLHQPRsdIFRLFDLVLLMTSG 289
Cdd:COG1136 171 PTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDPE--LAARADRVIRLRDG 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
88-267 |
4.53e-26 |
|
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: 107.32 E-value: 4.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLL-------DVitgrghggkmKSGQIWINGQP---STPQLVRKCVAHVRQhDQL 157
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILrllfrfyDV----------SSGSILIDGQDireVTLDSLRRAIGVVPQ-DTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 158 LPNLTVRETLAFiaqMRLPRTFSQ---AQRDKRVEDVIaeLRLRQCANTRVGNtyvRGV--SGGERRRVSIGVQLLWNPG 232
Cdd:cd03253 86 LFNDTIGYNIRY---GRPDATDEEvieAAKAAQIHDKI--MRFPDGYDTIVGE---RGLklSGGEKQRVAIARAILKNPP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1105531442 233 ILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLI 267
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI 192
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
88-302 |
4.93e-26 |
|
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: 112.93 E-value: 4.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkmKSGQIWINGQPST---PQLVRKCVAHVRQHDQLLPNlTVR 164
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP---YSGSILINGVDLSdldPASWRRQIAWVPQNPYLFAG-TIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAF------IAQMRlprtfsQAQRDKRVEDVIAelRLRQCANTRVGNTyVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:COG4988 429 ENLRLgrpdasDEELE------AALEAAGLDEFVA--ALPDGLDTPLGEG-GRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRLAKGnRLVLISLHQPrSDIfRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:COG4988 500 PTAHLDAETEAEILQALRRLAKG-RTVILITHRL-ALL-AQADRILVLDDGRIVEQGTHEELLA 560
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
88-290 |
5.01e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 106.05 E-value: 5.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHggkmkSGQIWINGQP---STPQLVRKCVAHVRQHDQLLPNlT 162
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADldPPT-----SGEIYLDGKPlsaMPPPEWRRQVAYVPQEPALWGG-T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFIAQMRlprtfSQAQRDKRVEDVIAELRLRQ-CANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:COG4619 90 VRDNLPFPFQLR-----ERKFDRERALELLERLGLPPdILDKPVER-----LSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGNR--LVLISlHQPRsDIFRLFDLVLLMTSGT 290
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGraVLWVS-HDPE-QIERVADRVLTLEAGR 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
88-295 |
1.40e-25 |
|
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: 105.63 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRKCVahVRQHDQLLPNLTVRETL 167
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLA---QPTSGGVILEGKQITEPGPDRMV--VFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AfIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 247
Cdd:TIGR01184 76 A-LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1105531442 248 AHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
88-288 |
2.02e-25 |
|
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: 104.86 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRkcVAHVRQHDQLLPNLTVRETL 167
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLE---RPTSGEVLVDGEPVTGPGPD--RGYVFQQDALLPWLTVLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMRLPRTfsqAQRDKRVEDVIAELRLrqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 247
Cdd:cd03293 95 ALGLELQGVPK---AEARERAEELLELVGL-----SGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1105531442 248 AHNLVTTLSRLAKGNRL--VLISlHqprsDI---FRLFDLVLLMTS 288
Cdd:cd03293 167 REQLQEELLDIWRETGKtvLLVT-H----DIdeaVFLADRVVVLSA 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
88-289 |
4.04e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.17 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGGKMK--SGQIWINGQPSTPQLVRkcVAHVRQHDQLLPNLTVRE 165
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLI-----AGLEKptSGEVLVDGKPVTGPGPD--RGVVFQEPALLPWLTVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCANTrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:COG1116 100 NVALGLELRgVPK----AERRERARELLELVGLAGFEDA-----YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1105531442 245 SFTAHNLVTTLSRLAKGNRL--VLISlHqprsDIF---RLFDLVLLMTSG 289
Cdd:COG1116 171 ALTRERLQDELLRLWQETGKtvLFVT-H----DVDeavFLADRVVVLSAR 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
88-290 |
5.51e-25 |
|
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: 102.27 E-value: 5.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKMKSGQIWINGQPST-----PQLVRKCVAHVRQHDQLLPNLT 162
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL---EEPDSGSILIDGEDLTdledeLPPLRRRIGMVFQDFALFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFiaqmrlprtfsqaqrdkrvedviaelrlrqcantrvgntyvrGVSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:cd03229 93 VLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1105531442 243 LDSFTAHNLVTTLSRL-AKGNRLVLISLHQPRsDIFRLFDLVLLMTSGT 290
Cdd:cd03229 131 LDPITRREVRALLKSLqAQLGITVVLVTHDLD-EAARLADRVVVLRDGK 178
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
88-289 |
1.23e-24 |
|
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: 100.92 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkM---KSGQIWINGQP---STPQLVRKCVAHVRQHDQLLpNL 161
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLR------LydpTSGEILIDGVDlrdLDLESLRKNIAYVPQDPFLF-SG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLafiaqmrlprtfsqaqrdkrvedviaelrlrqcantrvgntyvrgVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:cd03228 91 TIRENI---------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGnRLVLISLHQPRSdiFRLFDLVLLMTSG 289
Cdd:cd03228 126 ALDPETEALILEALRALAKG-KTVIVIAHRLST--IRDADRIIVLDDG 170
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
87-286 |
1.65e-24 |
|
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: 107.76 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGkmkSGQIWINGQPST---PQLVRKCVAHVRQHDQLLPNlTV 163
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIAVNGVPLAdadADSWRDQIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRlrQCANTRVGNTyVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:TIGR02857 413 AENIRLARPDASDAEIREALERAGLDEFVAALP--QGLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1105531442 244 DSFTAHNLVTTLSRLAKGnRLVLISLHQPRSdiFRLFDLVLLM 286
Cdd:TIGR02857 490 DAETEAEVLEALRALAQG-RTVLLVTHRLAL--AALADRIVVL 529
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
88-302 |
2.22e-24 |
|
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: 107.93 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkM---KSGQIWINGQPST---PQLVRKCVAHVRQHDQLLpNL 161
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR------FldpQSGSITLGGVDLRdldEDDLRRRIAVVPQRPHLF-DT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFI------AQMRlprtfsQAQRDKRVEDVIAelRLRQCANTRVGNTYvRGVSGGERRRVSIGVQLLWNPGILI 235
Cdd:COG4987 424 TLRENLRLArpdatdEELW------AALERVGLGDWLA--ALPDGLDTWLGEGG-RRLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 236 LDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISlHQPRSdiFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEALAGRTVLLIT-HRLAG--LERMDRILVLEDGRIVEQGTHEELLA 558
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
85-295 |
4.10e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 101.64 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 85 ELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPST---PQlvRKCVAHVRQHDQLLPNL 161
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFI---KPDSGKILLNGKDITnlpPE--KRDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFiaQMRLpRTFSQAQRDKRVEDVIAELRLRQcantrVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:cd03299 87 TVYKNIAY--GLKK-RKVDKKEIERKVLEIAEMLGIDH-----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
88-295 |
8.54e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 100.93 E-value: 8.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggKMKSGQIWINGQP----STPQLvRKCVAHV--RQHDQLLPNL 161
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP--PTYGNDVRLFGERrggeDVWEL-RKRIGLVspALQLRFPRDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETL--AFIAQMRLPRTFSQAQRDkRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEP 239
Cdd:COG1119 96 TVLDVVlsGFFDSIGLYREPTDEQRE-RARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 240 TSGLDSFTAHNLVTTLSRLAKGNR--LVLISlHQPrSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:COG1119 170 TAGLDLGARELLLALLDKLAAEGAptLVLVT-HHV-EEIPPGITHVLLLKDGRVVAAG 225
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
88-326 |
1.63e-23 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 106.47 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMKSGQIWINGQPSTPQLVRKCVAHVRQHDQLLPNLTVRETL 167
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKETL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMR-----------LPR------TFSQAQRDKRVEDVIAE--------------LRLRQCANTRVGNTYVRGVSGG 216
Cdd:PLN03140 261 DFSARCQgvgtrydllseLARrekdagIFPEAEVDLFMKATAMEgvksslitdytlkiLGLDICKDTIVGDEMIRGISGG 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 217 ERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNR-LVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:PLN03140 341 QKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILLSEGQIVYQG 420
|
250 260 270
....*....|....*....|....*....|.
gi 1105531442 296 AAQQMVQYFTSIGHPCPRYSNPADFYVDLTS 326
Cdd:PLN03140 421 PRDHILEFFESCGFKCPERKGTADFLQEVTS 451
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
88-299 |
1.64e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.19 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHggkmkSGQIWINGQP----STPQLVRKcVAHVRQHDQLLPNL 161
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGelTPS-----SGEVRLNGRPlaawSPWELARR-RAVLPQHSSLAFPF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVREtlafIAQM-RLPRTFSQAQRDKRVEDViaeLRLRQCANTRvGNTYvRGVSGGERRRVsigvQL------LWN---- 230
Cdd:COG4559 91 TVEE----VVALgRAPHGSSAAQDRQIVREA---LALVGLAHLA-GRSY-QTLSGGEQQRV----QLarvlaqLWEpvdg 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 231 -PGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHqprsdifrlfDL---------VLLMTSGTPIYLGAAQQ 299
Cdd:COG4559 158 gPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH----------DLnlaaqyadrILLLHQGRLVAQGTPEE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
88-310 |
2.17e-23 |
|
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: 104.21 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKMKSGQIWINGQPsTPQLVRKCVAHVRQH---------DQLL 158
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL---LRPTSGSILFDGKD-LTKLSRRSLRELRRRvqmvfqdpySSLN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 PNLTVRETLAFIaqMRLPRTFSQAQRDKRVEDVIAELRLrqcaNTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:COG1123 357 PRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGL----PPDLADRYPHELSGGQRQRVAIARALALEPKLLILDE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRLAKGNRL--VLISlHqprsDI---FRLFDLVLLMTSGTPIYLGAAQQMvqyFTSIGHP 310
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDLQRELGLtyLFIS-H----DLavvRYIADRVAVMYDGRIVEDGPTEEV---FANPQHP 499
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
88-300 |
4.79e-23 |
|
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: 103.44 E-value: 4.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR-GHGGKMkSGQIWINGQP---STPQLVRKCVAHVRQH--DQLLPnL 161
Cdd:COG1123 22 VDGVSLTIAPGETVALVGESGSGKSTLALALMGLlPHGGRI-SGEVLLDGRDlleLSEALRGRRIGMVFQDpmTQLNP-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFIAQMRLprtFSQAQRDKRVEDVIAELRLRqcantRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:COG1123 100 TVGDQIAEALENLG---LSRAEARARVLELLEAVGLE-----RRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1105531442 242 GLDSFTAHNLVTTLSRLAK--GNRLVLISlHQPrSDIFRLFDLVLLMTSGTPIYLGAAQQM 300
Cdd:COG1123 172 ALDVTTQAEILDLLRELQRerGTTVLLIT-HDL-GVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
88-322 |
5.23e-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: 98.18 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkmKSGQIWINGQPSTPQLVRK-CVAHVRQHDQLLPNLTVRET 166
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP---DSGTILFGGEDATDVPVQErNVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 LAFIAQMRlPRTF--SQAQRDKRVEDViaeLRLRQCANtrVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:cd03296 95 VAFGLRVK-PRSErpPEAEIRAKVHEL---LKLVQLDW--LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 245 SFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQMvqyftsighpcprYSNPADFYV 322
Cdd:cd03296 169 AKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV-------------YDHPASPFV 233
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
47-295 |
8.31e-23 |
|
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: 97.79 E-value: 8.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 47 LEVRDLTYQVDIASQVPWFEQLAQ--FKIPWRSHSSqdscelgIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHG 124
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGLIGSLKslFKRKYREVEA-------LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 125 gkmKSGQIWINGQ-PST--PQLVRKCVAHVRQHDQLLPNLTVRETLAFIAQM-RLPRTFSQAQRDKRVEdviaelrLRQC 200
Cdd:cd03267 74 ---TSGEVRVAGLvPWKrrKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIyDLPPARFKKRLDELSE-------LLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 201 anTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLakgNRL----VLISLHQPRsDI 276
Cdd:cd03267 144 --EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY---NRErgttVLLTSHYMK-DI 217
|
250
....*....|....*....
gi 1105531442 277 FRLFDLVLLMTSGTPIYLG 295
Cdd:cd03267 218 EALARRVLVIDKGRLLYDG 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
88-299 |
1.25e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.92 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGkmkSGQIWINGQP----STPQLVRkCVAHVRQHDQLLPNLTV 163
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD---SGEVRLNGRPladwSPAELAR-RRAVLPQHSSLSFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 REtlafIAQM-RLPRTFSQAQRDKRVEDVIAELRLRQCANtRvgntYVRGVSGGERRRVsigvQL------LWN----PG 232
Cdd:PRK13548 94 EE----VVAMgRAPHGLSRAEDDALVAAALAQVDLAHLAG-R----DYPQLSGGEQQRV----QLarvlaqLWEpdgpPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 233 ILILDEPTSGLDSFTAHNLVTTLSRLAKGNRL-VLISLHqprsdifrlfDL---------VLLMTSGTPIYLGAAQQ 299
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLAHERGLaVIVVLH----------DLnlaaryadrIVLLHQGRLVADGTPAE 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
88-299 |
1.65e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 97.42 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkMK--SGQIWINGQP----STPQLVRKCVAhvR--QHDQLLP 159
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF-----YRptSGRILFDGRDitglPPHRIARLGIA--RtfQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVRE--TLAFIAQMR------LPRTFSQAQRDK----RVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQL 227
Cdd:COG0411 93 ELTVLEnvLVAAHARLGrgllaaLLRLPRARREEReareRAEELLERVGLADRADEPAGN-----LSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 228 LWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRL--VLISlHqprsD---IFRLFDLVLLMTSGTPIYLGAAQQ 299
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGItiLLIE-H----DmdlVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
89-302 |
1.71e-22 |
|
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: 96.80 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGGKMK--SGQIWINGQPSTP------QLVRKCVAHVRQHDQLLPN 160
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLI-----VGLLRpdSGEVLIDGEDISGlseaelYRLRRRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFiaQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:cd03261 92 LTVFENVAF--PLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 241 SGLDSFTAHNLVTTLSRL--AKGNRLVLISlHQpRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:cd03261 165 AGLDPIASGVIDDLIRSLkkELGLTSIMVT-HD-LDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
87-299 |
2.60e-22 |
|
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: 96.48 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkmKSGQIWING------QPSTPQLVRKCVAHVRQHDQLLPN 160
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP---TSGSVLIDGtdinklKGKALRQLRRQIGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRET-----LAFIAQMR-LPRTFSQAQRDKRVEdVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGIL 234
Cdd:cd03256 93 LSVLENvlsgrLGRRSTWRsLFGLFPKEEKQRALA-ALERVGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 235 ILDEPTSGLDSFTAHNLVTTLSRLAKG-NRLVLISLHQPrsDIFRLF-DLVLLMTSGTPIYLGAAQQ 299
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQV--DLAREYaDRIVGLKDGRIVFDGPPAE 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
88-268 |
3.86e-22 |
|
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: 95.65 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTP------QLVRKCVAHVRQHDQ--LLP 159
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL---KPTSGSIIFDGKDLLKlsrrlrKIRRKEIQMVFQDPMssLNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVRETLAFIAQMRLPRTfSQAQRDKRVEDVIAELRLRqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEP 239
Cdd:cd03257 98 RMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGLP----EEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190
....*....|....*....|....*....|.
gi 1105531442 240 TSGLDSFTAHNLVTTLSRLAK--GNRLVLIS 268
Cdd:cd03257 173 TSALDVSVQAQILDLLKKLQEelGLTLLFIT 203
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
88-302 |
5.12e-22 |
|
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: 101.06 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkM---KSGQIWINGQPST---PQLVRKCVAHVRQHDQLLpNL 161
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG------LyepTSGRILIDGIDLRqidPASLRRQIGVVLQDVFLF-SG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAF------IAQMRlprtfsQAQRDKRVEDVIAELRLRqcANTRVGNtyvRGV--SGGERRRVSIGVQLLWNPGI 233
Cdd:COG2274 564 TIRENITLgdpdatDEEII------EAARLAGLHDFIEALPMG--YDTVVGE---GGSnlSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 234 LILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISlHqpRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKGRTVIIIA-H--RLSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
90-270 |
5.99e-22 |
|
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: 94.78 E-value: 5.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPsTPQLVRKCVAHVRQH-------DQLLPNLT 162
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEE---LPTSGTIRVNGQD-VSDLRGRAIPYLRRKigvvfqdFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFiaQMRLPRTFSQAQRdKRVEDVIAELRLRQCANTrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:cd03292 95 VYENVAF--ALEVTGVPPREIR-KRVPAALELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180
....*....|....*....|....*...
gi 1105531442 243 LDSFTAHNLVTTLSRLAKGNRLVLISLH 270
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
88-291 |
6.16e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 95.70 E-value: 6.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRKCVahVRQHDQLLPNLTVRETL 167
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFL---APSSGEITLDGVPVTGPGADRGV--VFQKDALLPWLNVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQcantrVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 246
Cdd:COG4525 98 AFGLRLRgVPK----AERRARAEELLALVGLAD-----FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1105531442 247 TAHNLVTTLSRL-AKGNRLVLISLHQPRSDIFRLFDLVLLmtSGTP 291
Cdd:COG4525 169 TREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM--SPGP 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
88-243 |
8.63e-22 |
|
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: 94.42 E-value: 8.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkM---KSGQIWINGQP----STPQLVRKCVAHVRQHDQLLPN 160
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMG------LlppRSGSIRFDGRDitglPPHERARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLafiaqmrlpRTFSQAQRDKRVEDVIAEL-----RLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILI 235
Cdd:cd03224 90 LTVEENL---------LLGAYARRRAKRKARLERVyelfpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLL 155
|
....*...
gi 1105531442 236 LDEPTSGL 243
Cdd:cd03224 156 LDEPSEGL 163
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
83-322 |
1.32e-21 |
|
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: 95.02 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 83 SCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTP-------QLVRKCVAHVRQHD 155
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI---EPTSGKVLIDGQDIAAmsrkelrELRRKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 156 QLLPNLTVRETLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQcantrVGNTYVRGVSGGERRRVSIGVQLLWNPGIL 234
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQgVPR----AEREERAAEALELVGLEG-----WEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 235 ILDEPTSGLDSFTAHNLVTTLSRLAK--GNRLVLISlHQPrSDIFRLFDLVLLMTSGtpiylgaaqQMVQyftsIGHPCP 312
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAelQKTIVFIT-HDL-DEALRLGDRIAIMKDG---------RLVQ----VGTPEE 247
|
250
....*....|
gi 1105531442 313 RYSNPADFYV 322
Cdd:cd03294 248 ILTNPANDYV 257
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
88-289 |
2.44e-21 |
|
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: 93.41 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQ------PSTPQLVRKCVAHVRQHDQLLPNL 161
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLE---RPTSGSVLVDGTdltllsGKELRKARRRIGMIFQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAF---IAQMrlprtfSQAQRDKRVEDVIAELRLRQCANTrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:cd03258 98 TVFENVALpleIAGV------PKAEIEERVLELLELVGLEDKADA-----YPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRLAK--GNRLVLISlHQpRSDIFRLFDLVLLMTSG 289
Cdd:cd03258 167 ATSALDPETTQSILALLRDINRelGLTIVLIT-HE-MEVVKRICDRVAVMEKG 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
89-270 |
2.66e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.81 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKMKSGQIWINGQPSTpQLVRKCVAHVRQH------D-QLLPNL 161
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG---EERPTSGQVLVNGQDLS-RLKRREIPYLRRRigvvfqDfRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFIaqMRLpRTFSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:COG2884 95 TVYENVALP--LRV-TGKSRKEIRRRVREVLDLVGLSDKAKALPHE-----LSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|..
gi 1105531442 242 GLDSFTAHNLVTTLSRLakgNRL---VLISLH 270
Cdd:COG2884 167 NLDPETSWEIMELLEEI---NRRgttVLIATH 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
88-295 |
3.54e-21 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 92.43 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWING--QPSTPQLVRKCVAHVRQHDQLLPNLTVRE 165
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL---EPDAGFATVDGfdVVKEPAEARRRLGFVSDSTGLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAqmRLPRTFSQAQRDkRVEDVIAELRLRQCANTRVGntyvrGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 245
Cdd:cd03266 98 NLEYFA--GLYGLKGDELTA-RLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1105531442 246 FTAHNLVTTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:cd03266 170 MATRALREFIRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
88-270 |
4.94e-21 |
|
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: 92.29 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITgRGHggKMKSGQIWINGQP----STPQLvRKCVAHVRQhDQLLPNLTV 163
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFY--DVDSGRILIDGHDvrdyTLASL-RRQIGLVSQ-DVFLFNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFiaqmrlprtfsqAQRDKRVEDVIAELRLrqcAN-------------TRVGntyVRGV--SGGERRRVSIGVQLL 228
Cdd:cd03251 93 AENIAY------------GRPGATREEVEEAARA---ANahefimelpegydTVIG---ERGVklSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1105531442 229 WNPGILILDEPTSGLDSFTAHNLVTTLSRLAKgNRLVLISLH 270
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAH 195
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
88-302 |
5.91e-21 |
|
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: 92.22 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLV----RKCVAHVRQHDQLLPNLTV 163
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV---KPDSGKILLDGQDITKLPMhkraRLGIGYLPQEASIFRKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLrqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:cd03218 93 EENILAVLEIR---GLSKKEREEKLEELLEEFHI-----THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 244 DSFTAHNLVTTLSRLAKGNRLVLISLHQPRsDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITDHNVR-ETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
88-244 |
7.86e-21 |
|
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: 91.16 E-value: 7.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPST--PQLVRKcVAHVRQHDQLLPNLTVRE 165
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE---EPTSGRIYIGGRDVTdlPPKDRD-IAMVFQNYALYPHMTVYD 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 166 TLAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQcantrVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:cd03301 92 NIAFGLKLR---KVPKDEIDERVREVAELLQIEH-----LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
88-289 |
1.45e-20 |
|
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: 90.42 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPqLVRKCVAHVRQHDQLLPNLTVRETL 167
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII---LPDSGEVLFDGKPLDI-AARNRIGYLPEERGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMR-LPRtfSQAQRdkRVEDVIAELRLRQCANTRVgntyvRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 246
Cdd:cd03269 92 VYLAQLKgLKK--EEARR--RIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1105531442 247 TAHNLVTTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSG 289
Cdd:cd03269 163 NVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKG 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
89-271 |
1.84e-20 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 90.28 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQ-----LVRKCVAHVRQHDQLLPNLTV 163
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLE---EPDSGTIIIDGLKLTDDkkninELRQKVGMVFQQFNLFPHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAfIAQMRLpRTFSQAQRDKRVEDVIAELRLRQCANTrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:cd03262 94 LENIT-LAPIKV-KGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180
....*....|....*....|....*...
gi 1105531442 244 DSFTAHNLVTTLSRLAKGNRLVLISLHQ 271
Cdd:cd03262 167 DPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
88-295 |
2.33e-20 |
|
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: 89.03 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPsTPQLVRKCVAhvrqhdqllpnltvrETL 167
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLL---KPSSGEILLDGKD-LASLSPKELA---------------RKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMrlprtfsqaqrdkrVEDV-IAELRLRqcantrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 246
Cdd:cd03214 76 AYVPQA--------------LELLgLAHLADR----------PFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1105531442 247 TAHNLVTTLSRLAK-GNRLVLISLHqprsDI---FRLFDLVLLMTSGTPIYLG 295
Cdd:cd03214 132 HQIELLELLRRLAReRGKTVVMVLH----DLnlaARYADRVILLKDGRIVAQG 180
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
88-285 |
2.72e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.91 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRKCVahVRQHDQLLPNLTVRETL 167
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFV---PYQHGSITLDGKPVEGPGAERGV--VFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMRlprTFSQAQRDKRVEDVIAELRLRQcantrVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 247
Cdd:PRK11248 92 AFGLQLA---GVEKMQRLEIAHQMLKKVGLEG-----AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1105531442 248 AHNLVTTLSRL-AKGNRLVLISLHQPRSDIFRLFDLVLL 285
Cdd:PRK11248 164 REQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
88-243 |
3.49e-20 |
|
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: 90.04 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP----STPQLVRKCVAHVRQHDQLLPNLTV 163
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLL---PPRSGSIRFDGEDitglPPHRIARLGIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLafiaQMRLPRTFSQAQRDKRVEDViAEL--RLRQCANTRVGNTyvrgvSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:COG0410 96 EENL----LLGAYARRDRAEVRADLERV-YELfpRLKERRRQRAGTL-----SGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
..
gi 1105531442 242 GL 243
Cdd:COG0410 166 GL 167
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
88-267 |
3.71e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.85 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGR---ASLL----DVitgrghggkmKSGQIWINGQPS---TPQLVRKCVAHVRQHDQL 157
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKstlVNLLlrfyDP----------TSGRILIDGVDIrdlTLESLRRQIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 158 LpNLTVRETLAFiaqmrlprtfsqAQRDKRVEDVIAELRLRQCA----------NTRVGNtyvRGV--SGGERRRVSIGV 225
Cdd:COG1132 426 F-SGTIRENIRY------------GRPDATDEEVEEAAKAAQAHefiealpdgyDTVVGE---RGVnlSGGQRQRIAIAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1105531442 226 QLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGnRLVLI 267
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKG-RTTIV 530
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
90-271 |
4.40e-20 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 88.81 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQpsTPQLVRKCVAHVR---QHDQLLPNLTVRET 166
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI---KPDSGEITFDGK--SYQKNIEALRRIGaliEAPGFYPNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 LAFIAqmRLPRTfsqaqRDKRVEDVIAELRLRQCANTRVGntyvrGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 246
Cdd:cd03268 93 LRLLA--RLLGI-----RKKRIDEVLDVVGLKDSAKKKVK-----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180
....*....|....*....|....*
gi 1105531442 247 TAHNLVTTLSRLAKGNRLVLISLHQ 271
Cdd:cd03268 161 GIKELRELILSLRDQGITVLISSHL 185
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
89-289 |
4.54e-20 |
|
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: 89.86 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHggkmkSGQIWINGQPSTPQL---VRKCVAHVRQH--DQLLPNL 161
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALAGleRPW-----SGEVTFDGRPVTRRRrkaFRRRVQMVFQDpyASLHPRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAF-IAQMRLPRtfsqaqRDKRVEDVIAELRLRQCANTRvgntYVRGVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:COG1124 97 TVDRILAEpLRIHGLPD------REERIAELLEQVGLPPSFLDR----YPHQLSGGQRQRVAIARALILEPELLLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 241 SGLD-SFTAH--NLVTTLsRLAKGNRLVLISlHQPRSdIFRLFDLVLLMTSG 289
Cdd:COG1124 167 SALDvSVQAEilNLLKDL-REERGLTYLFVS-HDLAV-VAHLCDRVAVMQNG 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
88-301 |
5.00e-20 |
|
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: 89.85 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkM---KSGQIWINGQP---STPQLVRKCVAHVRQhDQLLPNL 161
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR------FyvpENGRVLVDGHDlalADPAWLRRQVGVVLQ-ENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQcaNTRVGNTYVrGVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:cd03252 91 SIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGY--DTIVGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGnRLVLISLHqpRSDIFRLFDLVLLMTSGTPIYLGAAQQMV 301
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAG-RTVIIIAH--RLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
88-290 |
6.04e-20 |
|
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: 88.47 E-value: 6.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRKCVAHVRQH--DQLLPNlTVRE 165
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI---KESSGSILLNGKPIKAKERRKSIGYVMQDvdYQLFTD-SVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFiaqmRLPRTfsqAQRDKRVEDVIAELRLrqcantrvgNTYV----RGVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:cd03226 92 ELLL----GLKEL---DAGNEQAETVLKDLDL---------YALKerhpLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSdIFRLFDLVLLMTSGT 290
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGA 203
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
88-270 |
7.78e-20 |
|
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: 87.86 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKMKSGQIWINGQP---STPQL--VRKCVAHVRQH--DQLLPN 160
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNG---LLRPQSGAVLIDGEPldySRKGLleRRQRVGLVFQDpdDQLFAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 lTVRETLAFiaqmrLPRTF--SQAQRDKRVEDVIAEL-------RLRQCantrvgntyvrgVSGGERRRVSIGVQLLWNP 231
Cdd:TIGR01166 85 -DVDQDVAF-----GPLNLglSEAEVERRVREALTAVgasglreRPTHC------------LSGGEKKRVAIAGAVAMRP 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 1105531442 232 GILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLH 270
Cdd:TIGR01166 147 DVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
86-244 |
9.76e-20 |
|
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: 88.83 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 86 LGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRK-CVAHVRQHDQLLPNLTVR 164
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE---TPTSGEILLDGKDITNLPPHKrPVNTVFQNYALFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFiaQMRLPRTfSQAQRDKRVEDVIAELRLRQCANTrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:cd03300 91 ENIAF--GLRLKKL-PKAEIKERVAEALDLVQLEGYANR-----KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
89-302 |
1.05e-19 |
|
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: 88.88 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkMK--SGQIWINGQP----STPQL--VRKCVAHVRQHDQLLPN 160
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL-----LRpdSGEILVDGQDitglSEKELyeLRRRIGMLFQGGALFDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFiaQMRLPRTFSQAQRDKRVEDVIAELRLRQcantrVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:COG1127 97 LTVFENVAF--PLREHTDLSEAEIRELVLEKLELVGLPG-----AADKMPSELSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 241 SGLDSFTAHNLVTTLSRLAKGNRL--VLISlHQPRSdIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:COG1127 170 AGLDPITSAVIDELIRELRDELGLtsVVVT-HDLDS-AFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
88-308 |
1.29e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.86 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkmKSGQIWINGQ--PSTPQLVRKCVAHVRQHDQLLPNLTVRE 165
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHP---DAGSISLCGEpvPSRARHARQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAqmrlpRTF--SQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:PRK13537 100 NLLVFG-----RYFglSAAAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1105531442 244 DSFTAHNLVTTL-SRLAKGNRLVLISLHQPRSDifRLFDLVLLMTSGTPIYLGAAQQMVQyfTSIG 308
Cdd:PRK13537 170 DPQARHLMWERLrSLLARGKTILLTTHFMEEAE--RLCDRLCVIEEGRKIAEGAPHALIE--SEIG 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
88-301 |
1.52e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.66 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkMKS---GQIWINGQ--PSTPQLVRKCVAHVRQHDQLLPNLT 162
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILG------MTSpdaGKITVLGVpvPARARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFIAqmrlpRTFSQAQRDkrVEDVIAEL----RLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:PRK13536 131 VRENLLVFG-----RYFGMSTRE--IEAVIPSLlefaRLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 239 PTSGLDSFTAHNLVTTL-SRLAKGNRLVLISLHQPRSDifRLFDLVLLMTSGTPIYLGAAQQMV 301
Cdd:PRK13536 199 PTTGLDPHARHLIWERLrSLLARGKTILLTTHFMEEAE--RLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
91-295 |
2.37e-19 |
|
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: 87.16 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 91 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLV-RKCVAHVRQHDQLLPNLTVRETlaf 169
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFE---TPQSGRVLINGVDVTAAPPaDRPVSMLFQENNLFAHLTVEQN--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 170 IAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAH 249
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1105531442 250 NLVTTLSRLAKGNRL-VLISLHQPrSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:cd03298 166 EMLDLVLDLHAETKMtVLMVTHQP-EDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
88-322 |
2.45e-19 |
|
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: 87.74 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITgrghggKM---KSGQIWINGQPST---PQLVRKCVAHVRQHDQLLPNL 161
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN------RLiepTSGEIFIDGEDIReqdPVELRRKIGYVIQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:cd03295 91 TVEENIALVPKLL---KWPKEKIRERADELLALVGLDP---AEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 242 GLDSFTAHNLVTTLSRLAK--GNRLVLISlHqprsDI---FRLFDLVLLMTSGtpiylgaaqQMVQYftsiGHPCPRYSN 316
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQelGKTIVFVT-H----DIdeaFRLADRIAIMKNG---------EIVQV----GTPDEILRS 226
|
....*.
gi 1105531442 317 PADFYV 322
Cdd:cd03295 227 PANDFV 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
88-258 |
2.47e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.16 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGG--KMKSGQIWINGQPstpqlvrkcVAHVR----------QHD 155
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMI-----AGfeTPDSGRILLDGRD---------VTGLPpekrnvgmvfQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 156 QLLPNLTVRETLAF-IAQMRLPRtfsqAQRDKRVEDVIAELRLrqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGIL 234
Cdd:COG3842 87 ALFPHLTVAENVAFgLRMRGVPK----AEIRARVAELLELVGL-----EGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180
....*....|....*....|....
gi 1105531442 235 ILDEPTSGLDSFTAHNLVTTLSRL 258
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRL 181
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
89-270 |
2.52e-19 |
|
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: 92.19 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGR---ASLL----DVitgrghggkmKSGQIWINGQP---STPQLVRKCVAHVRQhDQLL 158
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKstlARLLfrfyDV----------TSGRILIDGQDirdVTQASLRAAIGIVPQ-DTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 PNLTVRETLAF------IAQMRlprtfsQAQRDKRVEDVIAelRLRQCANTRVGNtyvRGV--SGGERRRVSIGVQLLWN 230
Cdd:COG5265 444 FNDTIAYNIAYgrpdasEEEVE------AAARAAQIHDFIE--SLPDGYDTRVGE---RGLklSGGEKQRVAIARTLLKN 512
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1105531442 231 PGILILDEPTSGLDSFTAHNLVTTLSRLAKGnRLVLISLH 270
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIAH 551
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
89-272 |
3.49e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRKCVAHVRQHDQLLPNLTVRETLA 168
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL---PPAAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 169 FIAQMRlprtfsqAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSfTA 248
Cdd:PRK13539 96 FWAAFL-------GGEELDIAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALDA-AA 162
|
170 180
....*....|....*....|....*.
gi 1105531442 249 HNLVTTL--SRLAKGNrLVLISLHQP 272
Cdd:PRK13539 163 VALFAELirAHLAQGG-IVIAATHIP 187
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
88-244 |
5.02e-19 |
|
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: 86.27 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPST--PQLVRKCVAHVRQHDQLLPNLTVRE 165
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL---KPTSGRATVAGHDVVrePREVRRRIGIVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCANTRVGnTYvrgvSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:cd03265 93 NLYIHARLYgVPG----AERRERIDELLDFVGLLEAADRLVK-TY----SGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
88-289 |
5.79e-19 |
|
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: 86.10 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKMKSGQIWINGQPST---PQLVRKCVAHVRQHDQLLpNLTVR 164
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL---YKPTSGSVLLDGTDIRqldPADLRRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFiaqmrlprtFSQAQRDKRVEDV-----IAELRLRQCA--NTRVGNTYvRGVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:cd03245 96 DNITL---------GAPLADDERILRAaelagVTDFVNKHPNglDLQIGERG-RGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 238 EPTSGLDSFTAHNLVTTLSRLAKGNRLVLISlHqpRSDIFRLFDLVLLMTSG 289
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDKTLIIIT-H--RPSLLDLVDRIIVMDSG 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
77-270 |
1.37e-18 |
|
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: 83.90 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 77 SHSSQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKMKSGQIWINGQPstPQLVRKCVahvrqhdq 156
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG---DLKPQQGEITLDGVP--VSDLEKAL-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 157 llpnltvRETLAFIAQMrlPRTFsqaqrdkrvedviaelrlrqcaNTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILIL 236
Cdd:cd03247 74 -------SSLISVLNQR--PYLF----------------------DTTLRNNLGRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190
....*....|....*....|....*....|....
gi 1105531442 237 DEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLH 270
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHH 156
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
83-244 |
1.40e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 83 SCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP----STPQLVRKCVAHV---RQHD 155
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGAD---PADSGEIRLDGKPvrirSPRDAIRAGIAYVpedRKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 156 QLLPNLTVRE--TLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGI 233
Cdd:COG1129 340 GLVLDLSIREniTLASLDRLSRGGLLDRRRERALAEEYIKRLRIK----TPSPEQPVGNLSGGNQQKVVLAKWLATDPKV 415
|
170
....*....|.
gi 1105531442 234 LILDEPTSGLD 244
Cdd:COG1129 416 LILDEPTRGID 426
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
88-270 |
1.74e-18 |
|
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: 85.28 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGR---ASLL----DVItgrghggkmkSGQIWINGQPS---TPQLVRKCVAHVRQHDQL 157
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKstvVSLLerfyDPT----------SGEILLDGVDIrdlNLRWLRSQIGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 158 LPNlTVRETLAFiaqMRLPRTFSQAQRDKRV---EDVIAELRlrQCANTRVGNtyvRGV--SGGERRRVSIGVQLLWNPG 232
Cdd:cd03249 89 FDG-TIAENIRY---GKPDATDEEVEEAAKKaniHDFIMSLP--DGYDTLVGE---RGSqlSGGQKQRIAIARALLRNPK 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1105531442 233 ILILDEPTSGLDSFTAHNLVTTLSRLAKGnRLVLISLH 270
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKG-RTTIVIAH 196
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
87-302 |
1.74e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 89.64 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITgRGHggKMKSGQIWINGQPS---TPQLVRKCVAHVRQhDQLLPNLTV 163
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQ-RVF--DPQSGRILIDGTDIrtvTRASLRRNIAVVFQ-DAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETL------AFIAQMRLPRTFSQAQrdkrveDVIaeLRLRQCANTRVGNtyvRG--VSGGERRRVSIGVQLLWNPGILI 235
Cdd:PRK13657 426 EDNIrvgrpdATDEEMRAAAERAQAH------DFI--ERKPDGYDTVVGE---RGrqLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 236 LDEPTSGLDSFTAHNLVTTLSRLAKGnRLVLISLHqpRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKG-RTTFIIAH--RLSTVRNADRILVFDNGRVVESGSFDELVA 558
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
91-300 |
2.20e-18 |
|
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: 87.09 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 91 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWING---QPSTPQLV----RKCVAHVRQHDQLLPNLTV 163
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLT---RPDEGEIVLNGrtlFDSRKGIFlppeKRRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLafiaqmRLPRTFSQA-QRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:TIGR02142 93 RGNL------RYGMKRARPsERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 243 LDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQM 300
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
88-289 |
4.07e-18 |
|
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: 82.26 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKMKSGQIWINGQPST---PQLVRKCVAHVRQHDQLLPnltvr 164
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGL---LRPTSGRVRLDGADISqwdPNELGDHVGYLPQDDELFS----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 etlafiaqmrlprtfsqaqrdkrveDVIAELRLrqcantrvgntyvrgvSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:cd03246 90 -------------------------GSIAENIL----------------SGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1105531442 245 SFTAHNLVTTLSRL-AKGNRLVLISlHQPRsdIFRLFDLVLLMTSG 289
Cdd:cd03246 129 VEGERALNQAIAALkAAGATRIVIA-HRPE--TLASADRILVLEDG 171
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
88-258 |
6.56e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.33 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTpQLVRKCVAHVRQHD--------QLLP 159
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLD---TPTSGDVIFNGQPMS-KLSSAAKAELRNQKlgfiyqfhHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVRETLA---FIAQMRlprtfsQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILIL 236
Cdd:PRK11629 101 DFTALENVAmplLIGKKK------PAEINSRALEMLAAVGLEHRANHRPSE-----LSGGERQRVAIARALVNNPRLVLA 169
|
170 180
....*....|....*....|..
gi 1105531442 237 DEPTSGLDSFTAHNLVTTLSRL 258
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGEL 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
88-274 |
6.89e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.45 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRAS----LLDVITGRGhggkmksgQIWINGQPsTPQLVRKCVAHVRQHDQ------- 156
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQG--------EIWFDGQP-LHNLNRRQLLPVRHRIQvvfqdpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 157 --LLPNLTVRETLAFIAQMRLPrTFSQAQRDKRVEDVIAELRLRqcANTRvgNTYVRGVSGGERRRVSIGVQLLWNPGIL 234
Cdd:PRK15134 373 ssLNPRLNVLQIIEEGLRVHQP-TLSAAQREQQVIAVMEEVGLD--PETR--HRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1105531442 235 ILDEPTSGLDSFTAHNLVTTLSRLAKGNRL--VLIS--LHQPRS 274
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFIShdLHVVRA 491
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
88-289 |
1.23e-17 |
|
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: 82.23 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKMKSGQIWINGQP-----STPQLVRKCVAHVRQHDQLLPn 160
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIPGAPDEGEVLLDGKDiydldVDVLELRRRVGMVFQKPNPFP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFIAQMRLPRtfSQAQRDKRVEDVIAELRLRQCANTRvgnTYVRGVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:cd03260 95 GSIYDNVAYGLRLHGIK--LKEELDERVEEALRKAALWDEVKDR---LHALGLSGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1105531442 241 SGLDSFTAHNLVTTLSRLAKGNRLVLIS--LHQprsdIFRLFDLVLLMTSG 289
Cdd:cd03260 170 SALDPISTAKIEELIAELKKEYTIVIVThnMQQ----AARVADRTAFLLNG 216
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
91-270 |
1.54e-17 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 82.34 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 91 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkMKSGQIWINGQP--STPqlvRKCVAH---VRQHDQLLPNLTVRE 165
Cdd:TIGR03864 20 VSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYV---AQSGQISVAGHDlrRAP---RAALARlgvVFQQPTLDLDLSVRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCANTRVgntyvRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:TIGR03864 94 NLRYHAALHgLSR----AEARARIAELLARLGLAERADDKV-----RELNGGHRRRVEIARALLHRPALLLLDEPTVGLD 164
|
170 180
....*....|....*....|....*..
gi 1105531442 245 SFTAHNLVTTLSRLAKGNRL-VLISLH 270
Cdd:TIGR03864 165 PASRAAITAHVRALARDQGLsVLWATH 191
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
88-301 |
1.93e-17 |
|
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: 82.32 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLV----RKCVAHVRQHDQLLPNLTV 163
Cdd:TIGR04406 17 VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLV---RPDAGKILIDGQDITHLPMheraRLGIGYLPQEASIFRKLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFIAQMRlpRTFSQAQRDKRVEDVIAELRLrqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:TIGR04406 94 EENIMAVLEIR--KDLDRAEREERLEALLEEFQI-----SHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 244 DSFTAHNLVTTLSRLAKGNRLVLISLHQPRsDIFRLFDLVLLMTSGTPIYLGAAQQMV 301
Cdd:TIGR04406 167 DPIAVGDIKKIIKHLKERGIGVLITDHNVR-ETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
87-295 |
3.55e-17 |
|
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: 82.11 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGGKMK--SGQIWINGQPSTPQ------LVRKCVAHVRQH--DQ 156
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHL-----NGLLKptSGTVTIDGRDITAKkkkklkDLRKKVGLVFQFpeHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 157 LLPNlTVRETLAFIaqmrlPRTF--SQAQRDKRVEDVIA------ELRLRQCANtrvgntyvrgVSGGERRRVSI-GVqL 227
Cdd:TIGR04521 95 LFEE-TVYKDIAFG-----PKNLglSEEEAEERVKEALElvgldeEYLERSPFE----------LSGGQMRRVAIaGV-L 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 228 LWNPGILILDEPTSGLDSFTAHNLVTTLSRLAK--GNRLVLISlHQpRSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKekGLTVILVT-HS-MEDVAEYADRVIVMHKGKIVLDG 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
89-273 |
4.24e-17 |
|
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: 80.94 E-value: 4.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASL------LDVITgrghggkmkSGQIWINGQPSTP-------QLVRKCVAHVRQHD 155
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLlgllagLDRPT---------SGTVRLAGQDLFAldedaraRLRARHVGFVFQSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 156 QLLPNLTVRETLAFIAQMR-LPRTFSQAQrdkrvedviAELRlrqcantRVG-----NTYVRGVSGGERRRVSIGVQLLW 229
Cdd:COG4181 100 QLLPTLTALENVMLPLELAgRRDARARAR---------ALLE-------RVGlghrlDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1105531442 230 NPGILILDEPTSGLDSFTAHNLVTTLSRLAK--GNRLVLISlHQPR 273
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVT-HDPA 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
88-270 |
4.71e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 81.66 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP---STPQL--VRKCVAHVRQH--DQLL-P 159
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL---KPTSGEVLIKGEPikyDKKSLleVRKTVGIVFQNpdDQLFaP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 nlTVRETLAFiAQMRLprTFSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEP 239
Cdd:PRK13639 95 --TVEEDVAF-GPLNL--GLSKEEVEKRVKEALKAVGMEGFENKPPHH-----LSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 1105531442 240 TSGLDSFTAHNLVTTLSRLAKGNRLVLISLH 270
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
88-244 |
5.16e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkMKSGQIWINGQPST---PQlvRKCVAHVRQHDQLLPNLTVR 164
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFET---PDSGRIMLDGQDIThvpAE--NRHVNTVFQSYALFPHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAQM-RLPRtfsqAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:PRK09452 105 ENVAFGLRMqKTPA----AEITPRVMEALRMVQLEEFAQRKPHQ-----LSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
.
gi 1105531442 244 D 244
Cdd:PRK09452 176 D 176
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
88-306 |
5.84e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.85 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRK---CVahVRQHDQLLPNLTVR 164
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLE---KPTEGQIFIDGEDVTHRSIQQrdiCM--VFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLrqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:PRK11432 97 ENVGYGLKML---GVPKEERKQRVKEALELVDL-----AGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 245 SFTAHNLVTTLSRLAKgnRLVLISLH--QPRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQYFTS 306
Cdd:PRK11432 169 ANLRRSMREKIRELQQ--QFNITSLYvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
88-248 |
6.24e-17 |
|
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: 82.05 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP--STPQLVRKCVAHVRQHDQLLPNLTVRE 165
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLL---RPTSGTARVAGYDvvREPRKVRRSIGIVPQYASVDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCANTRVGnTYvrgvSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:TIGR01188 86 NLEMMGRLYgLPK----DEAEERAEELLELFELGEAADRPVG-TY----SGGMRRRLDIAASLIHQPDVLFLDEPTTGLD 156
|
....
gi 1105531442 245 SFTA 248
Cdd:TIGR01188 157 PRTR 160
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
88-289 |
7.13e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.83 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkMKSGQIWINGQP---STP-QLVRKCVAHV---RQHDQLLPN 160
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPG--RWEGEIFIDGKPvkiRNPqQAIAQGIAMVpedRKRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRE--TLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQC-ANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:PRK13549 356 MGVGKniTLAALDRFTGGSRIDDAAELKTILESIQRLKVKTAsPELAIAR-----LSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1105531442 238 EPTSGLDSFTAHNLVTTLSRLAK-GNRLVLISLHQPrsDIFRLFDLVLLMTSG 289
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELP--EVLGLSDRVLVMHEG 481
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
88-271 |
7.49e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.69 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkMK--SGQIWINGQPSTPQLVRKcvahvrqhdqLLPNLTVRE 165
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI-----LApdSGEVLWDGEPLDPEDRRRigylp-eergLYPKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAQMR-LPRtfSQAQRdkRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:COG4152 91 QLVYLARLKgLSK--AEAKR--RADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180
....*....|....*....|....*..
gi 1105531442 245 SFTAHNLVTTLSRLAKGNRLVLISLHQ 271
Cdd:COG4152 162 PVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
90-289 |
8.66e-17 |
|
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: 79.70 E-value: 8.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP-----STPQ--LVRKCVAHVRQHDQLLPNLT 162
Cdd:TIGR02211 23 GVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLD---NPTSGEVLFNGQSlsklsSNERakLRNKKLGFIYQFHHLLPDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFIAqmrLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:TIGR02211 100 ALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSE-----LSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1105531442 243 LDSFTAH---NLVTTLSRlAKGNRLVLISlHQPRsdIFRLFDLVLLMTSG 289
Cdd:TIGR02211 172 LDNNNAKiifDLMLELNR-ELNTSFLVVT-HDLE--LAKKLDRVLEMKDG 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
88-314 |
1.71e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITgRGHggKMKSGQIWINGQP----STPQLvRKCVAHVRQHDQLLpNLTV 163
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAW--DPQQGEILLNGQPiadySEAAL-RQAISVVSQRVHLF-SATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFIAqmrlprtfSQAQrDKRVEDVIAELRLRQCANTRVG-NTYV----RGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:PRK11160 431 RDNLLLAA--------PNAS-DEALIEVLQQVGLEKLLEDDKGlNAWLgeggRQLSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRLAKGNRLVLISlHqprsdifRL-----FDLVLLMTSGTPIYLGAAQQMVQyftsighPCPR 313
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHAQNKTVLMIT-H-------RLtgleqFDRICVMDNGQIIEQGTHQELLA-------QQGR 566
|
.
gi 1105531442 314 Y 314
Cdd:PRK11160 567 Y 567
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
89-322 |
1.86e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.61 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQ------PStpqlvRKCVAHVRQHDQLLPNLT 162
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE---DITSGDLFIGEKrmndvpPA-----ERGVGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFiaQMRLPRTfSQAQRDKRVEDVIAELRLRQCANTRVgntyvRGVSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:PRK11000 92 VAENMSF--GLKLAGA-KKEEINQRVNQVAEVLQLAHLLDRKP-----KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 243 LDSFTAHNLVTTLSRLAKgnRLvlislhqPRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQyftsIGHPCPRYSNPADFYV 322
Cdd:PRK11000 164 LDAALRVQMRIEISRLHK--RL-------GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQ----VGKPLELYHYPANRFV 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
89-272 |
2.53e-16 |
|
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: 82.41 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITG----RGhggkmksGQIWINGQP--STPQ-LVRKCVAHVRQhDQLLPNL 161
Cdd:TIGR02868 352 DGVSLDLPPGERVAILGPSGSGKSTLLATLAGlldpLQ-------GEVTLDGVPvsSLDQdEVRRRVSVCAQ-DAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFIAQMRLPRTFSQAQRDKRVEDVIAelRLRQCANTRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:TIGR02868 424 TVRENLRLARPDATDEELWAALERVGLADWLR--ALPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|.
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGNRLVLISlHQP 272
Cdd:TIGR02868 501 HLDAETADELLEDLLAALSGRTVVLIT-HHL 530
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
83-289 |
4.48e-16 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 76.70 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 83 SCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP----STPQLVRKCVAHV---RQHD 155
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLR---PPASGEITLDGKPvtrrSPRDAIRAGIAYVpedRKRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 156 QLLPNLTVRETLAFIAQMrlprtfsqaqrdkrvedviaelrlrqcantrvgntyvrgvSGGERRRVSIGVQLLWNPGILI 235
Cdd:cd03215 88 GLVLDLSVAENIALSSLL----------------------------------------SGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 236 LDEPTSGLDSFTAHNLVTTLSRLAKGNRLVL-ISlhqprSD---IFRLFDLVLLMTSG 289
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLlIS-----SEldeLLGLCDRILVMYEG 180
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
88-267 |
7.24e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 7.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKMKSGQIWINGQ---PSTP-QLVRKCVAHV---RQHDQLLPN 160
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFG---VDKRAGGEIRLNGKdisPRSPlDAVKKGMAYItesRRDNGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFIAQMRLPR------TFSQAQRDKRVEDVIAELRLRqCANTrvgNTYVRGVSGGERRRVSIGVQLLWNPGIL 234
Cdd:PRK09700 356 FSIAQNMAISRSLKDGGykgamgLFHEVDEQRTAENQRELLALK-CHSV---NQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190
....*....|....*....|....*....|...
gi 1105531442 235 ILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLI 267
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM 464
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
89-244 |
7.62e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.35 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP----STPQL--VRKCVAHVRQHDQLLPNLT 162
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLE---RPTSGSVLVDGVDltalSERELraARRKIGMIFQHFNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAF---IAQMrlprtfSQAQRDKRVEDVIAelrlrqcantRVG-----NTYVRGVSGGERRRVSIGVQLLWNPGIL 234
Cdd:COG1135 99 VAENVALpleIAGV------PKAEIRKRVAELLE----------LVGlsdkaDAYPSQLSGGQKQRVGIARALANNPKVL 162
|
170
....*....|
gi 1105531442 235 ILDEPTSGLD 244
Cdd:COG1135 163 LCDEATSALD 172
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
92-289 |
7.80e-16 |
|
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: 79.37 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 92 SFKVRSGQMLAIIGSSGCGRASLLDVITG--RGhggkmKSGQIWINGQP--STPQLV-----RKCVAHVRQHDQLLPNLT 162
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGleRP-----DSGRIRLGGEVlqDSARGIflpphRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFiAQMRLPRTFSQAQRDkrveDVIAELRL-----RqcantrvgntYVRGVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:COG4148 94 VRGNLLY-GRKRAPRAERRISFD----EVVELLGIghlldR----------RPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 238 EPTSGLDSFTAHNLVTTLSRLAKGNRL--VLISlHQPRsDIFRLFDLVLLMTSG 289
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDELDIpiLYVS-HSLD-EVARLADHVVLLEQG 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
89-273 |
9.84e-16 |
|
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: 76.24 E-value: 9.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkMKSGQIWINGQPS---TPQLVRKCvAHVRQHDQLLPNLTVRE 165
Cdd:TIGR01189 17 EGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR---PDSGEVRWNGTPLaeqRDEPHENI-LYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAqmrlpRTFSQAQRDkrVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 245
Cdd:TIGR01189 93 NLHFWA-----AIHGGAQRT--IEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1105531442 246 ---------FTAHnlvttlsrLAKGNrLVLISLHQPR 273
Cdd:TIGR01189 161 agvallaglLRAH--------LARGG-IVLLTTHQDL 188
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
88-335 |
2.14e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.34 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkmKSGQIWINGQ--PSTPQLVRKcVAHVRQHDQLLPNLTVRE 165
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---TAGQIMLDGVdlSHVPPYQRP-INMMFQSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAF-IAQMRLPRtfsqAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:PRK11607 111 NIAFgLKQDKLPK----AEIASRVNEMLGLVHMQEFAKRKPHQ-----LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 245 S----FTAHNLVTTLSRLakGNRLVLISLHQprSDIFRLFDLVLLMTSGTPIYLGAAQQMVQyftsigHPCPRYSnpADF 320
Cdd:PRK11607 182 KklrdRMQLEVVDILERV--GVTCVMVTHDQ--EEAMTMAGRIAIMNRGKFVQIGEPEEIYE------HPTTRYS--AEF 249
|
250
....*....|....*
gi 1105531442 321 YVDLTSIDRRSKERE 335
Cdd:PRK11607 250 IGSVNVFEGVLKERQ 264
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
79-290 |
2.15e-15 |
|
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: 75.20 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 79 SSQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkMKSGQIWINGQpstpqlvrkcVAHVRQHDQLL 158
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---KLSGSVSVPGS----------IAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 pNLTVRETLAFIAQMrlprtfsqaqRDKRVEDVIaelrlRQCA------------NTRVGntyVRGV--SGGERRRVSIG 224
Cdd:cd03250 79 -NGTIRENILFGKPF----------DEERYEKVI-----KACAlepdleilpdgdLTEIG---EKGInlSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 225 VQLLWNPGILILDEPTSGLDSFTAHNLVTT-LSRLAKGNRLVLISLHQPrsDIFRLFDLVLLMTSGT 290
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQL--QLLPHADQIVVLDNGR 204
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
88-271 |
2.62e-15 |
|
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: 79.38 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkMKSGQIWINGQP---STPQLVRKCVAHVRQHDQLLpNLTVR 164
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE---PDSGQILLDGHDladYTLASLRRQVALVSQDVVLF-NDTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAqmrlPRTFSQAqrdkRVEDVIAELRLRQCAN-------TRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:TIGR02203 424 NNIAYGR----TEQADRA----EIERALAAAYAQDFVDklplgldTPIGENGVL-LSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190
....*....|....*....|....*....|....
gi 1105531442 238 EPTSGLDSFTAHNLVTTLSRLAKGnRLVLISLHQ 271
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLMQG-RTTLVIAHR 527
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
88-290 |
2.74e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRKcvAH------VRQHDQLLPNL 161
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIV---PPDSGTLEIGGNPCARLTPAK--AHqlgiylVPQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFiaqmRLPRTfsqAQRDKRVEDVIAELRLRQCANTRVGNTYVrgvsgGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:PRK15439 102 SVKENILF----GLPKR---QASMQKMKQLLAALGCQLDLDSSAGSLEV-----ADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1105531442 242 GLDSFTAHNLVTTL-SRLAKGNRLVLISLHQPrsDIFRLFDLVLLMTSGT 290
Cdd:PRK15439 170 SLTPAETERLFSRIrELLAQGVGIVFISHKLP--EIRQLADRISVMRDGT 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
90-294 |
3.67e-15 |
|
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: 79.67 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFkvRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQL--VRKCVAHVRQHDQLLPNLTVRETL 167
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLL---PPTSGTVLVGGKDIETNLdaVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMRlPRTFSQAQRDkrVEDVIAELRLRQCANTRVgntyvRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 247
Cdd:TIGR01257 1025 LFYAQLK-GRSWEEAQLE--MEAMLEDTGLHHKRNEEA-----QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1105531442 248 AHNLVTTLSRLAKGNRLVLISLHQPRSDIfrLFDLVLLMT------SGTPIYL 294
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGRTIIMSTHHMDEADL--LGDRIAIISqgrlycSGTPLFL 1147
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
90-245 |
5.37e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.05 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkMKSGQIWINGQPSTPQLVR-KCVAHVRQHDQLLPNLTVRETLA 168
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEH---QTSGHIRFHGTDVSRLHARdRKVGFVFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 169 FIAQMrLPR--TFSQAQRDKRVEDVIAELRLrqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 245
Cdd:PRK10851 97 FGLTV-LPRreRPNAAAIKAKVTQLLEMVQL-----AHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
88-244 |
5.85e-15 |
|
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: 76.25 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCG-----RAsLLDVITGRGHggkmKSGQIWINGQPSTpQLVRKCVAHVRQHD-----Q- 156
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGkstlaRA-ILGLLPPPGI----TSGEILFDGEDLL-KLSEKELRKIRGREiqmifQd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 157 ----LLPNLTVRETLAFIaqMRLPRTFSQAQRDKRVEDVIAELRLRQcANTRVGNtYVRGVSGGERRRVSIGVQLLWNPG 232
Cdd:COG0444 95 pmtsLNPVMTVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLPD-PERRLDR-YPHELSGGMRQRVMIARALALEPK 170
|
170
....*....|..
gi 1105531442 233 ILILDEPTSGLD 244
Cdd:COG0444 171 LLIADEPTTALD 182
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
86-322 |
6.23e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.38 E-value: 6.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 86 LGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKmksGQIWING-------QPSTPQLVRKCVAHVRQHDQLL 158
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR---GQVLIDGvdiakisDAELREVRRKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 PNLTVRETLAFiaQMRLPRTFSQAQRDKRVEdviaelRLRQCANTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:PRK10070 119 PHMTVLDNTAF--GMELAGINAEERREKALD------ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGtpiylgaaqQMVQyftsIGHPCPRYSNPA 318
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG---------EVVQ----VGTPDEILNNPA 257
|
....
gi 1105531442 319 DFYV 322
Cdd:PRK10070 258 NDYV 261
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
91-271 |
6.80e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.79 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 91 LSFKVRSGQMLAIIGSSGCGRASLLDVIT--GRGHGGKMKSGQIWINGQPSTPQ---LVRKC---VAHVRQHDQLLPNLT 162
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINllEQPEAGTIRVGDITIDTARSLSQqkgLIRQLrqhVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLafiaqMRLPRTFSQAQRDKrvedviAELRLRQCAnTRVG-----NTYVRGVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:PRK11264 102 VLENI-----IEGPVIVKGEPKEE------ATARARELL-AKVGlagkeTSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190
....*....|....*....|....*....|....
gi 1105531442 238 EPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQ 271
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
80-302 |
6.90e-15 |
|
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: 74.57 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 80 SQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPS---TPQLVRKCVAHVRQhDQ 156
Cdd:cd03254 11 SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFY---DPQKGQILIDGIDIrdiSRKSLRSMIGVVLQ-DT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 157 LLPNLTVRETLAFiaqmrlprtFSQAQRDKRVEDVIAELRLRQCANTRVG--NTYVR----GVSGGERRRVSIGVQLLWN 230
Cdd:cd03254 87 FLFSGTIMENIRL---------GRPNATDEEVIEAAKEAGAHDFIMKLPNgyDTVLGenggNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 231 PGILILDEPTSGLDSFTAHNLVTTLSRLAKGnRLVLISLHqpRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKG-RTSIIIAH--RLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
88-300 |
7.06e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.65 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP---STPQL--VRKCVAHVRQH-DQLLPNL 161
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL---KPSSGRILFDGKPidySRKGLmkLRESVGMVFQDpDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAF-IAQMRLPRTFSQaqrdKRVEDVIAelrlrqcantRVGNTYVRG-----VSGGERRRVSIGVQLLWNPGILI 235
Cdd:PRK13636 99 SVYQDVSFgAVNLKLPEDEVR----KRVDNALK----------RTGIEHLKDkpthcLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 236 LDEPTSGLDSFTAHNLVTTLSRLAKGNRL-VLISLHQprSDIFRLF-DLVLLMTSGTPIYLGAAQQM 300
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELGLtIIIATHD--IDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
88-302 |
8.58e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.83 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP-STPQL--VRKCVAHVRQHDQLLPNlTVR 164
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF---DVSEGDIRFHDIPlTKLQLdsWRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAQMRLPRTFSQAQRDKRVEDVIaeLRLRQCANTRVGNtyvRGV--SGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:PRK10789 407 NNIALGRPDATQQEIEHVARLASVHDDI--LRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1105531442 243 LDSFTAHNLVTTLSRLAKGnRLVLISLHqprsdifRLFDL-----VLLMTSGTPIYLGAAQQMVQ 302
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEG-RTVIISAH-------RLSALteaseILVMQHGHIAQRGNHDQLAQ 538
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
86-244 |
9.47e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 86 LGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RghggKMKSGQIWINGQP----STPQLVRKCVAHV---RQHDQL 157
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGlR----PPASGSIRLDGEDitglSPRERRRLGVAYIpedRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 158 LPNLTVRETLAFIAQMRLPRT----FSQAQRDKRVEDVIAELRLRqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGI 233
Cdd:COG3845 348 VPDMSVAENLILGRYRRPPFSrggfLDRKAIRAFAEELIEEFDVR----TPGPDTPARSLSGGNQQKVILARELSRDPKL 423
|
170
....*....|.
gi 1105531442 234 LILDEPTSGLD 244
Cdd:COG3845 424 LIAAQPTRGLD 434
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
86-299 |
1.02e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.64 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 86 LGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKMKSGQIWINGQPSTpQLVRKCVAHVRQHDQLLPNLTV 163
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfyKPTGGTILLRGQHIEGLPGH-QIARMGVVRTFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLaFIAQMRLPRT-----------FSQAQRDK--RVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWN 230
Cdd:PRK11300 98 IENL-LVAQHQQLKTglfsgllktpaFRRAESEAldRAATWLERVGLLEHANRQAGN-----LAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 231 PGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQ 299
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
88-343 |
1.57e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 74.70 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLV-----RKCVAHVRQHD--QLLPN 160
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL---KPTSGKIIIDGVDITDKKVklsdiRKKVGLVFQYPeyQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 lTVRETLAFiaqmrlprtfsqAQRDKRVEDVIAELRLRQCANTrVGNTYVR-------GVSGGERRRVSIGVQLLWNPGI 233
Cdd:PRK13637 100 -TIEKDIAF------------GPINLGLSEEEIENRVKRAMNI-VGLDYEDykdkspfELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 234 LILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQM---VQYFTSIGHP 310
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVfkeVETLESIGLA 245
|
250 260 270
....*....|....*....|....*....|....*....
gi 1105531442 311 CPRysnpadfyvdLTSIDRRSKER------EVATVEKAQ 343
Cdd:PRK13637 246 VPQ----------VTYLVRKLRKKgfnipdDIFTIEEAK 274
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
90-313 |
1.96e-14 |
|
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: 74.07 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTpQLVRKCVAHVRQHDQLL---------PN 160
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLE---KPAQGTVSFRGQDLY-QLDRKQRRAFRRDVQLVfqdspsavnPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAfiAQMRLPRTFSQAQRDKRVEDVIAELRLRqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:TIGR02769 105 MTVRQIIG--EPLRHLTSLDESEQKARIAELLDMVGLR----SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1105531442 241 SGLDSFTAHNLVTTLSRL--AKGNRLVLISlHQPRSdIFRLFDLVLLMTSGTPIylgaAQQMVQYFTSIGHPCPR 313
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLqqAFGTAYLFIT-HDLRL-VQSFCQRVAVMDKGQIV----EECDVAQLLSFKHPAGR 247
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
88-285 |
2.32e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.88 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkmksgqiwiNGQPSTPQLVRKC---VAHVRQH---DQLLPnL 161
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAG--------------VLRPTSGTVRRAGgarVAYVPQRsevPDSLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRE--TLAFIAQMRLPRTFSQAQRdKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEP 239
Cdd:NF040873 73 TVRDlvAMGRWARRGLWRRLTRDDR-AAVDDALERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1105531442 240 TSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLL 285
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDL-ELVRRADPCVLL 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
88-291 |
2.85e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.12 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITgrgHGGKMKSGQIWINGQP---STPQLVRKCVAHVRQHdQLLP-NLTV 163
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFA---RLLTPQSGTVFLGDKPismLSSRQLARRLALLPQH-HLTPeGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFIAQMRLPRTFSQAQRDK-RVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:PRK11231 94 RELVAYGRSPWLSLWGRLSAEDNaRVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 243 LDSFTAHNLVTTLSRLAKGNRLVLISLHqprsDI---FRLFD-LVLL-----MTSGTP 291
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQGKTVVTVLH----DLnqaSRYCDhLVVLanghvMAQGTP 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
92-244 |
6.05e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 73.23 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 92 SFKVRSGQMLAIIGSSGCGRASL------LDVITgrghggkmkSGQIWINGQPSTpQLVRKCVAHVRQHDQ--------- 156
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLgrlllrLEEPT---------SGEILFDGQDIT-GLSGRELRPLRRRMQmvfqdpyas 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 157 LLPNLTVRETLAfiAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRvgntYVRGVSGGERRRVSIGVQLLWNPGILIL 236
Cdd:COG4608 108 LNPRMTVGDIIA--EPLRIHGLASKAERRERVAELLELVGLRPEHADR----YPHEFSGGQRQRIGIARALALNPKLIVC 181
|
....*...
gi 1105531442 237 DEPTSGLD 244
Cdd:COG4608 182 DEPVSALD 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
87-244 |
6.11e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKMKSGQIWINGQ---PSTPQ-LVRKCVAHV---RQHDQLLP 159
Cdd:PRK10762 267 GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG---ALPRTSGYVTLDGHevvTRSPQdGLANGIVYIsedRKRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVRETLAFIAQMRLPRTFSQAQRDKR---VEDVIAELRLRQ-CANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILI 235
Cdd:PRK10762 344 GMSVKENMSLTALRYFSRAGGSLKHADEqqaVSDFIRLFNIKTpSMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLI 418
|
....*....
gi 1105531442 236 LDEPTSGLD 244
Cdd:PRK10762 419 LDEPTRGVD 427
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
90-271 |
6.24e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.05 E-value: 6.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLL------DVITGrghgGKMKSGQIWINGQPSTPQLVRKCVAHVRQHDQLLPNLTV 163
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLrcinklEEITS----GDLIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFiAQMRLpRTFSQAQRDKRVEDVIAELRLRQCANTrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:PRK09493 95 LENVMF-GPLRV-RGASKEEAEKQARELLAKVGLAERAHH-----YPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180
....*....|....*....|....*...
gi 1105531442 244 DSFTAHNLVTTLSRLAKGNRLVLISLHQ 271
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
88-289 |
7.44e-14 |
|
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: 74.48 E-value: 7.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrGHGGKMKsGQIWINGQP----STPQLVRKCVAHV---RQHDQLLPN 160
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFE-GNVFINGKPvdirNPAQAIRAGIAMVpedRKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRE--TLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:TIGR02633 354 LGVGKniTLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVK----TASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 239 PTSGLD---SFTAHNLVTTLSRlaKGNRLVLISLHQPrsDIFRLFDLVLLMTSG 289
Cdd:TIGR02633 430 PTRGVDvgaKYEIYKLINQLAQ--EGVAIIVVSSELA--EVLGLSDRVLVIGEG 479
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
88-302 |
8.04e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.17 E-value: 8.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR-----GHGGKMKSGQIWINGQP----STPQLVRKCVAHVRQHDQLL 158
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggAPRGARVTGDVTLNGEPlaaiDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 PnLTVRETLAFiaqMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNTyVRGVSGGERRRVSIGVQL--LW------- 229
Cdd:PRK13547 97 A-FSAREIVLL---GRYPHARRAGALTHRDGEIAWQALALAGATALVGRD-VTTLSGGELARVQFARVLaqLWpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 230 NPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRL-VLISLHQPRSDIfRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPADVLT 244
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
88-244 |
9.28e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 71.21 E-value: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTP----QLVRKCVAHVRQHDQLLPNLTV 163
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV---KPDSGRIFLDGEDITHlpmhKRARLGIGYLPQEASIFRKLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLrqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:COG1137 96 EDNILAVLELR---KLSKKEREERLEELLEEFGI-----THLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGV 167
|
.
gi 1105531442 244 D 244
Cdd:COG1137 168 D 168
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
88-273 |
9.81e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.46 E-value: 9.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPST----PQLVRKCVAHVRQHDQLLPNLTV 163
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIV---PRDAGNIIIDDEDISllplHARARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFIAQMRlpRTFSQAQRDKRVEDVIAELRLrqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:PRK10895 96 YDNLMAVLQIR--DDLSAEQREDRANELMEEFHI-----EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190
....*....|....*....|....*....|
gi 1105531442 244 DSFTAHNLVTTLSRLAKGNRLVLISLHQPR 273
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVR 198
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
92-244 |
9.93e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 72.69 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 92 SFKVRSGQMLAIIGSSGCGRASLLDVITgrghggkM----KSGQIWINGQ------PSTPQLVRKCVAHVRQ--HDQLLP 159
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLT-------MietpTGGELYYQGQdllkadPEAQKLLRQKIQIVFQnpYGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVRETLAfiAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRvgntYVRGVSGGERRRVSIGVQLLWNPGILILDEP 239
Cdd:PRK11308 108 RKKVGQILE--EPLLINTSLSAAERREKALAMMAKVGLRPEHYDR----YPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
....*
gi 1105531442 240 TSGLD 244
Cdd:PRK11308 182 VSALD 186
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
90-244 |
9.93e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 71.20 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVI----TGRghggkmkSGQIWINGQ---------PSTPQLVRKCVAHVRQHDQ 156
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLnlleTPD-------SGQLNIAGHqfdfsqkpsEKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 157 LLPNLTVRETLaFIAQMR-LPRTFSQAQrdKRVEDVIAELRLRQCANTrvgntYVRGVSGGERRRVSIGVQLLWNPGILI 235
Cdd:COG4161 93 LWPHLTVMENL-IEAPCKvLGLSKEQAR--EKAMKLLARLRLTDKADR-----FPLHLSGGQQQRVAIARALMMEPQVLL 164
|
....*....
gi 1105531442 236 LDEPTSGLD 244
Cdd:COG4161 165 FDEPTAALD 173
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
90-283 |
1.00e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGkmkSGQIWINGQP----STPQLVRKCVAHVRQHDQLLPNLTVRE 165
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD---AGSILIDGQEmrfaSTTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLaFIAQmrLPRTFSQAQRDKRVEDVIAELRlrqcantRVG-----NTYVRGVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:PRK11288 99 NL-YLGQ--LPHKGGIVNRRLLNYEAREQLE-------HLGvdidpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1105531442 241 SGLDSFTAHNLVTTLSRLAKGNRLVLISLHqpRSD-IFRLFDLV 283
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSH--RMEeIFALCDAI 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
92-302 |
1.08e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.15 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 92 SFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkmKSGQIWINGQP--STPQlVRKCVAHVRQHDQLLPNLTVRETLAF 169
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTP---ASGSLTLNGQDhtTTPP-SRRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 170 IAQ--MRLprtfSQAQRDKrVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 247
Cdd:PRK10771 95 GLNpgLKL----NAAQREK-LHAIARQMGIEDLLARLPGQ-----LSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1105531442 248 AHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:PRK10771 165 RQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
88-290 |
1.10e-13 |
|
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: 71.14 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRgHGGKMKSGQIWINGQP----STPQLVRKCVAHVRQHDQLLPNLTV 163
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH-PSYEVTSGTILFKGQDllelEPDERARAGLFLAFQYPEEIPGVSN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 REtlaFIaqmrlpRTFSQAQRDKRVEDVIAEL-----------RLRQCAN--TRVGNTyvrGVSGGERRRVSIGVQLLWN 230
Cdd:TIGR01978 95 LE---FL------RSALNARRSARGEEPLDLLdfekllkeklaLLDMDEEflNRSVNE---GFSGGEKKRNEILQMALLE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 231 PGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRsdIFRLF--DLVLLMTSGT 290
Cdd:TIGR01978 163 PKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR--LLNYIkpDYVHVLLDGR 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
91-302 |
1.25e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.36 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 91 LSFKVRSGQMLAIIGSSGCGRASLLDVItGRGHggKMKSGQIWINGQP----STPQLVRKcVAHVRQHDQLLPNLTVREt 166
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQ--PPSEGEILLDAQPleswSSKAFARK-VAYLPQQLPAAEGMTVRE- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 laFIAQMRLP-----RTFSQAQRdKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:PRK10575 105 --LVAIGRYPwhgalGRFGAADR-EKVEEAISLVGLKPLAHRLVDS-----LSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 242 GLDsfTAH--NLVTTLSRLAKGNRLVLIS-LHqprsDI---FRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:PRK10575 177 ALD--IAHqvDVLALVHRLSQERGLTVIAvLH----DInmaARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
89-244 |
1.25e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkMK--SGQIWINGQpstpqlVRkcVAHVRQHDQLLPNLTVRET 166
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGE-----LEpdSGEVSIPKG------LR--IGYLPQEPPLDDDLTVLDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 L--AFIAQMRLPRTFSQAQR---------------------------DKRVEDVIAELRLrqcaNTRVGNTYVRGVSGGE 217
Cdd:COG0488 82 VldGDAELRALEAELEELEAklaepdedlerlaelqeefealggweaEARAEEILSGLGF----PEEDLDRPVSELSGGW 157
|
170 180
....*....|....*....|....*..
gi 1105531442 218 RRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
88-302 |
2.76e-13 |
|
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: 72.86 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkmksgqIWingQPStpqlvRKCV----AHVRQHD-------- 155
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVG-----------VW---PPT-----AGSVrldgADLSQWDreelgrhi 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 156 -------QLLPNlTVRETlafIAqmrlpRtFSQAQRDKRVE--------DVIaeLRLRQCANTRVGntyVRGV--SGGER 218
Cdd:COG4618 409 gylpqdvELFDG-TIAEN---IA-----R-FGDADPEKVVAaaklagvhEMI--LRLPDGYDTRIG---EGGArlSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 219 RRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRsdIFRLFDLVLLMTSGTPIYLGAAQ 298
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDGRVQAFGPRD 551
|
....
gi 1105531442 299 QMVQ 302
Cdd:COG4618 552 EVLA 555
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
95-299 |
4.15e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 95 VRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMKSGQIWINGQpsTPQL-------VRKCVAH---VRQHDQLLPNLTVR 164
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGR--TVQRegrlardIRKSRANtgyIFQQFNLVNRLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAQMRLP------RTFSQAQRDKRVEdviaelrlrqcANTRVGNTY-----VRGVSGGERRRVSIGVQLLWNPGI 233
Cdd:PRK09984 105 ENVLIGALGSTPfwrtcfSWFTREQKQRALQ-----------ALTRVGMVHfahqrVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 234 LILDEPTSGLDSFTAHNLVTTLSRLAKGNRL-VLISLHQPRSDIfRLFDLVLLMTSGTPIYLGAAQQ 299
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQVDYAL-RYCERIVALRQGHVFYDGSSQQ 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
88-306 |
4.38e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.69 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKMK-SGQIWING----QPSTPQLvRKCVAHVRQHDQLLPN 160
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRliEIYDSKIKvDGKVLYFGkdifQIDAIKL-RKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFIAQmrlprtfSQAQRDKR-----VEDVIAELRLRQCANTRVgNTYVRGVSGGERRRVSIGVQLLWNPGILI 235
Cdd:PRK14246 105 LSIYDNIAYPLK-------SHGIKEKReikkiVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1105531442 236 LDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISlHQPRSdIFRLFDLVLLMTSGTPIYLGAAQQMvqyFTS 306
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQQ-VARVADYVAFLYNGELVEWGSSNEI---FTS 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
76-272 |
4.92e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.45 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 76 RSHSSQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrGHGGKMKSGQIWINGQ-------PSTPQLVRKCV 148
Cdd:PRK10535 12 RSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL---GCLDKPTSGTYRVAGQdvatldaDALAQLRREHF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 149 AHVRQHDQLLPNLTVRETLafiaqmRLPRTFSQAQRDKRVEDVIAELrlrqcanTRVG-----NTYVRGVSGGERRRVSI 223
Cdd:PRK10535 89 GFIFQRYHLLSHLTAAQNV------EVPAVYAGLERKQRLLRAQELL-------QRLGledrvEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1105531442 224 GVQLLwNPGILIL-DEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQP 272
Cdd:PRK10535 156 ARALM-NGGQVILaDEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
89-271 |
5.14e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.60 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP----STPQLV--RKCVAHVRQHDQLLPNLT 162
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE---RPTSGRVLVDGQDltalSEKELRkaRRQIGMIFQHFNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFiaQMRLPRTfSQAQRDKRVEDVIAelrlrqcantRVG-----NTYVRGVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:PRK11153 99 VFDNVAL--PLELAGT-PKAEIKARVTELLE----------LVGlsdkaDRYPAQLSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 1105531442 238 EPTSGLDSFTAHNLvttLSRLAKGNR-----LVLISlHQ 271
Cdd:PRK11153 166 EATSALDPATTRSI---LELLKDINRelgltIVLIT-HE 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
91-272 |
5.72e-13 |
|
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: 68.29 E-value: 5.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 91 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP---STPQLVRKCvAHVRQHDQLLPNLTVRETL 167
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLS---PPLAGRVLLNGGPldfQRDSIARGL-LYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFiaqmrlprtFSQAQRDKRVEDVIAELRLRQcantrVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 247
Cdd:cd03231 95 RF---------WHADHSDEQVEEALARVGLNG-----FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....*
gi 1105531442 248 AHNLVTTLSRLAKGNRLVLISLHQP 272
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
89-268 |
7.73e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.21 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLldvitgrghggkMK---------SGQIWINGQP---STPQLVRKC-VAHVRQHD 155
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTL------------MKilyglyqpdSGEILIDGKPvriRSPRDAIALgIGMVHQHF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 156 QLLPNLTVRETLAfIAQMRLPRTF-SQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGIL 234
Cdd:COG3845 90 MLVPNLTVAENIV-LGLEPTKGGRlDRKAARARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEILKALYRGARIL 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1105531442 235 ILDEPTSGLdsfT---AHNLVTTLSRLAK-GNRLVLIS 268
Cdd:COG3845 164 ILDEPTAVL---TpqeADELFEILRRLAAeGKSIIFIT 198
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
88-244 |
8.24e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 8.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkmKSGQIWINGQpsTPQLVRKcvAHVR-------QHDQLLPN 160
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVP---TSGEVRVLGY--VPFKRRK--EFARrigvvfgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFIAQM-RLPRtfsqAQRDKRVEDVIAELRLRQCANTRVgntyvRGVSGGERRRVSIGVQLLWNPGILILDEP 239
Cdd:COG4586 111 LPAIDSFRLLKAIyRIPD----AEYKKRLDELVELLDLGELLDTPV-----RQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
....*
gi 1105531442 240 TSGLD 244
Cdd:COG4586 182 TIGLD 186
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
90-244 |
8.77e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.50 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggKM-KSGQIWINGQ---------PSTPQLVRKCVAHVRQHDQLLP 159
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLL----EMpRSGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVRETLafI-AQMRLpRTFSQAQRDKRVEDVIAELRLRQCANTrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:PRK11124 96 HLTVQQNL--IeAPCRV-LGLSKDQALARAEKLLERLRLKPYADR-----FPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
....*.
gi 1105531442 239 PTSGLD 244
Cdd:PRK11124 168 PTAALD 173
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
88-302 |
1.59e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.94 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVIT--------GRGHGGKMKSGQIwINGQPSTPQLVRKCVAHVRQHDQLLP 159
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelneeARVEGEVRLFGRN-IYSPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVRETLAFIAQM-RLPRtfSQAQRDKRVEDVIAELRLRQCANTRVgNTYVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:PRK14267 99 HLTIYDNVAIGVKLnGLVK--SKKELDERVEWALKKAALWDEVKDRL-NDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRLAKGNRLVLISlHQPrSDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVT-HSP-AQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
88-244 |
1.67e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.49 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQ------PSTpqlvRKCvAHVRQHDQLLPNL 161
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLE---RITSGEIWIGGRvvnelePAD----RDI-AMVFQNYALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAF---IaqmrlpRTFSQAQRDKRVEDV--IAEL------RLRQcantrvgntyvrgVSGGERRRVSIGVQLLWN 230
Cdd:PRK11650 92 SVRENMAYglkI------RGMPKAEIEERVAEAarILELeplldrKPRE-------------LSGGQRQRVAMGRAIVRE 152
|
170
....*....|....
gi 1105531442 231 PGILILDEPTSGLD 244
Cdd:PRK11650 153 PAVFLFDEPLSNLD 166
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
90-244 |
1.75e-12 |
|
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: 70.10 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCG-----RAsLLDVITGrghggkmkSGQIWINGQPSTpQLVRKCVAHVRQHDQ-------- 156
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGkstlgLA-LLRLIPS--------EGEIRFDGQDLD-GLSRRALRPLRRRMQvvfqdpfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 157 -LLPNLTVRETLA---FIAQMRLPRtfsqAQRDKRVEDVIAELRLRqcANTRvgNTYVRGVSGGERRRVSIGVQLLWNPG 232
Cdd:COG4172 374 sLSPRMTVGQIIAeglRVHGPGLSA----AERRARVAEALEEVGLD--PAAR--HRYPHEFSGGQRQRIAIARALILEPK 445
|
170
....*....|..
gi 1105531442 233 ILILDEPTSGLD 244
Cdd:COG4172 446 LLVLDEPTSALD 457
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
88-300 |
1.78e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.29 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQ---LVRKCVAHVRQH--DQLLpNLT 162
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL---KPTSGSVLIRGEPITKEnirEVRKFVGLVFQNpdDQIF-SPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAF-IAQMRLprtfSQAQRDKRVEDVIAELRLRQCaNTRVGNTyvrgVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:PRK13652 96 VEQDIAFgPINLGL----DEETVAHRVSSALHMLGLEEL-RDRVPHH----LSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGNRL-VLISLHQpRSDIFRLFDLVLLMTSGTPIYLGAAQQM 300
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMtVIFSTHQ-LDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
44-289 |
1.80e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.22 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 44 SNTLEVRDLTYqvdiasqvpwfeqlaqfkipwRSHSSQDSCELgiRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGh 123
Cdd:PRK13650 2 SNIIEVKNLTF---------------------KYKEDQEKYTL--NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 124 ggKMKSGQIWINGQPSTPQLV---RKCVAHVRQH-DQLLPNLTVRETLAF-IAQMRLPRTFSQAQRDKRVEDV-IAELRL 197
Cdd:PRK13650 58 --EAESGQIIIDGDLLTEENVwdiRHKIGMVFQNpDNQFVGATVEDDVAFgLENKGIPHEEMKERVNEALELVgMQDFKE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 198 RQCANtrvgntyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIf 277
Cdd:PRK13650 136 REPAR----------LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV- 204
|
250
....*....|..
gi 1105531442 278 RLFDLVLLMTSG 289
Cdd:PRK13650 205 ALSDRVLVMKNG 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
85-270 |
1.97e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.05 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 85 ELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITgRGHggKMKSGQIWING---QPSTPQLVRKCVAHVRQHDQLLpNL 161
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT-RFY--DIDEGEILLDGhdlRDYTLASLRNQVALVSQNVHLF-ND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFIAQMRLPR-TFSQAQRDKRVEDVIAelRLRQCANTRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:PRK11176 432 TIANNIAYARTEQYSReQIEEAARMAYAMDFIN--KMDNGLDTVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190
....*....|....*....|....*....|
gi 1105531442 241 SGLDSFTAHNLVTTLSRLAKgNRLVLISLH 270
Cdd:PRK11176 509 SALDTESERAIQAALDELQK-NRTSLVIAH 537
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
75-244 |
2.04e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.82 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 75 WRSHSSQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMkSGQIWINGQP----STPQLVRKCVAH 150
Cdd:NF040905 263 WTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNI-SGTVFKDGKEvdvsTVSDAIDAGLAY 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 151 V---RQHDQLLPNLTVRE--TLAfiaqmRLPRTFSQAQRDKRVEDVIAElRLRQCANTRVGNTY--VRGVSGGERRRVSI 223
Cdd:NF040905 342 VtedRKGYGLNLIDDIKRniTLA-----NLGKVSRRGVIDENEEIKVAE-EYRKKMNIKTPSVFqkVGNLSGGNQQKVVL 415
|
170 180
....*....|....*....|.
gi 1105531442 224 GVQLLWNPGILILDEPTSGLD 244
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGID 436
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
88-258 |
2.05e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP----STPQLVRKCVAHVRQHDQLLPNLTV 163
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDP---RATSGRIVFDGKDitdwQTAKIMREAVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLA---FIAQmrlpRTFSQaQRDKRVEDVIAELRLRQcaNTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:PRK11614 98 EENLAmggFFAE----RDQFQ-ERIKWVYELFPRLHERR--IQRAGT-----MSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170
....*....|....*...
gi 1105531442 241 SGLDSFTAHNLVTTLSRL 258
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQL 183
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
70-270 |
2.07e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 70 QFKIPWRS-HSSqdscelgIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkMKSGQIWINGQPSTPQLVRKCV 148
Cdd:PRK15056 11 DVTVTWRNgHTA-------LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVR---LASGKISILGQPTRQALQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 149 AHVRQHDQ-------LLPNLTVRETLAFIAQMRLPRTFSQAQRDKRVEDV-IAELRLRQCANtrvgntyvrgVSGGERRR 220
Cdd:PRK15056 81 AYVPQSEEvdwsfpvLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVdMVEFRHRQIGE----------LSGGQKKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1105531442 221 VSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLH 270
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
95-273 |
2.27e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 95 VRSGQMLAIIGSSGCGRASLLDVITGRGHGGkmkSGQIWINGQPST-------PQLVRKCVAHVRQHDQLLPNLTVRETL 167
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGS---SGEVSLVGQPLHqmdeearAKLRAKHVGFVFQSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAqmrLPRTFSQAQRDKRVEDVIAELRLRQcantRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 247
Cdd:PRK10584 110 ELPA---LLRGESSRQSRNGAKALLEQLGLGK----RLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*...
gi 1105531442 248 AHNLVTTLSRLAK--GNRLVLISlHQPR 273
Cdd:PRK10584 182 GDKIADLLFSLNRehGTTLILVT-HDLQ 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
87-292 |
2.46e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 67.93 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQL-------VRKCVAHVRQ--HDQL 157
Cdd:PRK13641 22 GLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALL---KPSSGTITIAGYHITPETgnknlkkLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 158 LPNlTVRETLAFiaqmrLPRTFSqAQRDKRVEDVIAELRlRQCANTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:PRK13641 99 FEN-TVLKDVEF-----GPKNFG-FSEDEAKEKALKWLK-KVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1105531442 238 EPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSGTPI 292
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGKLI 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
88-271 |
2.85e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.30 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITgrgHGGKMKSGQIWINGQ----------------PSTPQLVRKCVAHV 151
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCIN---FLEKPSEGSIVVNGQtinlvrdkdgqlkvadKNQLRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 152 RQHDQLLPNLTVRETLafiaqMRLPRT---FSQAQRDKRVEDVIAELRLRQCANTRvgntYVRGVSGGERRRVSIGVQLL 228
Cdd:PRK10619 98 FQHFNLWSHMTVLENV-----MEAPIQvlgLSKQEARERAVKYLAKVGIDERAQGK----YPVHLSGGQQQRVSIARALA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1105531442 229 WNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQ 271
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
90-260 |
3.00e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.66 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPST---PQLVRKCVAHVRQHDQLLPNlTVRET 166
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLI---SPTSGTLLFEGEDIStlkPEIYRQQVSYCAQTPTLFGD-TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 LAFIAQMRlprtfSQAQRDKRVEDVIAELRLRQcantRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 246
Cdd:PRK10247 101 LIFPWQIR-----NQQPDPAIFLDDLERFALPD----TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170
....*....|....
gi 1105531442 247 TAHNLVTTLSRLAK 260
Cdd:PRK10247 172 NKHNVNEIIHRYVR 185
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
88-271 |
3.43e-12 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 66.20 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggKMKSGQIWINGQPSTPQLV------RKCVAHVRQHDQLLpNL 161
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ--TLEGKVHWSNKNESEPSFEatrsrnRYSVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFIAQMrlprtfsQAQRDKRVEDVIA---ELRLRQCAN-TRVGNtyvRGV--SGGERRRVSIGVQLLWNPGILI 235
Cdd:cd03290 94 TVEENITFGSPF-------NKQRYKAVTDACSlqpDIDLLPFGDqTEIGE---RGInlSGGQRQRICVARALYQNTNIVF 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1105531442 236 LDEPTSGLDSFTAHNLVTT--LSRLAKGNRLVLISLHQ 271
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK 201
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
88-310 |
3.85e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRA----SLLDVItgRGHGGKMKSGQIWIN---------GQPSTPQLvrkcvAHVRQH 154
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL--EQAGGLVQCDKMLLRrrsrqvielSEQSAAQM-----RHVRGA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 155 D----------QLLPNLTVRETLAfiAQMRLPRTFSQAQRDKRVEDVIAELRLRQcANTRVGNtYVRGVSGGERRRVSIG 224
Cdd:PRK10261 105 DmamifqepmtSLNPVFTVGEQIA--ESIRLHQGASREEAMVEAKRMLDQVRIPE-AQTILSR-YPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 225 VQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQMvqyF 304
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI---F 257
|
....*.
gi 1105531442 305 TSIGHP 310
Cdd:PRK10261 258 HAPQHP 263
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
79-302 |
4.02e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.10 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 79 SSQDSCELGirNLSFKVRSGQMLAIIGSSGCGRASLLDVITG----RGHggkmksgqIWINGQP---STPQLVRKCVAHV 151
Cdd:PRK11174 359 SPDGKTLAG--PLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyQGS--------LKINGIElreLDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 152 RQHDQLLPNlTVRETLAF----IAQMRLPRTFSQAQRDKRVEdviaelRLRQCANTRVGNTyVRGVSGGERRRVSIGVQL 227
Cdd:PRK11174 429 GQNPQLPHG-TLRDNVLLgnpdASDEQLQQALENAWVSEFLP------LLPQGLDTPIGDQ-AAGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1105531442 228 LWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISlHqpRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-H--QLEDLAQWDQIWVMQDGQIVQQGDYAELSQ 572
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
47-310 |
4.21e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.81 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 47 LEVRDLTYQVDIASQVPWFeqlaqfkipWRSHSSQDScelgIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggK 126
Cdd:PRK15079 9 LEVADLKVHFDIKDGKQWF---------WQPPKTLKA----VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV---K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 127 MKSGQIWINGQPSTpQLVRKCVAHVRQHDQL-----LPNLTVRETLAFIAQMRLpRTF----SQAQRDKRVEDVIAELRL 197
Cdd:PRK15079 73 ATDGEVAWLGKDLL-GMKDDEWRAVRSDIQMifqdpLASLNPRMTIGEIIAEPL-RTYhpklSRQEVKDRVKAMMLKVGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 198 RQcantRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIF 277
Cdd:PRK15079 151 LP----NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVK 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 1105531442 278 RLFDLVLLMtsgtpiYLGAAQQMVQY---FTSIGHP 310
Cdd:PRK15079 227 HISDRVLVM------YLGHAVELGTYdevYHNPLHP 256
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
88-289 |
5.66e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.26 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGR----ASLLDVITGrghGGKMKSGQIWINGQPSTPQLVR-KCVAHVRQHDQ--LLPN 160
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKsltcAAALGILPA---GVRQTAGRVLLDGKPVAPCALRgRKIATIMQNPRsaFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LT----VRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLrqcantrvgntYVRGVSGGERRRVSIGVQLLWNPGILIL 236
Cdd:PRK10418 96 HTmhthARETCLALGKPADDATLTAALEAVGLENAARVLKL-----------YPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 237 DEPTSGLDSFTAHNLVTTLSRLAKGNRL-VLISLHqprsD---IFRLFDLVLLMTSG 289
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALgMLLVTH----DmgvVARLADDVAVMSHG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
87-289 |
7.25e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.15 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RghggKMKSGQIWINGQP----STPQLVRKCVAHV---RQHDQLL 158
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGlR----PARGGRIMLNGKEinalSTAQRLARGLVYLpedRQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 PNLTVRETLAFIAQMRLPrTFSQAQRDKRVEDviaelRLRQCANTRV--GNTYVRGVSGGERRRVSIGVQLLWNPGILIL 236
Cdd:PRK15439 354 LDAPLAWNVCALTHNRRG-FWIKPARENAVLE-----RYRRALNIKFnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 237 DEPTSGLDSFTAHNLVTTLSRLAKGNRLVL-ISlhqprSD---IFRLFDLVLLMTSG 289
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVLfIS-----SDleeIEQMADRVLVMHQG 479
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
89-244 |
7.36e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITG---RGhggkmkSGQIWINGQP---STPQLVRKC-VAHVRQHDQLLPNL 161
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGvyqPD------SGEILLDGEPvrfRSPRDAQAAgIAIIHQELNLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLaFIAqmRLPRTF---SQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:COG1129 95 SVAENI-FLG--REPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGD-----LSVAQQQLVEIARALSRDARVLILDE 166
|
....*.
gi 1105531442 239 PTSGLD 244
Cdd:COG1129 167 PTASLT 172
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
82-269 |
7.58e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.58 E-value: 7.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 82 DSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLV---RKCVAHVRQH-DQL 157
Cdd:PRK13635 17 DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLL---LPEAGTITVGGMVLSEETVwdvRRQVGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 158 LPNLTVRETLAFIAQMR-LPRTfsqaQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILIL 236
Cdd:PRK13635 94 FVGATVQDDVAFGLENIgVPRE----EMVERVDQALRQVGMEDFLNREPHR-----LSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190
....*....|....*....|....*....|...
gi 1105531442 237 DEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISL 269
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSI 197
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
88-312 |
1.12e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.93 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRKCVAHVRQHDQLLPNLTVRETL 167
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE---KVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMRLP-RTFSQAQRDKRVEDVIAELRLRQCANTRVgntyvRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 246
Cdd:PRK13648 102 KYDVAFGLEnHAVPYDEMHRRVSEALKQVDMLERADYEP-----NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 247 TAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLfDLVLLMTSGTPIYLGAAQQM---VQYFTSIGHPCP 312
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTPTEIfdhAEELTRIGLDLP 244
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
89-271 |
1.18e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.78 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITgrgHGGKMKSGQIWING---QPSTPQLVRKCVAHVRQHDQLLPNLTVRE 165
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS---RLMTPAHGHVWLDGehiQHYASKEVARRIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 tlaFIAQMRLPRTFSQAQRDKRVEDVIAElRLRQCANTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 245
Cdd:PRK10253 101 ---LVARGRYPHQPLFTRWRKEDEEAVTK-AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190
....*....|....*....|....*....|
gi 1105531442 246 FTAHNLVTTLSRL--AKGNRL--VLISLHQ 271
Cdd:PRK10253 177 SHQIDLLELLSELnrEKGYTLaaVLHDLNQ 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
88-244 |
1.36e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR--GHGGKMKSGQiwingqpsTpqlVRkcVAHVRQH-DQLLPNLTVR 164
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGElePDSGTVKLGE--------T---VK--IGYFDQHqEELDPDKTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLafiaqmrlprtfSQAQRDKRvedviaELRLRQC------ANTRVgNTYVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:COG0488 398 DEL------------RDGAPGGT------EQEVRGYlgrflfSGDDA-FKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
....*.
gi 1105531442 239 PTSGLD 244
Cdd:COG0488 459 PTNHLD 464
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
71-270 |
1.94e-11 |
|
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: 64.41 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 71 FKIPWRSHSsqdsceLGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITgrgHGGKMKSGQIWINGQPSTP---QLVRKC 147
Cdd:cd03248 19 FAYPTRPDT------LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLE---NFYQPQGGQVLLDGKPISQyehKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 148 VAHVRQHDQLLPNlTVRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRlrQCANTRVGNtyvRG--VSGGERRRVSIGV 225
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELA--SGYDTEVGE---KGsqLSGGQKQRVAIAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1105531442 226 QLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLH 270
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHR 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
89-286 |
3.49e-11 |
|
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: 62.06 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKMKSGQIWINGQPstpqlvrkcvahVRQHDqllPNLTVRETLA 168
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSG---LYKPDSGEILVDGKE------------VSFAS---PRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 169 FIAQMrlprtfsqaqrdkrvedviaelrlrqcantrvgntyvrgvSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTA 248
Cdd:cd03216 79 MVYQL----------------------------------------SVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 1105531442 249 HNLVTTLSRL-AKGNRLVLISlHQPRsDIFRLFDLVLLM 286
Cdd:cd03216 119 ERLFKVIRRLrAQGVAVIFIS-HRLD-EVFEIADRVTVL 155
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
88-329 |
4.50e-11 |
|
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: 65.59 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRgHGGKMKSGQI-----------WINGQPSTPQLVRKCVAHVRQHDQ 156
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM-DQYEPTSGRIiyhvalcekcgYVERPSKVGEPCPVCGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 157 LLPNLTVRETLAF---IAQMrLPRTFSQAQRDKRVEDVIAEL---------------RLRQCANTRVGNTYV-RGVSGGE 217
Cdd:TIGR03269 95 DFWNLSDKLRRRIrkrIAIM-LQRTFALYGDDTVLDNVLEALeeigyegkeavgravDLIEMVQLSHRITHIaRDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 218 RRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLI-SLHQPRSdIFRLFDLVLLMTSGTPIYLGA 296
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVlTSHWPEV-IEDLSDKAIWLENGEIKEEGT 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1105531442 297 AQQMVQYF------------TSIGHPCPRYSNPADFYVdltSIDR 329
Cdd:TIGR03269 253 PDEVVAVFmegvsevekeceVEVGEPIIKVRNVSKRYI---SVDR 294
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
88-271 |
5.02e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.90 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGR---ASLLDvitgrgHGGKMKSGQIWINGQPsTPQL----VRKCVAHVRQHDQLLpN 160
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKstvAALLQ------NLYQPTGGQVLLDGVP-LVQYdhhyLHRQVALVGQEPVLF-S 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRlrQCANTRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:TIGR00958 569 GSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFP--NGYDTEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190
....*....|....*....|....*....|.
gi 1105531442 241 SGLDSFTAHNLVTTLSRlakGNRLVLISLHQ 271
Cdd:TIGR00958 646 SALDAECEQLLQESRSR---ASRTVLLIAHR 673
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
88-309 |
5.41e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.39 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKMKSGQIWINGQPSTPQ---LVRKCVAHVRQHDQLLPNLT 162
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEARVSGEVYLDGQDIFKMdviELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFIAQM-RLPRtfSQAQRDKRVEDVIAELRLRQCANTRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:PRK14247 99 IFENVALGLKLnRLVK--SKKELQERVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDifRLFDLVLLMTSGTPIYLGAAQQMvqyFTSIGH 309
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDMTIVLVTHFPQQAA--RISDYVAFLYKGQIVEWGPTREV---FTNPRH 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
90-300 |
6.45e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RGHGGkmKSGQIWINGQPSTPQLVR----KCVAHVRQHDQLLPNLTVR 164
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGT--YEGEIIFEGEELQASNIRdterAGIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLaFIAQ-------MRLPRTFSQAQRdkrvedVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:PRK13549 101 ENI-FLGNeitpggiMDYDAMYLRAQK------LLAQLKLDINPATPVGN-----LGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1105531442 238 EPTSGL-DSFTAH--NLVTTLSrlAKGNRLVLISlHQpRSDIFRLFDLVLLMTSGTPIYLGAAQQM 300
Cdd:PRK13549 169 EPTASLtESETAVllDIIRDLK--AHGIACIYIS-HK-LNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
89-272 |
7.06e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkmKSGQIWINGQPstpqlvrkcVAHVRQ--HDQLL-------- 158
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARP---DAGEVLWQGEP---------IRRQRDeyHQDLLylghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 -PNLTVRETLAFIAQMrlprtfSQAQRDKRVEDVIAELRLRqcantRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:PRK13538 86 kTELTALENLRFYQRL------HGPGDDEALWEALAQVGLA-----GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1105531442 238 EPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQP 272
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
88-273 |
7.68e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.78 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR-GHggKMKSGQIWINGQP----STPQLVRKCVAHVRQHDQLLPNLT 162
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpKY--EVTSGSILLDGEDilelSPDERARAGIFLAFQYPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRvgntYV-RGVSGGERRRVSIgVQ-LLWNPGILILDEPT 240
Cdd:COG0396 94 VSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDR----YVnEGFSGGEKKRNEI-LQmLLLEPKLAILDETD 168
|
170 180 190
....*....|....*....|....*....|...
gi 1105531442 241 SGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPR 273
Cdd:COG0396 169 SGLDIDALRIVAEGVNKLRSPDRGILIITHYQR 201
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
88-310 |
8.01e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.72 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRKCVAHVRQHDQLLPNLTVRETL 167
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLI---KSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQmrlprtFSQAQ--RDKRVEDV--------IAELRLRQCANTRV-----GNTYVR----GVSGGERRRVSIGVQLL 228
Cdd:PRK13631 119 SMVFQ------FPEYQlfKDTIEKDImfgpvalgVKKSEAKKLAKFYLnkmglDDSYLErspfGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 229 WNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLM------TSGTPIYLGAAQQMVQ 302
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMdkgkilKTGTPYEIFTDQHIIN 271
|
....*...
gi 1105531442 303 YfTSIGHP 310
Cdd:PRK13631 272 S-TSIQVP 278
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
88-295 |
1.13e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 61.78 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkMKSGQIWINGQPSTPqlvrkcvahVRQHDQLLPNLTVRETL 167
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP---PDSGTVTVRGRVSSL---------LGLGGGFNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMrlpRTFSQAQRDKRVEDVIAELRLRQCANTRVGnTYvrgvSGGERRRVSIGVQLLWNPGILILDEPTSGLD-SF 246
Cdd:cd03220 106 YLNGRL---LGLSRKEIDEKIDEIIEFSELGDFIDLPVK-TY----SSGMKARLAFAIATALEPDILLIDEVLAVGDaAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1105531442 247 TAHNLVTTLSRLAKGNRLVLISlHQPRSdIFRLFDLVLLMTSGTPIYLG 295
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVS-HDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
88-300 |
1.17e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 62.49 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRG--HGGKMKSGQIWINGQ----PSTPQL-VRKCVAHVRQHDQLLPn 160
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEVTITGSIVYNGHniysPRTDTVdLRKEIGMVFQQPNPFP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFiaQMRLprtfsQAQRDKRVEDVIAELRLRQCA-----NTRVGNTYVrGVSGGERRRVSIGVQLLWNPGILI 235
Cdd:PRK14239 100 MSIYENVVY--GLRL-----KGIKDKQVLDEAVEKSLKGASiwdevKDRLHDSAL-GLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 236 LDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLI--SLHQPRsdifRLFDLVLLMTSGTPIYLGAAQQM 300
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVtrSMQQAS----RISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
88-290 |
1.19e-10 |
|
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: 61.39 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRgHGGKMKSGQIWINGQPSTpqlvrkcvahvrqhdQLLPNLTVRE-- 165
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEVTEGEILFKGEDIT---------------DLPPEERARLgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFiaqmrlprtfsqaQRDKRVEDViaelrlrqcantRVGNtYVRGV----SGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:cd03217 80 FLAF-------------QYPPEIPGV------------KNAD-FLRYVnegfSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRsdIFRLF--DLVLLMTSGT 290
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIITHYQR--LLDYIkpDRVHVLYDGR 182
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
88-289 |
1.23e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RGHggkmKSGQIWINGQP----STPQLVRKCVAHV---RQHDQLLP 159
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGiREK----SAGTITLHGKKinnhNANEAINHGFALVteeRRSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVrETLAFIAQMRLPRTFSQAQRDKRVED----VIAELRLRqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILI 235
Cdd:PRK10982 340 YLDI-GFNSLISNIRNYKNKVGLLDNSRMKSdtqwVIDSMRVK----TPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 236 LDEPTSGLD---SFTAHNLVTTLSRLAKGnrLVLISLHQPrsDIFRLFDLVLLMTSG 289
Cdd:PRK10982 415 LDEPTRGIDvgaKFEIYQLIAELAKKDKG--IIIISSEMP--ELLGITDRILVMSNG 467
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
88-290 |
1.32e-10 |
|
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: 61.74 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRAS----LLDVITgrghggkMKSGQIWINGQPST---PQLVRKCVAHVRQHDQLLPN 160
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE-------LSSGSILIDGVDISkigLHDLRSRISIIPQDPVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 lTVRETLAFIAQM---RLPRTFSQAQRDKRVEDVIAELRLRQCANtrvGNTYvrgvSGGERRRVSIGVQLLWNPGILILD 237
Cdd:cd03244 93 -TIRSNLDPFGEYsdeELWQALERVGLKEFVESLPGGLDTVVEEG---GENL----SVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 238 EPTSGLDSFTAHNLVTTLsRLAKGNRLVLISLHqprsdifRL-----FDLVLLMTSGT 290
Cdd:cd03244 165 EATASVDPETDALIQKTI-REAFKDCTVLTIAH-------RLdtiidSDRILVLDKGR 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
88-244 |
2.48e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.59 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLL-------DVItgrgHGGKMkSGQIWINGQ----PST-PQLVRKCVAHVRQHd 155
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLI----PGARV-EGEILLDGEdiydPDVdVVELRRRVGMVFQK- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 156 qllPN---LTVRETLAFiaqmrLPRTfsQAQRDKRVEDVIAELRLRQCA-----NTRVgNTYVRGVSGGERRRVSIGVQL 227
Cdd:COG1117 101 ---PNpfpKSIYDNVAY-----GLRL--HGIKSKSELDEIVEESLRKAAlwdevKDRL-KKSALGLSGGQQQRLCIARAL 169
|
170
....*....|....*..
gi 1105531442 228 LWNPGILILDEPTSGLD 244
Cdd:COG1117 170 AVEPEVLLMDEPTSALD 186
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
88-295 |
2.57e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 61.55 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWING---QPSTPQLVRKCVAHVRQH-DQLLPNLTV 163
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL---KPQSGEIKIDGitiSKENLKEIRKKIGIIFQNpDNQFIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAF-IAQMRLPRtfsqaqrdKRVEDVIAELrlrqcaNTRVGNT-YVR----GVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:PRK13632 102 EDDIAFgLENKKVPP--------KKMKDIIDDL------AKKVGMEdYLDkepqNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 238 EPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFrLFDLVLLMTSGTPIYLG 295
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQG 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
91-299 |
2.82e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 91 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkmkSGQIWINGQP----STPQLvrkcvAHVR----QHDQLLPNLT 162
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG----SGSIQFAGQPleawSAAEL-----ARHRaylsQQQTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAfiaqMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSI-GVQL-LW---NPG--ILI 235
Cdd:PRK03695 86 VFQYLT----LHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQ-----LSGGEWQRVRLaAVVLqVWpdiNPAgqLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 236 LDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHqprsDI---FRLFDLVLLMTSGTPIYLGAAQQ 299
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSH----DLnhtLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
90-244 |
2.93e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.61 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASlldviTgrghggkMK---------SGQIWINGQPSTPQ--LVRKCVAHVRQHDQLL 158
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKST-----T-------MKmltgllpasEGEAWLFGQPVDAGdiATRRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 PNLTVRETLAFIAQM-RLPRtfsqAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:NF033858 352 GELTVRQNLELHARLfHLPA----AEIAARVAEMLERFDLADVADALPDS-----LPLGIRQRLSLAVAVIHKPELLILD 422
|
....*..
gi 1105531442 238 EPTSGLD 244
Cdd:NF033858 423 EPTSGVD 429
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
77-269 |
3.98e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 61.35 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 77 SHSSQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMKSGQIWINGQPSTPQL---VRKCVAHVRQ 153
Cdd:PRK13640 12 SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTvwdIREKVGIVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 154 H-DQLLPNLTVRETLAFIAQMR-LPRTfsqaQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNP 231
Cdd:PRK13640 92 NpDNQFVGATVGDDVAFGLENRaVPRP----EMIKIVRDVLADVGMLDYIDSEPAN-----LSGGQKQRVAIAGILAVEP 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1105531442 232 GILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISL 269
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISI 200
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
88-270 |
4.65e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.90 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKmksGQIWINGQ---PSTPQLVRKCVAHVRQH--DQLLPNlT 162
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQR---GRVKVMGRevnAENEKWVRSKVGLVFQDpdDQVFSS-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFIAQ-MRLprtfSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:PRK13647 97 VWDDVAFGPVnMGL----DKDEVERRVEEALKAVRMWDFRDKPPYH-----LSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180
....*....|....*....|....*....
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGNRLVLISLH 270
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQGKTVIVATH 196
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
91-289 |
4.75e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.17 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 91 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGkmkSGQIWINGQP----STPQLVRKcVAHVRQHDQLLPNLTVREt 166
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT---AGTVLVAGDDvealSARAASRR-VASVPQDTSLSFEFDVRQ- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 lafIAQM-RLPRT--FSQAQRDKR--VEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:PRK09536 97 ---VVEMgRTPHRsrFDTWTETDRaaVERAMERTGVAQFADRPVTS-----LSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 242 GLDsftAHNLVTTLS---RLAKGNRLVLISLHqprsDI---FRLFDLVLLMTSG 289
Cdd:PRK09536 169 SLD---INHQVRTLElvrRLVDDGKTAVAAIH----DLdlaARYCDELVLLADG 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
88-270 |
5.10e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.89 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWING------QPSTPQLVRKCVAHVRQHDQLLPNL 161
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIE---RPSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAfiaqmrLPRTFSQAQRD---KRVEDVIAELRLRQCANTrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:PRK10908 95 TVYDNVA------IPLIIAGASGDdirRRVSAALDKVGLLDKAKN-----FPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|..
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRLAKGNRLVLISLH 270
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
88-244 |
5.13e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.86 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTpQLVRKCVAHVRQHDQLL--------- 158
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLE---SPSQGNVSWRGEPLA-KLNRAQRKAFRRDIQMVfqdsisavn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 PNLTVRETLAfiAQMRLPRTFSQAQRDKRVEDVIAELRLR-QCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:PRK10419 104 PRKTVREIIR--EPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQ-----LSGGQLQRVCLARALAVEPKLLILD 176
|
....*..
gi 1105531442 238 EPTSGLD 244
Cdd:PRK10419 177 EAVSNLD 183
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
88-243 |
5.14e-10 |
|
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: 62.15 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RGHGGkmKSGQIWINGQPSTPQLVR----KCVAHVRQHDQLLPNLT 162
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGT--WDGEIYWSGSPLKASNIRdterAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFIAQMRLP-RTFSQAQRDKRVEDVIAELRLRQCANTRVgntyVRGVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:TIGR02633 95 VAENIFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTRP----VGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
..
gi 1105531442 242 GL 243
Cdd:TIGR02633 171 SL 172
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
90-300 |
5.29e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.55 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGGKMK--SGQIWINGQpSTPQL-------VRKCVAHVRQHDQLLPN 160
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLI-----GGQIApdHGEILFDGE-NIPAMsrsrlytVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFI--AQMRLPRTFSQAQRDKRVEDViaelRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:PRK11831 99 MNVFDNVAYPlrEHTQLPAPLLHSTVMMKLEAV----GLRGAAKLMPSE-----LSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 239 PTSGLDSFTAHNLVTTLSRL--AKGNRLVLISLHQPrsDIFRLFDLVLLMTSGTPIYLGAAQQM 300
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVP--EVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
90-302 |
7.61e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKMKSGQIWINGQPSTPQL--VRKCVAHVRQ--HDQLLPNlTV 163
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTVGDIVVSSTSKQKEIkpVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFiaqmrLPRTFSQAQRDkrVEDVIAELRLRQCANTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:PRK13643 103 LKDVAF-----GPQNFGIPKEK--AEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 244 DSFTAHNLVTTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
90-302 |
8.47e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.42 E-value: 8.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFkvRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKMKSGQIWINGQPSTPQL--VRKCVAHVRQ--HDQLLPNlTV 163
Cdd:PRK13634 27 NVSI--PSGSYVAIIGHTGSGKSTLLQHLNGllQPTSGTVTIGERVITAGKKNKKLkpLRKKVGIVFQfpEHQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAFiaqmrLPRTF--SQAQRDKRVEDVIAELRLRQCANTRVGNTyvrgVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:PRK13634 104 EKDICF-----GPMNFgvSEEDAKQKAREMIELVGLPEELLARSPFE----LSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
87-304 |
9.34e-10 |
|
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: 62.34 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKMKSGQIWINGQPSTPQL--VRKCVAHVRQHDQLLPNLTVR 164
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSILTNIsdVHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAQMR-LPrtfsqAQRDKRVED-VIAELRLRQCANtRVGNTYvrgvSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:TIGR01257 2031 EHLYLYARLRgVP-----AEEIEKVANwSIQSLGLSLYAD-RLAGTY----SGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 243 LDSFTAHNLVTTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQYF 304
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIIREGRAVVLTSHS-MEECEALCTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
92-267 |
1.06e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 92 SFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKMKSGQIWINGQPSTPQLVRKCVAHV-------RQHDQLLPNLTVR 164
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYG---ATRRTAGQVYLDGKPIDIRSPRDAIRAGimlcpedRKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAQmrlpRTFSQAQ--RDKRVEDVIAELRLRQCA-NTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:PRK11288 350 DNINISAR----RHHLRAGclINNRWEAENADRFIRSLNiKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180
....*....|....*....|....*.
gi 1105531442 242 GLDSFTAHNLVTTLSRLAKGNRLVLI 267
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
88-289 |
1.73e-09 |
|
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: 58.19 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASL-------LDVITGRghggkmksgqIWINGQPstpqlvrkcVAHVRQHDqllpn 160
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLilalfrfLEAEEGK----------IEIDGID---------ISTIPLED----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 ltVRETLAFIAQMrlPRTFSQAQR------DKRV-EDVIAELRLRQCANTrvgntyvrgVSGGERRRVSIGVQLLWNPGI 233
Cdd:cd03369 80 --LRSSLTIIPQD--PTLFSGTIRsnldpfDEYSdEEIYGALRVSEGGLN---------LSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1105531442 234 LILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISlHQPRSDIfrLFDLVLLMTSG 289
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIA-HRLRTII--DYDKILVMDAG 199
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
102-289 |
2.09e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.89 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 102 AIIGSSGCGRASLLDVITGRGHGgkmKSGQIWINGQP--------STPQLVRKcVAHVRQHDQLLPNLTVRETLAFiaQM 173
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRP---QKGRIVLNGRVlfdaekgiCLPPEKRR-IGYVFQDARLFPHYKVRGNLRY--GM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 174 RlprTFSQAQRDKRVEDV-IAELRLRqcantrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLV 252
Cdd:PRK11144 102 A---KSMVAQFDKIVALLgIEPLLDR----------YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1105531442 253 TTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSG 289
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
88-268 |
4.01e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.07 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKMKSGQIwINGQPSTPQLVRKCVAHVRQHDQL-LPNLTVR 164
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGllRPQKGKVLVSGI-DTGDFSKLQGIRKLVGIVFQNPETqFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAQ-MRLPRTfsqaQRDKRVEDVIAELRLRqcantRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:PRK13644 97 EDLAFGPEnLCLPPI----EIRKRVDRALAEIGLE-----KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180
....*....|....*....|....*.
gi 1105531442 244 DSFTAHNLVTTLSRL-AKGNRLVLIS 268
Cdd:PRK13644 168 DPDSGIAVLERIKKLhEKGKTIVYIT 193
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
88-295 |
4.72e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKMKSGQIWINGQpSTPQLVRKCVAH-----VRQHDQLLPNLT 162
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG---IHEPTKGTITINNI-NYNKLDHKLAAQlgigiIYQELSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLaFIAqmRLP-------RTFSQAQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILI 235
Cdd:PRK09700 97 VLENL-YIG--RHLtkkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1105531442 236 LDEPTSGLDSFTAHNLVTTLSRLAK-GNRLVLISlHQpRSDIFRLFDLVLLMTSGTPIYLG 295
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYIS-HK-LAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
91-244 |
6.50e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 91 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGkmkSGQIWINGQPSTPQLVRKCVAHVRQHDQLLPNLTVRETLAFI 170
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVE---SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 171 AQMrlprtfsQAQRDKRVEDviaelrlrqCANTRVG-----NTYVRGVSGGERRRVSIGvQLLWNPGIL-ILDEPTSGLD 244
Cdd:PRK13543 107 CGL-------HGRRAKQMPG---------SALAIVGlagyeDTLVRQLSAGQKKRLALA-RLWLSPAPLwLLDEPYANLD 169
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
88-257 |
2.23e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASlldviTGRG--HGGKMKSGQIWINGQ------PSTPQLVRKCVAHVRQ--HDQL 157
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKST-----TGRAllRLVESQGGEIIFNGQridtlsPGKLQALRRDIQFIFQdpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 158 LPNLTVRETLafIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRvgntYVRGVSGGERRRVSIGVQLLWNPGILILD 237
Cdd:PRK10261 415 DPRQTVGDSI--MEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWR----YPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180
....*....|....*....|...
gi 1105531442 238 EPTSGLD-SFTAH--NLVTTLSR 257
Cdd:PRK10261 489 EAVSALDvSIRGQiiNLLLDLQR 511
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
90-247 |
2.62e-08 |
|
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: 56.73 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKM--KSGQIWINGQPSTPQL---VRKCVAHVRQHDQLLPNLT 162
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGvlEPTSGEVnvRVGDEWVDMTKPGPDGrgrAKRYIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFIAQMRLPRTFSQAQ----------RDKRVEDVIaelrlrqcantrvgNTYVRGVSGGERRRVSIGVQLLWNPG 232
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKavitlkmvgfDEEKAEEIL--------------DKYPDELSEGERHRVALAQVLIKEPR 447
|
170
....*....|....*
gi 1105531442 233 ILILDEPTSGLDSFT 247
Cdd:TIGR03269 448 IVILDEPTGTMDPIT 462
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
88-319 |
2.84e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.43 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGH-GGKMK-SGQIWINGQPSTPQLV-----RKCVAHVRQHDQLLPn 160
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElESEVRvEGRVEFFNQNIYERRVnlnrlRRQVSMVHPKPNLFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 LTVRETLAFiaQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:PRK14258 102 MSVYDNVAY--GVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALD-LSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 241 SGLD---SFTAHNLVTTLsRLAKGNRLVLISLHQPRsdIFRLFDLVLLMTSGTpiylGAAQQMVQYftsiGHPCPRYSNP 317
Cdd:PRK14258 179 FGLDpiaSMKVESLIQSL-RLRSELTMVIVSHNLHQ--VSRLSDFTAFFKGNE----NRIGQLVEF----GLTKKIFNSP 247
|
..
gi 1105531442 318 AD 319
Cdd:PRK14258 248 HD 249
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
88-247 |
3.72e-08 |
|
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: 55.25 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR--GHGGKMK-SGQIWINGQPStpqlvrkcvahvrqhdQLLPNlTVR 164
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGElePSEGKIKhSGRISFSSQFS----------------WIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAQMRLPRTFSQAQRDKRVEDViaeLRLRQCANTRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:cd03291 116 ENIIFGVSYDEYRYKSVVKACQLEEDI---TKFPEKDNTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
...
gi 1105531442 245 SFT 247
Cdd:cd03291 192 VFT 194
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
86-244 |
4.58e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.79 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 86 LGIRNLSFKVRSGQMLAIIGSSGCGRASLL-------DVITGRGHGGKMKSGQIWINGQPSTPQLVRKCVAHVRQHDQLL 158
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRVEGKVTFHGKNLYAPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 PNlTVRETLAFIAQMR---------LPRTFSQAQRDKRVEDviaelRLRQCANTrvgntyvrgVSGGERRRVSIGVQLLW 229
Cdd:PRK14243 104 PK-SIYDNIAYGARINgykgdmdelVERSLRQAALWDEVKD-----KLKQSGLS---------LSGGQQQRLCIARAIAV 168
|
170
....*....|....*
gi 1105531442 230 NPGILILDEPTSGLD 244
Cdd:PRK14243 169 QPEVILMDEPCSALD 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
75-289 |
4.77e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 75 WRSHSSQDScelgIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkmksgqiwINGQPSTPQLVRKCVAHVRQH 154
Cdd:PLN03232 624 WDSKTSKPT----LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE------------LSHAETSSVVIRGSVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 155 DQLLpNLTVRETLAFIAQMrlprtfsQAQRDKRVEDVIA---ELRLRQCAN-TRVGNtyvRGV--SGGERRRVSIGVQLL 228
Cdd:PLN03232 688 SWIF-NATVRENILFGSDF-------ESERYWRAIDVTAlqhDLDLLPGRDlTEIGE---RGVniSGGQKQRVSMARAVY 756
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 229 WNPGILILDEPTSGLDSFTAHNLVTT-LSRLAKGNRLVLIS--LHqprsdIFRLFDLVLLMTSG 289
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTnqLH-----FLPLMDRIILVSEG 815
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
90-302 |
5.85e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 54.75 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLVRKCVAHVRQH---------DQLLPN 160
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH---VPTQGSVRVDDTLITSTSKNKDIKQIRKKvglvfqfpeSQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 161 lTVRETLAFiaqmrLPRTFSQAQRDKrveDVIAELRLRQcantrVG---NTYVRG---VSGGERRRVSIGVQLLWNPGIL 234
Cdd:PRK13649 102 -TVLKDVAF-----GPQNFGVSQEEA---EALAREKLAL-----VGiseSLFEKNpfeLSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1105531442 235 ILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQ 302
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHL-MDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
88-290 |
7.99e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 54.40 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKMKSGQIWINGQPSTPQL--VRKCVAHVRQ--HDQLLPNL 161
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllKPTTGTVTVDDITITHKTKDKYIrpVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFiaqmrlPRTFSQAQrdKRVEDVIAELRLRQCANTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:PRK13646 103 VEREIIFG------PKNFKMNL--DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1105531442 242 GLDSFTAHNLVTTLSRLA-KGNRLVLISLHQpRSDIFRLFDLVLLMTSGT 290
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtDENKTIILVSHD-MNEVARYADEVIVMKEGS 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
89-244 |
8.81e-08 |
|
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: 55.08 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRA----SLLDVItgrGHGGKMKSGQIWINGQP----STPQLvRKcvahVRQHD----- 155
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvtalSILRLL---PDPAAHPSGSILFDGQDllglSEREL-RR----IRGNRiamif 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 156 Q-----LLPNLTV----RETLafiaqmRLPRTFSQAQRDKRVEDVIAELRLRQcANTRVgNTYVRGVSGGERRRVSIGVQ 226
Cdd:COG4172 99 QepmtsLNPLHTIgkqiAEVL------RLHRGLSGAAARARALELLERVGIPD-PERRL-DAYPHQLSGGQRQRVMIAMA 170
|
170
....*....|....*...
gi 1105531442 227 LLWNPGILILDEPTSGLD 244
Cdd:COG4172 171 LANEPDLLIADEPTTALD 188
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
88-302 |
9.11e-08 |
|
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: 55.72 E-value: 9.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggKMK--SGQIWINGQpstpqlvrkcVAHVRQHdQLLPNLTVRE 165
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLA-----EMDkvEGHVHMKGS----------VAYVPQQ-AWIQNDSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAQMRLPRTFSQAQRDKRVEDViaELrLRQCANTRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 245
Cdd:TIGR00957 718 NILFGKALNEKYYQQVLEACALLPDL--EI-LPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 246 FTA----HNLVTTLSRLAKGNRLVL---ISlHQPRSDIfrlfdlVLLMTSGTPIYLGAAQQMVQ 302
Cdd:TIGR00957 794 HVGkhifEHVIGPEGVLKNKTRILVthgIS-YLPQVDV------IIVMSGGKISEMGSYQELLQ 850
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
85-244 |
9.71e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.78 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 85 ELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR---GHGG---KMKSGQIWINGQPSTPQ---LVRKCVAHVRQH- 154
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARlapDAGEvhyRMRDGQLRDLYALSEAErrrLLRTEWGFVHQHp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 155 -DQLLPNLT----VRETLAFIAQMRLPRTFSQAQR-DKRVEdvIAELRLRQCANTrvgntyvrgVSGGERRRVSIGVQLL 228
Cdd:PRK11701 99 rDGLRMQVSaggnIGERLMAVGARHYGDIRATAGDwLERVE--IDAARIDDLPTT---------FSGGMQQRLQIARNLV 167
|
170
....*....|....*.
gi 1105531442 229 WNPGILILDEPTSGLD 244
Cdd:PRK11701 168 THPRLVFMDEPTGGLD 183
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
89-304 |
1.05e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 53.55 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggKMK--SGQIWINGQPSTpqlvrkcvahvrqhdqLL-------P 159
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAG-----ILEptSGRVEVNGRVSA----------------LLelgagfhP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVRETLAFIAQMRlprTFSQAQRDKRVEDVI--AELRlrQCANTRVGnTYvrgvSGGERRRVSIGVQLLWNPGILILD 237
Cdd:COG1134 102 ELTGRENIYLNGRLL---GLSRKEIDEKFDEIVefAELG--DFIDQPVK-TY----SSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 238 EPTS-GLDSFT--AHNLVTtlSRLAKGNRLVLISlHQPRSdIFRLFDLVLLMTSGTPIYLGAAQQMVQYF 304
Cdd:COG1134 172 EVLAvGDAAFQkkCLARIR--ELRESGRTVIFVS-HSMGA-VRRLCDRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
83-268 |
1.70e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 83 SCELGIRNLSFKVRSGQM--------------LAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTP---QLVR 145
Cdd:PRK10790 338 SGRIDIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYY---PLTEGEIRLDGRPLSSlshSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 146 KCVAHVRQHDQLLPNltvretlAFIAQMRLPRTFSQAQRDKRVEDV-IAEL--RLRQCANTRVG---NTyvrgVSGGERR 219
Cdd:PRK10790 415 QGVAMVQQDPVVLAD-------TFLANVTLGRDISEEQVWQALETVqLAELarSLPDGLYTPLGeqgNN----LSVGQKQ 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1105531442 220 RVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLIS 268
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
27-303 |
2.26e-07 |
|
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: 53.98 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 27 LFSSESDNSLYFTYSGQSN-TLEVRDLTYQVDIASQVpwfeqlaqfkipwrshssqdscelgIRNLSFKVRSGQMLAIIG 105
Cdd:TIGR01193 453 LVDSEFINKKKRTELNNLNgDIVINDVSYSYGYGSNI-------------------------LSDISLTIKMNSKTTIVG 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 106 SSGCGRASLLDVITGRGHGGkmkSGQIWINGQPstpqLVRKCVAHVRQHDQLLPNL------TVRETLAFIAQmrlpRTF 179
Cdd:TIGR01193 508 MSGSGKSTLAKLLVGFFQAR---SGEILLNGFS----LKDIDRHTLRQFINYLPQEpyifsgSILENLLLGAK----ENV 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 180 SQAQRDKRVEdvIAELR-----LRQCANTRVgNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTT 254
Cdd:TIGR01193 577 SQDEIWAACE--IAEIKddienMPLGYQTEL-SEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNN 653
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1105531442 255 LSRLAkgNRLVLISLHqpRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQY 303
Cdd:TIGR01193 654 LLNLQ--DKTIIFVAH--RLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
81-296 |
2.37e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.70 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 81 QDSCELGIRNLSFKVRSgqMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQP---STPQLV--RKCVAHVRQH- 154
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSP--VTGLVGANGCGKSTLFMNLSGLL---RPQKGAVLWQGKPldySKRGLLalRQQVATVFQDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 155 DQLLPNLTVRETLAF-IAQMRLPrtfsQAQRDKRVEDVIAEL---RLRQcantrvgnTYVRGVSGGERRRVSIGVQLLWN 230
Cdd:PRK13638 87 EQQIFYTDIDSDIAFsLRNLGVP----EAEITRRVDEALTLVdaqHFRH--------QPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1105531442 231 PGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSGTPIYLGA 296
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDI-DLIYEISDAVYVLRQGQILTHGA 219
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
88-284 |
2.53e-07 |
|
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: 51.00 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkmksgqIWINGQPSTPQLVRKCVAHVRQHdQLLPNLTVRETL 167
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-----------LWPWGSGRIGMPEGEDLLFLPQR-PYLPLGTLREQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQMRLprtfsqaqrdkrvedviaelrlrqcantrvgntyvrgvSGGERRRVSIGVQLLWNPGILILDEPTSGLDsft 247
Cdd:cd03223 85 IYPWDDVL--------------------------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALD--- 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 1105531442 248 aHNLVTTLSRLAKGNRLVLISL-HQPRSDIFrlFDLVL 284
Cdd:cd03223 124 -EESEDRLYQLLKELGITVISVgHRPSLWKF--HDRVL 158
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
90-244 |
3.18e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFkvRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWingqpstPQLVRKcVAHVRQHDQLLPNLTVRET--- 166
Cdd:TIGR03719 25 SLSF--FPGAKIGVLGLNGAGKSTLLRIMAGVD---KDFNGEAR-------PQPGIK-VGYLPQEPQLDPTKTVRENvee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 -LAFIAQM--RLPRTFSQ-----AQRDK------RVEDVIA-------ELRLRQCANT-RV--GNTYVRGVSGGERRRVS 222
Cdd:TIGR03719 92 gVAEIKDAldRFNEISAKyaepdADFDKlaaeqaELQEIIDaadawdlDSQLEIAMDAlRCppWDADVTKLSGGERRRVA 171
|
170 180
....*....|....*....|..
gi 1105531442 223 IGVQLLWNPGILILDEPTSGLD 244
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
88-268 |
3.47e-07 |
|
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: 50.14 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRG--HGGKMKSGQiwingqpstpqlvrkcvahvrqhdqllpnltvRE 165
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELepDEGIVTWGS--------------------------------TV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFIAQMrlprtfsqaqrdkrvedviaelrlrqcantrvgntyvrgvSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 245
Cdd:cd03221 64 KIGYFEQL----------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180
....*....|....*....|...
gi 1105531442 246 FTAHNLVTTLSRLaKGNrLVLIS 268
Cdd:cd03221 104 ESIEALEEALKEY-PGT-VILVS 124
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
88-247 |
4.30e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKMKSGqiwingqpSTPqlvrkcVAHVR-------QHDQLL 158
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGleTPSAGELLAG--------TAP------LAEARedtrlmfQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 159 PNLTVRETLAFiaqmrlprTFSQAQRDkRVEDVIAELRLRQCANTrvgntYVRGVSGGERRRVSIGVQLLWNPGILILDE 238
Cdd:PRK11247 94 PWKKVIDNVGL--------GLKGQWRD-AALQALAAVGLADRANE-----WPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
....*....
gi 1105531442 239 PTSGLDSFT 247
Cdd:PRK11247 160 PLGALDALT 168
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
87-296 |
4.64e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.93 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIwINGQPSTPQLVRKC--VAHVRQHDQLLPNL--- 161
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI---ISETGQT-IVGDYAIPANLKKIkeVKRLRKEIGLVFQFpey 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 -----TVRETLAFiAQMRLPRTFSQAQrdKRVEDVIAELRLRQcantrvgnTYVR----GVSGGERRRVSIGVQLLWNPG 232
Cdd:PRK13645 102 qlfqeTIEKDIAF-GPVNLGENKQEAY--KKVPELLKLVQLPE--------DYVKrspfELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1105531442 233 ILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGA 296
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
88-316 |
5.33e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.63 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWINGQPSTPQLV---RKCVAHVRQH-DQLLPNLTV 163
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF---EEFEGKVKIDGELLTAENVwnlRRKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RETLAF-IAQMRLPRTfsqaQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:PRK13642 100 EDDVAFgMENQGIPRE----EMIKRVDEALLAVNMLDFKTREPAR-----LSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1105531442 243 LDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRlFDLVLLMTSGTPIYLGAAQQMV---QYFTSIGHPCPRYSN 316
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFatsEDMVEIGLDVPFSSN 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
88-275 |
7.66e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKMKSGQIWingqpstpqlVRKCVAHVRQHDQLLpNLTVRETL 167
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF---EISEGRVW----------AERSIAYVPQQAWIM-NATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 168 AFIAQmrlprtfsqaQRDKRVEDVIA----ELRLRQCA---NTRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPT 240
Cdd:PTZ00243 742 LFFDE----------EDAARLADAVRvsqlEADLAQLGgglETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1105531442 241 SGLDSFTAHNLVTT--LSRLAKGNRlvLISLHQ----PRSD 275
Cdd:PTZ00243 811 SALDAHVGERVVEEcfLGALAGKTR--VLATHQvhvvPRAD 849
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
88-247 |
1.11e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR--GHGGKMK-SGQIWINGQPStpqlvrkcvahvrqhdQLLPNlTVR 164
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGElePSEGKIKhSGRISFSPQTS----------------WIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAQMRLPRTFSQAQRDKRVEDVIaelRLRQCANTRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:TIGR01271 505 DNIIFGLSYDEYRYTSVIKACQLEEDIA---LFPEKDKTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
...
gi 1105531442 245 SFT 247
Cdd:TIGR01271 581 VVT 583
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
89-244 |
1.46e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 89 RNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RghggKMKSGQIWING----QPSTPQLVRKCVAHVRQH--DQLLPNL 161
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGaR----KIQQGRVEVLGgdmaDARHRRAVCPRIAYMPQGlgKNLYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFIAqmrlpRTFSQ--AQRDKRVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEP 239
Cdd:NF033858 94 SVFENLDFFG-----RLFGQdaAERRRRIDELLRATGLAPFADRPAGK-----LSGGMKQKLGLCCALIHDPDLLILDEP 163
|
....*
gi 1105531442 240 TSGLD 244
Cdd:NF033858 164 TTGVD 168
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
79-315 |
1.72e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.49 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 79 SSQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRA----SLLDVITGRGH-GG------------------KMKSGQI-WI 134
Cdd:PRK09473 23 STPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRiGGsatfngreilnlpekelnKLRAEQIsMI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 135 NGQPST---PqlvrkcvaHVRQHDQLLpnltvrETLAFIAQMRLPRTFSQAQRdkRVEDV-IAELRLRQcantrvgNTYV 210
Cdd:PRK09473 103 FQDPMTslnP--------YMRVGEQLM------EVLMLHKGMSKAEAFEESVR--MLDAVkMPEARKRM-------KMYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 211 RGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGT 290
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
250 260
....*....|....*....|....*
gi 1105531442 291 PIYLGAAQQMvqyFTSIGHPcprYS 315
Cdd:PRK09473 240 TMEYGNARDV---FYQPSHP---YS 258
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
90-249 |
2.13e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.28 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhgGKMKSGQIWINGQpstpqlvrkcVAHVRQHDQLLpNLTVRETLAF 169
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGEL--PPRSDASVVIRGT----------VAYVPQVSWIF-NATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 170 IAQMrlprtfsQAQRDKRVEDVIA---ELRLRQCAN-TRVGNtyvRGV--SGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:PLN03130 702 GSPF-------DPERYERAIDVTAlqhDLDLLPGGDlTEIGE---RGVniSGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
....*.
gi 1105531442 244 DsftAH 249
Cdd:PLN03130 772 D---AH 774
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
85-271 |
2.13e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 85 ELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKMKSGQIWINGQPSTPQLV--RKCVAHVRQHDQLLPNLT 162
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL---LNPEKGEILFERQSIKKDLCtyQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFIAQmrlprtFSQAQRDkrVEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVsiGVQLLWNPG--ILILDEPT 240
Cdd:PRK13540 91 LRENCLYDIH------FSPGAVG--ITELCRLFSLEHLIDYPCGL-----LSSGQKRQV--ALLRLWMSKakLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|.
gi 1105531442 241 SGLDSFTAHNLVTTLSRLAKGNRLVLISLHQ 271
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
88-289 |
2.72e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 49.40 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKMKSGQIWINGQPSTPQLVRKCVAHVRQHDQ-----LLPNLT 162
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM---IEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQdpstsLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 163 VRETLAFiaQMRLPRTFSQAQRDKRVEDVIAELRLRqcanTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:PRK15112 106 ISQILDF--PLRLNTDLEPEQREKQIIETLRQVGLL----PDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1105531442 243 LDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSG 289
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
202-271 |
3.06e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 3.06e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 202 NTRVGNTYVRgVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLaKG--NRLVLISLHQ 271
Cdd:PTZ00265 570 ETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL-KGneNRITIIIAHR 639
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
197-310 |
3.53e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 197 LRQCANtRVgNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDI 276
Cdd:PRK15134 143 IRQAAK-RL-TDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIV 220
|
90 100 110
....*....|....*....|....*....|....
gi 1105531442 277 FRLFDLVLLMTSGTPIYLGAAQQMvqyFTSIGHP 310
Cdd:PRK15134 221 RKLADRVAVMQNGRCVEQNRAATL---FSAPTHP 251
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
90-325 |
4.65e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.94 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSgqMLAIIGSSGCGRASLL-------DVITGRGHGG------------------KMKSGQIWINGQPSTPQLV 144
Cdd:PRK14271 41 SMGFPARA--VTSLMGPTGSGKTTFLrtlnrmnDKVSGYRYSGdvllggrsifnyrdvlefRRRVGMLFQRPNPFPMSIM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 145 RKCVAHVRQHdQLLPnltvRETLAFIAQMRLprtfsqaqrdkrvedviAELRLRQCANTRVGNTYVRgVSGGERRRVSIG 224
Cdd:PRK14271 119 DNVLAGVRAH-KLVP----RKEFRGVAQARL-----------------TEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 225 VQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAkgNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQMvqyF 304
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL---F 250
|
250 260
....*....|....*....|.
gi 1105531442 305 TSighpcPRYSNPADFYVDLT 325
Cdd:PRK14271 251 SS-----PKHAETARYVAGLS 266
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
87-268 |
5.76e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 87 GIRNLSFKVRSGQMLAIIGSSGCG--RASLLDVITGRGHGGKMKSGQIWINGQPStpqLVRKCVAHVRQHDQLLPNLTVR 164
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRA---LRRTIG*HRPVR*GRRESFSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 165 ETLAFIAQ-MRLPRTFSQAqrdkRVEDVIAELRLRQCANtRVGNTYvrgvSGGERRRVSIGVQLLWNPGILILDEPTSGL 243
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARA----RADELLERFSLTEAAG-RAAAKY----SGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180
....*....|....*....|....*
gi 1105531442 244 DSFTAHNLVTTLSRLAKGNRLVLIS 268
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGATVLLT 200
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
214-244 |
6.50e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 6.50e-06
10 20 30
....*....|....*....|....*....|.
gi 1105531442 214 SGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
270-324 |
8.48e-06 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 48.75 E-value: 8.48e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1105531442 270 HQPRSDIFRLF-DLVLLMTSGTPIYLGAAQQMVQYFTSIGHPCPRYSNPADFYVDL 324
Cdd:pfam19055 1 HQPSYTLFKMFdDLILLAKGGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDI 56
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
88-244 |
1.13e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLdvitgrghggKMKSGQIwingQPSTPQLvrKC-----VAHVRQHDQLL-PNL 161
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLL----------KLMLGQL----QADSGRI--HCgtkleVAYFDQHRAELdPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 TVRETLAFIAQmrlprTFSQAQRDKRV----EDVI-AELRLRqcantrvgnTYVRGVSGGERRRVSIGVQLLWNPGILIL 236
Cdd:PRK11147 399 TVMDNLAEGKQ-----EVMVNGRPRHVlgylQDFLfHPKRAM---------TPVKALSGGERNRLLLARLFLKPSNLLIL 464
|
....*...
gi 1105531442 237 DEPTSGLD 244
Cdd:PRK11147 465 DEPTNDLD 472
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
212-270 |
1.31e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.77 E-value: 1.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 212 GVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLH 270
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
88-267 |
1.37e-05 |
|
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: 46.16 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLL-DVITgrghggkmKSGQIWINGQPSTPQlvrkcvahvrqhdqllPNLTVret 166
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVnEGLY--------ASGKARLISFLPKFS----------------RNKLI--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 laFIAQMrlprtfsqaqrdKRVEDV-IAELRLRQCANTrvgntyvrgVSGGERRRVSIGVQLLWNPG--ILILDEPTSGL 243
Cdd:cd03238 64 --FIDQL------------QFLIDVgLGYLTLGQKLST---------LSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180
....*....|....*....|....*
gi 1105531442 244 DSFTAHNLVTTLSRL-AKGNRLVLI 267
Cdd:cd03238 121 HQQDINQLLEVIKGLiDLGNTVILI 145
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
154-281 |
1.81e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 154 HDQLLPNLTVRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQcaNTRVGnTYVRGVSGGERRRVSIGVQLLWNPGI 233
Cdd:PTZ00265 1303 QEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKY--DTNVG-PYGKSLSGGQKQRIAIARALLREPKI 1379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1105531442 234 LILDEPTSGLDSFTAHNLVTTLSRLA-KGNRLVLISLHQ----PRSDIFRLFD 281
Cdd:PTZ00265 1380 LLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRiasiKRSDKIVVFN 1432
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
90-289 |
3.02e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkMKSGQIWINGQ------PSTPQLVRKCVAHvrQHDQLLPNLTV 163
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT---RDAGSILYLGKevtfngPKSSQEAGIGIIH--QELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 -------RETLAFIAQMRLPRTFSQAqrDKrvedVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILIL 236
Cdd:PRK10762 97 aeniflgREFVNRFGRIDWKKMYAEA--DK----LLARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1105531442 237 DEPTSGL-DSFTAhNLVTTLSRL-AKGNRLVLISlHQPRsDIFRLFDLVLLMTSG 289
Cdd:PRK10762 166 DEPTDALtDTETE-SLFRVIRELkSQGRGIVYIS-HRLK-EIFEICDDVTVFRDG 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
88-297 |
4.61e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.40 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrgHGG-KMKSGQIWINGQpSTPQLVrkcvAHVRQHDQLLpnltvret 166
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAyKILEGDILFKGE-SILDLE----PEERAHLGIF-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 167 LAFIAQMRLP--------RTFSQAQRDKRVEDVIAELRLRQCANTR---VG------NTYV-RGVSGGERRRVSIGVQLL 228
Cdd:CHL00131 88 LAFQYPIEIPgvsnadflRLAYNSKRKFQGLPELDPLEFLEIINEKlklVGmdpsflSRNVnEGFSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1105531442 229 WNPGILILDEPTSGLDSFTAHNLVTTLSRLA-KGNRLVLISLHQprsdifRLF-----DLVLLMTSGTPIYLGAA 297
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQ------RLLdyikpDYVHVMQNGKIIKTGDA 236
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
88-272 |
6.09e-05 |
|
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: 46.28 E-value: 6.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghggkmksGQIW--INGQPSTPqlvRKCVAHVRQHDQLLPNLTVRE 165
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRIL-----------GELWpvYGGRLTKP---AKGKLFYVPQRPYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLafIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNTYVRG----VSGGERRRVSIGVQLLWNPGILILDEPTS 241
Cdd:TIGR00954 534 QI--IYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDwmdvLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|..
gi 1105531442 242 GLdsftAHNLVTTLSRLAKGNRLVLISL-HQP 272
Cdd:TIGR00954 612 AV----SVDVEGYMYRLCREFGITLFSVsHRK 639
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
212-272 |
7.91e-05 |
|
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: 43.50 E-value: 7.91e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1105531442 212 GVSGGERRRVSIGVQL---LWNPGIL-ILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQP 272
Cdd:cd03227 77 QLSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
186-270 |
9.31e-05 |
|
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: 45.55 E-value: 9.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 186 KRVEDVIAELRLRQcantrVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLV 265
Cdd:COG1245 191 GKLDELAEKLGLEN-----ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYV 265
|
....*
gi 1105531442 266 LISLH 270
Cdd:COG1245 266 LVVEH 270
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
90-244 |
9.82e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 44.33 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITG---RGHGGKMKSGQIWINGQPSTPQLvrkcvahvrqhDQLLPnLTVRET 166
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGlvaPDEGVIKRNGKLRIGYVPQKLYL-----------DTTLP-LTVNRF 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 167 lafiaqMRL-PRTfsqaqrdkRVEDVIAELRLRQCANtrVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:PRK09544 90 ------LRLrPGT--------KKEDILPALKRVQAGH--LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
90-289 |
1.04e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 90 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkMKSGQIWINGQP----STPQLVRKCVAHVRQHDQLLPNLTVRE 165
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ---KDSGSILFQGKEidfkSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 166 TLAFiaqMRLPRTFSQAQRDKRVEDVIA---ELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILILDEPTSG 242
Cdd:PRK10982 93 NMWL---GRYPTKGMFVDQDKMYRDTKAifdELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1105531442 243 LDSFTAHNLVTTLSRL-AKGNRLVLISlHQpRSDIFRLFDLVLLMTSG 289
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLkERGCGIVYIS-HK-MEEIFQLCDEITILRDG 210
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
88-273 |
3.71e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.86 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 88 IRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRgHGGKMKSGQIWINGQP----STPQLVRKCVAHVRQHDQLLPNLTV 163
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEVTGGTVEFKGKDllelSPEDRAGEGIFMAFQYPVEIPGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 164 RetlaFIAQMRLP--RTFSQAQRDKR------VEDVIAELRLRQCANTRVGNTyvrGVSGGERRRVSIGVQLLWNPGILI 235
Cdd:PRK09580 96 Q----FFLQTALNavRSYRGQEPLDRfdfqdlMEEKIALLKMPEDLLTRSVNV---GFSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1105531442 236 LDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPR 273
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQR 206
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
160-267 |
4.24e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 43.46 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVRETLAFIAQMRLPrtfsqAQRDKRVEDVIAELRLRQCANTRVGNTYV------RGVSGGERRRV----SIGVQLLw 229
Cdd:TIGR00630 435 ELSIREAHEFFNQLTLT-----PEEKKIAEEVLKEIRERLGFLIDVGLDYLslsraaGTLSGGEAQRIrlatQIGSGLT- 508
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1105531442 230 npGIL-ILDEPTSGLDSFTAHNLVTTLSRLAK-GNRLVLI 267
Cdd:TIGR00630 509 --GVLyVLDEPSIGLHQRDNRRLINTLKRLRDlGNTLIVV 546
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
214-267 |
5.07e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 5.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1105531442 214 SGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLA-KGNRLVLI 267
Cdd:PRK10938 137 STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHqSGITLVLV 191
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
95-270 |
5.64e-04 |
|
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: 42.35 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 95 VRSGQMLAIIGSSGCGRASLLDVITGR--GHGGKMKSGQIW------ING---QPSTPQLVRKCVAHVR--QHDQLLPNL 161
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKlkPNLGKFDDPPDWdeildeFRGselQNYFTKLLEGDVKVIVkpQYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 162 ---TVRETLAfiaqmrlprtfsqaQRDKR--VEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVSIGVQLLWNPGILIL 236
Cdd:cd03236 103 vkgKVGELLK--------------KKDERgkLDELVDQLELRHVLDRNIDQ-----LSGGELQRVAIAAALARDADFYFF 163
|
170 180 190
....*....|....*....|....*....|....
gi 1105531442 237 DEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLH 270
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
183-244 |
6.30e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 6.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1105531442 183 QRDKRVEDVIAELRLRqcantrvGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:PRK11147 134 QLENRINEVLAQLGLD-------PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
214-291 |
1.11e-03 |
|
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: 41.45 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 214 SGGERRRVSIGVQLLW---NPGILILDEPTSGLDSFTAHNLVTTLSRL-AKGNRLVLISlHQprSDIFRLFDLVL----- 284
Cdd:cd03271 171 SGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIE-HN--LDVIKCADWIIdlgpe 247
|
90
....*....|....
gi 1105531442 285 -------LMTSGTP 291
Cdd:cd03271 248 ggdgggqVVASGTP 261
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
148-270 |
1.41e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 148 VAHVRQHDQLLPNL---TVRETLAfiaqmrlprtfsqaQRDKR--VEDVIAELRLRQCANTRVGNtyvrgVSGGERRRVS 222
Cdd:PRK13409 162 VVHKPQYVDLIPKVfkgKVRELLK--------------KVDERgkLDEVVERLGLENILDRDISE-----LSGGELQRVA 222
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1105531442 223 IGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKgNRLVLISLH 270
Cdd:PRK13409 223 IAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEH 269
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
205-267 |
2.90e-03 |
|
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: 40.77 E-value: 2.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1105531442 205 VGNTYVR------GVSGGERRRVSIGVQLL---WNPGILILDEPTSGLDSFTAHNLVTTLSRL-AKGNRLVLI 267
Cdd:TIGR00630 816 VGLGYIRlgqpatTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLvDKGNTVVVI 888
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
174-272 |
2.94e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 174 RLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNTYVRGVSGGERRRVSIGVQLL---WNPGILILDEPTSGLDSFTAHN 250
Cdd:pfam13304 198 NLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRR 277
|
90 100
....*....|....*....|..
gi 1105531442 251 LVTTLSRLAKGNRLVLISLHQP 272
Cdd:pfam13304 278 LLELLKELSRNGAQLILTTHSP 299
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
214-283 |
3.20e-03 |
|
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: 39.55 E-value: 3.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1105531442 214 SGGERRRV----SIGVQLLwnpGIL-ILDEPTSGLDSFTAHNLVTTLSRL-AKGNRLVLISlHQPrsDIFRLFDLV 283
Cdd:cd03270 139 SGGEAQRIrlatQIGSGLT---GVLyVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVE-HDE--DTIRAADHV 208
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
210-245 |
3.26e-03 |
|
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: 39.70 E-value: 3.26e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1105531442 210 VRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 245
Cdd:cd03237 113 VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
185-291 |
4.85e-03 |
|
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: 40.15 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 185 DKRVEDViaelrLRQCANTRVGNTY------------------VRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 246
Cdd:COG1245 415 DGTVEEF-----LRSANTDDFGSSYykteiikplgleklldknVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1105531442 247 TAHNLVTTLSRLAKGN-RLVLISLHqprsDIFrLFDLV---LLMTSGTP 291
Cdd:COG1245 490 QRLAVAKAIRRFAENRgKTAMVVDH----DIY-LIDYIsdrLMVFEGEP 533
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
160-265 |
4.90e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1105531442 160 NLTVRETLAFIAQMRLPrtfsqAQRDKRVEDVIAEL--RLRQCANtrVGNTYV------RGVSGGERRRV----SIGVQL 227
Cdd:COG0178 432 ALSIDEALEFFENLELT-----EREAEIAERILKEIrsRLGFLVD--VGLDYLtldrsaGTLSGGEAQRIrlatQIGSGL 504
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1105531442 228 LwnpGIL-ILDEPTSGL---DSftaHNLVTTLSRLAK-GNRLV 265
Cdd:COG0178 505 V---GVLyVLDEPSIGLhqrDN---DRLIETLKRLRDlGNTVI 541
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
209-244 |
8.46e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.41 E-value: 8.46e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1105531442 209 YVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLD 244
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
213-270 |
9.55e-03 |
|
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: 37.55 E-value: 9.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1105531442 213 VSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLA-KGNRLVLISLH 270
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeEGKKTALVVEH 130
|
|
| |
