|
Name |
Accession |
Description |
Interval |
E-value |
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
64-299 |
2.12e-122 |
|
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: 363.13 E-value: 2.12e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 64 SQVPWFEQLAQFKMpwtspscQNSCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKSGQIWINGQPS 143
Cdd:cd03234 2 RVLPWWDVGLKAKN-------WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 144 SPQLVRKCVAHVRQHNQLLPNLTVRETLAFIAQMRLPRTFSQAQRDKRVEDViaelRLRQCADTRVGNMYVRGLSGGERR 223
Cdd:cd03234 75 KPDQFQKCVAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDV----LLRDLALTRIGGNLVKGISGGERR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 224 RVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03234 151 RVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
92-667 |
1.47e-111 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 349.35 E-value: 1.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKSGQIWINGQPSSPQLVRKCVAHVRQHNQLLPNLTVRETL 171
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNM-YVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 250
Cdd:TIGR00955 121 MFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 251 TAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQYFTAIGYPCPRYSNPADFYVDLTS 330
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 331 IDRRSREQELATREK-AQSLAALFLEKVRDLDDFLWKAETKDLDEDTCVESSVtpldtnclpspTKMPGAVQQFTTLIRR 409
Cdd:TIGR00955 281 VIPGSENESRERIEKiCDSFAVSDIGRDMLVNTNLWSGKAGGLVKDSENMEGI-----------GYNASWWTQFYALLKR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 410 QISNDFRDLPTLLIHGAEACLMSMTIGFLYFGHGSIQLSFMDTAALLFMIGALIPFNVILDVISKCYSERAMLYYELEDG 489
Cdd:TIGR00955 350 SWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 490 LYTTGPYFFAKILGELPEHCAYIIIYGMPTYWLANLRPGLQPFLLHFLLVWLVVFCCRIMALAAAALLPTFHMASFFSNA 569
Cdd:TIGR00955 430 LYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPP 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 570 LYNSFYLAGGFMINLSSlwtVPA---WISKVSFLRWCFEGLMKIQFSRRTYKMPLGNLTIAV---SGDKILSVMELDSYP 643
Cdd:TIGR00955 510 FVIPFLLFGGFFINSDS---IPVyfkWLSYLSWFRYGNEGLLINQWSDVDNIECTSANTTGPcpsSGEVILETLSFRNAD 586
|
570 580
....*....|....*....|....
gi 767915028 644 LYAIYLIVIGLSGGFMVLYYVSLR 667
Cdd:TIGR00955 587 LYLDLIGLVILIFFFRLLAYFALR 610
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
64-299 |
4.20e-80 |
|
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: 252.47 E-value: 4.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 64 SQVPWFEQLAQFKMPWTSpscqNSCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIkSGQIWINGQPS 143
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPS----KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV-SGEVLINGRPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 144 SPQLVRKCVAHVRQHNQLLPNLTVRETLAFIAQMRlprtfsqaqrdkrvedviaelrlrqcadtrvgnmyvrGLSGGERR 223
Cdd:cd03213 76 DKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGERK 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 224 RVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
102-612 |
1.15e-73 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 250.57 E-value: 1.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 102 GQMLAIIGSSGCGRASLLDVITGRGHGGKIkSGQIWINGQPSSPQLVRKcVAHVRQHNQLLPNLTVRETLAFIAQMRLPR 181
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNF-TGTILANNRKPTKQILKR-TGFVTQDDILYPHLTVRETLVFCSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 182 TFSQAQRDKRVEDVIAELRLRQCADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSR 261
Cdd:PLN03211 172 SLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 262 LAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQYFTAIGYPCPRYSNPADFYVDLTS----IDRRS-R 336
Cdd:PLN03211 252 LAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANgvcqTDGVSeR 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 337 EQELATREKAQSLAALFLEKVRD---LDDFLW-KAETKDLDEDTCVESSvtplDTNCLPSptkmpgAVQQFTTLIRRQIS 412
Cdd:PLN03211 332 EKPNVKQSLVASYNTLLAPKVKAaieMSHFPQaNARFVGSASTKEHRSS----DRISIST------WFNQFSILLQRSLK 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 413 N-DFRDLPTLLIHgaeACLMSMTIGFLYFGHgSIQLSFMDTAALLFMI----GALIPFNVILDVIskcySERAMLYYELE 487
Cdd:PLN03211 402 ErKHESFNTLRVF---QVIAAALLAGLMWWH-SDFRDVQDRLGLLFFIsifwGVFPSFNSVFVFP----QERAIFVKERA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 488 DGLYTTGPYFFAKILGELPEHCAYIIIYGMPTYWLANLRPGLQPFLLHFLLVWLVVFCCRIMALAAAALLPTFHMASFFS 567
Cdd:PLN03211 474 SGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIV 553
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 767915028 568 NALYNSFYLAGGFMINlsSLWTVPAWISKVSFLRWCFEGLMKIQF 612
Cdd:PLN03211 554 TVTMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYRLLINVQY 596
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
99-615 |
2.64e-56 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 207.65 E-value: 2.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 99 VRSGQMLAIIGSSGCGRASLLDVITGRGHGGKI-KSGQIWINGQPSS---PQLvRKCVAHVRQHNQLLPNLTVRETLAFI 174
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIgVEGVITYDGITPEeikKHY-RGDVVYNAETDVHFPHLTVGETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 175 AQMRLPRT----FSQAQRDKRVEDVI-AELRLRQCADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 249
Cdd:TIGR00956 163 ARCKTPQNrpdgVSREEYAKHIADVYmATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 250 FTAHNLVKTLSRLAK-GNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQYFTAIGYPCPRYSNPADFyvdL 328
Cdd:TIGR00956 243 ATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADF---L 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 329 TSIDRRSREQELATREKAQSLAALFLEK-----------VRDLDDFLWKAETKDLDEdTCVESSVTPLDTNCLPSPTKMP 397
Cdd:TIGR00956 320 TSLTSPAERQIKPGYEKKVPRTPQEFETywrnspeyaqlMKEIDEYLDRCSESDTKE-AYRESHVAKQSKRTRPSSPYTV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 398 GAVQQFTTLIRRQISNDFRDLPTLLIHGAEACLMSMTIGFLYFghgSIQlsfMDTAALLFMIGAL---IPFNVI--LDVI 472
Cdd:TIGR00956 399 SFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFY---NLP---KNTSDFYSRGGALffaILFNAFssLLEI 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 473 SKCYSERAMLYYELEDGLYTTGPYFFAKILGELPEHCAYIIIYGMPTYWLANLRPGLQPFLLHFLLVWLVVFCCRIMALA 552
Cdd:TIGR00956 473 ASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRS 552
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915028 553 AAALLPTFHMASFFSNALYNSFYLAGGFMINLSSLWTVPAWISKVSFLRWCFEGLMKIQFSRR 615
Cdd:TIGR00956 553 IGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGR 615
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
99-611 |
4.27e-49 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 186.08 E-value: 4.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 99 VRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKSGQIWINGQPSSPQLVRKcVAHVRQHNQLLPNLTVRETLAFIAQMR 178
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRS-IGYVQQQDLHLPTSTVRESLRFSAYLR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 179 LPRTFSQAQRDKRVEDVIAELRLRQCADTRVGnMYVRGLSGGERRRVSIGVQLLWNPGILI-LDEPTSGLDSFTAHNLVK 257
Cdd:TIGR00956 865 QPKSVSKSEKMEYVEEVIKLLEMESYADAVVG-VPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 258 TLSRLAKGNRLVLISLHQPRSDIFRLFD-LVLLMTSGTPIYLG----AAQHMVQYFTAIGYP-CPRYSNPADFYVDLTSI 331
Cdd:TIGR00956 944 LMRKLADHGQAILCTIHQPSAILFEEFDrLLLLQKGGQTVYFGdlgeNSHTIINYFEKHGAPkCPEDANPAEWMLEVIGA 1023
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 332 DRRSR-EQELATREKAQSLAALFLEKVRDLDDFLWKAETKDLDEDtcvessvtpldtnclPSPTKMPGAvQQFTTLIRRQ 410
Cdd:TIGR00956 1024 APGAHaNQDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDA---------------LSKYAASLW-YQFKLVLWRT 1087
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 411 ISNDFRDLPTLLIHGAEACLMSMTIGFLYF--GHGSIQLsfmdTAALLFMIGALIPFNVILDVISKCY--SERAMLYYEL 486
Cdd:TIGR00956 1088 FQQYWRTPDYLYSKFFLTIFAALFIGFTFFkvGTSLQGL----QNQMFAVFMATVLFNPLIQQYLPPFvaQRDLYEVRER 1163
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 487 EDGLYTTGPYFFAKILGELPEHC-----AYIIIY-GMPTYWLANLRPGLQPfllHFLLVWLVVFCCRI----MALAAAAL 556
Cdd:TIGR00956 1164 PSRTFSWLAFIAAQITVEIPYNLvagtiFFFIWYyPVGFYWNASKTGQVHE---RGVLFWLLSTMFFLyfstLGQMVISF 1240
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 557 LPTFHMASFFSNALYNSFYLAGGFMINLSSL---WTvpaWISKVSFLRWCFEGLMKIQ 611
Cdd:TIGR00956 1241 NPNADNAAVLASLLFTMCLSFCGVLAPPSRMpgfWI---FMYRCSPFTYLVQALLSTG 1295
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
100-612 |
1.38e-44 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 172.34 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 100 RSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKsGQIWINGQPSSPQLVRKCVAHVRQHNQLLPNLTVRETLAFIAQMRL 179
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIE-GDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRL 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 180 PRTFSQAQRDKRVEDVIAELRLRQCADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTL 259
Cdd:PLN03140 983 PKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 260 SRLAKGNRLVLISLHQPRSDIFRLFDLVLLMT-SGTPIYLGA----AQHMVQYFTAI-GYP-CPRYSNPADFYVDLTSID 332
Cdd:PLN03140 1063 RNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKrGGQVIYSGPlgrnSHKIIEYFEAIpGVPkIKEKYNPATWMLEVSSLA 1142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 333 RRSR-EQELATREKAQSLAALFLEKVRDLDdfLWKAETKDLDEDTCVESSVTPLDTNCLpsptkmpgaVQQFTTLIRRQI 411
Cdd:PLN03140 1143 AEVKlGIDFAEHYKSSSLYQRNKALVKELS--TPPPGASDLYFATQYSQSTWGQFKSCL---------WKQWWTYWRSPD 1211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 412 SNDFRDLPTLLihgaeACLMsmtIGFLYFGHGSIQLSFMDtaaLLFMIGALIPfNVILDVISKCYS-------ERAMLYY 484
Cdd:PLN03140 1212 YNLVRFFFTLA-----AALM---VGTIFWKVGTKRSNAND---LTMVIGAMYA-AVLFVGINNCSTvqpmvavERTVFYR 1279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 485 ELEDGLYTTGPYFFAKILGELPE---HCAY--IIIYGMPTY-WLAnlrpglQPFLLHFLLVWLVVFCCRIMALAAAALLP 558
Cdd:PLN03140 1280 ERAAGMYSALPYAIAQVVCEIPYvliQTTYytLIVYAMVAFeWTA------AKFFWFYFISFFSFLYFTYYGMMTVSLTP 1353
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 559 TFHMASFFSNALYNSFYLAGGFMI---NLSSLWTVPAWISKVSflrWCFEGLMKIQF 612
Cdd:PLN03140 1354 NQQVAAIFAAAFYGLFNLFSGFFIprpKIPKWWVWYYWICPVA---WTVYGLIVSQY 1407
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
92-299 |
2.31e-44 |
|
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: 157.40 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKsGQIWINGQPSSPQLVRKcVAHVRQHNQLLPNLTVRETL 171
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVIT-GEILINGRPLDKNFQRS-TGYVEQQDVHSPNLTVREAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAqmrlprtfsqaqrdkrvedviaelrlrqcadtrvgnmYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 251
Cdd:cd03232 101 RFSA-------------------------------------LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767915028 252 AHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTS-GTPIYLG 299
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
92-299 |
1.37e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 142.90 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkIK--SGQIWINGQP--SSPQLVRKCVAHVRQHNQLLPNLTV 167
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL-----LRptSGEVRVLGEDvaRDPAEVRRRIGYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:COG1131 91 RENLRFFARLYgLPR----KEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767915028 247 LDSFTAHNLVKTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:COG1131 162 LDPEARRELWELLRELAAEGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
92-245 |
1.83e-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: 136.62 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQPSSP---QLVRKCVAHVRQHNQLLPNLTVR 168
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP---TEGTILLDGQDLTDderKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 169 ETLAFIAQMRLPrtfSQAQRDKRVEDVIAELRLRQCADTRVGNmYVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:pfam00005 78 ENLRLGLLLKGL---SKREKDARAEEALEKLGLGDLADRPVGE-RPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
91-302 |
1.26e-36 |
|
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: 137.30 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPS--SPQLVRKCVAHVRQHNQLLPNLTVR 168
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL---KPDSGSILIDGEDVrkEPREARRQIGVLPDERGLYDRLTVR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIA-QMRLPRtfsqAQRDKRVEDVIAELRLRQCADTRVGnmyvrGLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:COG4555 93 ENIRYFAeLYGLFD----EELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 248 DSFTAHNLVKTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSGTPIYLGAAQ 302
Cdd:COG4555 164 DVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLD 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
92-303 |
6.76e-35 |
|
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: 131.86 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP--SSPQLVRKCVAHVRQHNQLLPNLTVRE 169
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL---RPTSGTAYINGYSirTDRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAFIAQMR-LPRTfsqaQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03263 95 HLRFYARLKgLPKS----EIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 249 SFTAHNLVKTLSRLaKGNRLVLISLHQPRsDIFRLFDLVLLMTSGTPIYLGAAQH 303
Cdd:cd03263 166 PASRRAIWDLILEV-RKGRSIILTTHSMD-EAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
92-299 |
4.26e-34 |
|
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: 128.92 E-value: 4.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKSGQIWINGQPSSpQLVRKC---VAHVRQHNQLLPNLTVR 168
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYK-EFAEKYpgeIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMRlprtfsqaqrdkrvedviaelrlrqcadtrvGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03233 102 ETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915028 249 SFTAHNLVKTLSRLAKGNRLV-LISLHQPRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
92-294 |
3.53e-33 |
|
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: 126.81 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP---SSPQLVRKCVAHVRQH--NQLLpNLT 166
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL---GPTSGEVLVDGKDltkLSLKELRRKVGLVFQNpdDQFF-GPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAF-IAQMRLPRtfsqAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:cd03225 93 VEEEVAFgLENLGLPE----EEIEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSGT 294
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
92-305 |
4.83e-31 |
|
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: 122.07 E-value: 4.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP----SSPQLVRKcVAHVRQHNQLLPNLTV 167
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLL---KPSSGEVLLDGRDlaslSRRELARR-IAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAF--IAQMRLPRTFSQAQRDKrVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIG---VQllwNPGILILDE 242
Cdd:COG1120 93 RELVALgrYPHLGLFGRPSAEDREA-VEEALERTGLEHLADRPVDE-----LSGGERQRVLIAralAQ---EPPLLLLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 243 PTSGLDsfTAH-----NLVKTLSRlaKGNRLVLISLHqprsDI---FRLFDLVLLMTSGTPIYLGAAQHMV 305
Cdd:COG1120 164 PTSHLD--LAHqlevlELLRRLAR--ERGRTVVMVLH----DLnlaARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
406-610 |
1.07e-30 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 119.30 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 406 LIRRQISNDFRDLPTLLIHGAEACLMSMTIGFLYFGHGSiQLSFMDTAALLFMIGALIPFNVILDVISKCYSERAMLYYE 485
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGN-QQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 486 LEDGLYTTGPYFFAKILGELPEHCAYIIIYGMPTYWLANLRPGLQPFLLHFLLVWLVVFCCRIMALAAAALLPTFHMASF 565
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767915028 566 FSNALYNSFYLAGGFMINLSSLWTVPAWISKVSFLRWCFEGLMKI 610
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
92-302 |
1.20e-30 |
|
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: 120.13 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkI---KSGQIWINGQPsspqLVRKCVAHVRQH---------N 159
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG------LlkpTSGEVLVDGKD----ITKKNLRELRRKvglvfqnpdD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 160 QLLpNLTVRETLAF-IAQMRLPRtfsqAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSI-GVqLLWNPGI 237
Cdd:COG1122 87 QLF-APTVEEDVAFgPENLGLPR----EEIRERVEEALELVGLEHLADRPPHE-----LSGGQKQRVAIaGV-LAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 238 LILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRsDIFRLFDLVLLMTSGTPIYLGAAQ 302
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
92-294 |
1.33e-30 |
|
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: 117.35 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPqlvrkcvahvrqhnqlLPNLTVRETL 171
Cdd:cd00267 15 LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL---KPTSGEILIDGKDIAK----------------LPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAQmrlprtfsqaqrdkrvedviaelrlrqcadtrvgnmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 251
Cdd:cd00267 76 GYVPQ----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915028 252 AHNLVKTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSGT 294
Cdd:cd00267 116 RERLLELLRELAEEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
92-303 |
2.21e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggKIK--SGQIWINGQPssPQLVRKCVAHVRQHNQLLPN--LTV 167
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILG-----LLPptSGTVRLFGKP--PRRARRRIGYVPQRAEVDWDfpITV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLA--FIAQMRLPRTFSQAQRDkRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:COG1121 95 RDVVLmgRYGRRGLFRRPSRADRE-AVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMtSGTPIYLGAAQH 303
Cdd:COG1121 169 GVDAATEEALYELLRELRREGKTILVVTHDL-GAVREYFDRVLLL-NRGLVAHGPPEE 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
94-299 |
3.08e-30 |
|
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: 118.55 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVrSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIK-SGQIWINGQPS---SPQlvRKCVAHVRQHNQLLPNLTV 167
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGleKPDGGTIVlNGTVLFDSRKKinlPPQ--QRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFIAqmrlpRTFSQAQRDKRVEDVIAELRLRQcadtrVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:cd03297 93 RENLAFGL-----KRKRNREDRISVDELLDLLGLDH-----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767915028 248 DSFTAHNLVKTLSRLAKG-NRLVLISLHQPrSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03297 163 DRALRLQLLPELKQIKKNlNIPVIFVTHDL-SEAEYLADRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
83-276 |
7.21e-30 |
|
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: 117.19 E-value: 7.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 83 SCQN-SCELG----IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP--SSPQLVRKCVAHV 155
Cdd:COG4133 4 EAENlSCRRGerllFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLL---PPSAGEVLWNGEPirDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 156 RQHNQLLPNLTVRETLAFIAQMRlprtfSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNP 235
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALY-----GLRADREAIDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767915028 236 GILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQP 276
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
90-299 |
7.68e-30 |
|
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: 117.29 E-value: 7.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 90 LGIQNLSFKVRSGQ------------MLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP--SSPQLVRKCVAHV 155
Cdd:cd03264 1 LQLENLTKRYGKKRaldgvsltlgpgMYGLLGPNGAGKTTLMRILATLT---PPSSGTIRIDGQDvlKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 156 RQHNQLLPNLTVRETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQCADTRVGnmyvrGLSGGERRRVSIGVQLLWNP 235
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 236 GILILDEPTSGLD-----SFtaHNLvktLSRLAKgNRLVLISLHQpRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03264 150 SILIVDEPTAGLDpeeriRF--RNL---LSELGE-DRIVILSTHI-VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
92-293 |
1.01e-28 |
|
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: 114.15 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP-SSPQLVRKCVAHVRQHNQLLPNLTVRET 170
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE---RPDSGEILIDGRDvTGVPPERRNIGMVFQDYALFPHLTVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 LAFiaQMRLpRTFSQAQRDKRVEDVIAELRLRqcadtRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 250
Cdd:cd03259 93 IAF--GLKL-RGVPKAEIRARVRELLELVGLE-----GLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915028 251 TAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSG 293
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
92-294 |
1.22e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.76 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHggkikSGQIWINGQP---SSPQLVRKCVAHVRQHNQLLPNlT 166
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADldPPT-----SGEIYLDGKPlsaMPPPEWRRQVAYVPQEPALWGG-T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFIAQMRlprtfSQAQRDKRVEDVIAELRLRQ-CADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:COG4619 90 VRDNLPFPFQLR-----ERKFDRERALELLERLGLPPdILDKPVER-----LSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNR--LVLISlHQPRsDIFRLFDLVLLMTSGT 294
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGraVLWVS-HDPE-QIERVADRVLTLEAGR 208
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
92-299 |
1.25e-28 |
|
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: 113.78 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggKIK--SGQIWINGQPssPQLVRKCVAHVRQHNQLLPN--LTV 167
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILG-----LLKptSGSIRVFGKP--LEKERKRIGYVPQRRSIDRDfpISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RET--LAFIAQMRLPRTFSQAQRDKrVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:cd03235 88 RDVvlMGLYGHKGLFRRLSKADKAK-VDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSdIFRLFDLVLLMTsGTPIYLG 299
Cdd:cd03235 162 GVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
92-303 |
1.66e-28 |
|
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: 114.07 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggKIK--SGQIWINGQP----SSPQLVRKCVAHVRQHNQLLPNL 165
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISG-----FLRptSGSVLFDGEDitglPPHEIARLGIGRTFQIPRLFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQMRLPRTFSQAQR-------DKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGIL 238
Cdd:cd03219 91 TVLENVMVAAQARTGSGLLLARArreereaRERAEELLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 239 ILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHqprsD---IFRLFDLVLLMTSGTPIYLGAAQH 303
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRERGITVLLVEH----DmdvVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
92-293 |
1.83e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.60 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGG--KIKSGQIWINGQP----SSPQLV---RKCVAHVRQHNQLL 162
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL-----GGldRPTSGEVLIDGQDisslSERELArlrRRHIGFVFQFFNLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLAFIAqmrLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:COG1136 99 PELTALENVALPL---LLAGVSRKERRERARELLERVGLGDRLDHRPSQ-----LSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLAK-GNRLVLISLHQPRsdIFRLFDLVLLMTSG 293
Cdd:COG1136 171 PTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDPE--LAARADRVIRLRDG 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
92-293 |
3.13e-28 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 112.97 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSS-------PQLVRKCVAHVRQHNQLLPN 164
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLD---RPTSGEVRVDGTDISklsekelAAFRRRHIGFVFQSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:cd03255 97 LTALENVELPLLLA---GVPKKERRERAEELLERVGLGDRLNHYPSE-----LSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915028 245 SGLDSFTAHNLVKTLSRLAKG-NRLVLISLHQPrsDIFRLFDLVLLMTSG 293
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEaGTTIVVVTHDP--ELAEYADRIIELRDG 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
92-296 |
8.41e-28 |
|
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: 118.32 E-value: 8.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP---SSPQLVRKCVAHVRQHNQLLPnLTVR 168
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL---PPYSGSILINGVDlsdLDPASWRRQIAWVPQNPYLFA-GTIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAF------IAQMRlprtfsQAQRDKRVEDVIAelRLRQCADTRVGNmYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:COG4988 429 ENLRLgrpdasDEELE------AALEAAGLDEFVA--ALPDGLDTPLGE-GGRGLSGGQAQRLALARALLRDAPLLLLDE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLAKGnRLVLISLHQPrSDIfRLFDLVLLMTSGTPI 296
Cdd:COG4988 500 PTAHLDAETEAEILQALRRLAKG-RTVILITHRL-ALL-AQADRILVLDDGRIV 550
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
92-293 |
3.05e-27 |
|
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: 108.24 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP---SSPQLVRKCVAHVRQHNQLLpNLTVR 168
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY---DPTSGEILIDGVDlrdLDLESLRKNIAYVPQDPFLF-SGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLafiaqmrlprtfsqaqrdkrvedviaelrlrqcadtrvgnmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03228 94 ENI---------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767915028 249 SFTAHNLVKTLSRLAKGnRLVLISLHQPRSdiFRLFDLVLLMTSG 293
Cdd:cd03228 129 PETEALILEALRALAKG-KTVIVIAHRLST--IRDADRIIVLDDG 170
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
92-293 |
3.41e-27 |
|
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: 108.25 E-value: 3.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkIK--SGQIWINGQP--SSPQLVRKCVAHVRQHNQLLPNLTV 167
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL-----LKpdSGEIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAfiaqmrlprtfsqaqrdkrvedviaelrlrqcadtrvgnmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:cd03230 91 RENLK--------------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915028 248 DSFTAHNLVKTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSG 293
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHIL-EEAERLCDRVAILNNG 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
94-294 |
1.23e-26 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 106.89 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP------SSPQLVRKcVAHVRQHNQLLPNLTV 167
Cdd:cd03229 18 DVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE---EPDSGSILIDGEDltdledELPPLRRR-IGMVFQDFALFPHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFiaqmrlprtfsqaqrdkrvedviaelrlrqcadtrvgnmyvrGLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:cd03229 94 LENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915028 248 DSFTAHNLVKTLSRL-AKGNRLVLISLHQPRsDIFRLFDLVLLMTSGT 294
Cdd:cd03229 132 DPITRREVRALLKSLqAQLGITVVLVTHDLD-EAARLADRVVVLRDGK 178
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
92-299 |
2.17e-26 |
|
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: 107.94 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQ----PSSPQLVrkcvahVRQHNQLLPNLTV 167
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLA---QPTSGGVILEGKqitePGPDRMV------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAfIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:TIGR01184 72 RENIA-LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915028 248 DSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
99-345 |
3.52e-26 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 114.94 E-value: 3.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 99 VRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKSGQIWINGQPSSPQLVRKCVAHVRQHNQLLPNLTVRETLAFIAQMR 178
Cdd:PLN03140 188 IKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKETLDFSARCQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 179 -----------LPR------TFSQAQRDKRVEDVIAE--------------LRLRQCADTRVGNMYVRGLSGGERRRVSI 227
Cdd:PLN03140 268 gvgtrydllseLARrekdagIFPEAEVDLFMKATAMEgvksslitdytlkiLGLDICKDTIVGDEMIRGISGGQKKRVTT 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 228 GVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNR-LVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQ 306
Cdd:PLN03140 348 GEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILLSEGQIVYQGPRDHILE 427
|
250 260 270
....*....|....*....|....*....|....*....
gi 767915028 307 YFTAIGYPCPRYSNPADFYVDLTSidRRSREQELATREK 345
Cdd:PLN03140 428 FFESCGFKCPERKGTADFLQEVTS--KKDQEQYWADRNK 464
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
91-290 |
3.60e-26 |
|
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: 113.15 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGkikSGQIWINGQP---SSPQLVRKCVAHVRQHNQLLPNlTV 167
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIAVNGVPladADADSWRDQIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRlrQCADTRVGNmYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:TIGR02857 413 AENIRLARPDASDAEIREALERAGLDEFVAALP--QGLDTPIGE-GGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915028 248 DSFTAHNLVKTLSRLAKGnRLVLISLHQPRSdiFRLFDLVLLM 290
Cdd:TIGR02857 490 DAETEAEVLEALRALAQG-RTVLLVTHRLAL--AALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
92-271 |
3.75e-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: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLL-------DVitgrghggkiKSGQIWINGQP-SSPQL--VRKCVAHVRQhNQL 161
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILrllfrfyDV----------SSGSILIDGQDiREVTLdsLRRAIGVVPQ-DTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 162 LPNLTVRETLAFiaqMRLPRTFSQ---AQRDKRVEDVIaeLRLRQCADTRVGNmyvRG--LSGGERRRVSIGVQLLWNPG 236
Cdd:cd03253 86 LFNDTIGYNIRY---GRPDATDEEvieAAKAAQIHDKI--MRFPDGYDTIVGE---RGlkLSGGEKQRVAIARAILKNPP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 767915028 237 ILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLI 271
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
92-272 |
5.35e-26 |
|
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: 106.82 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSP------QLVRKCVAHVRQH--NQLLP 163
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL---KPTSGSIIFDGKDLLKlsrrlrKIRRKEIQMVFQDpmSSLNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVRETLAFIAQMRLPRTfSQAQRDKRVEDVIAELRLrqcaDTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEP 243
Cdd:cd03257 98 RMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGL----PEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190
....*....|....*....|....*....|.
gi 767915028 244 TSGLDSFTAHNLVKTLSRLAK--GNRLVLIS 272
Cdd:cd03257 173 TSALDVSVQAQILDLLKKLQEelGLTLLFIT 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
92-292 |
1.47e-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: 105.25 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQLVRkcVAHVRQHNQLLPNLTVRETL 171
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLE---RPTSGEVLVDGEPVTGPGPD--RGYVFQQDALLPWLTVLDNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAQMRLPRTfsqAQRDKRVEDVIAELRLrqcadTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 251
Cdd:cd03293 95 ALGLELQGVPK---AEARERAEELLELVGL-----SGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915028 252 AHNLVKTLSRLAKGNRL--VLISlHqprsDI---FRLFDLVLLMTS 292
Cdd:cd03293 167 REQLQEELLDIWRETGKtvLLVT-H----DIdeaVFLADRVVVLSA 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
92-306 |
1.95e-25 |
|
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: 111.01 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RghggKIKSGQIWINGQPS---SPQLVRKCVAHVRQHNQLLpNLTV 167
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRfL----DPQSGSITLGGVDLrdlDEDDLRRRIAVVPQRPHLF-DTTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFI------AQMRlprtfsQAQRDKRVEDVIAelRLRQCADTRVGNmYVRGLSGGERRRVSIGVQLLWNPGILILD 241
Cdd:COG4987 426 RENLRLArpdatdEELW------AALERVGLGDWLA--ALPDGLDTWLGE-GGRRLSGGERRRLALARALLRDAPILLLD 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 242 EPTSGLDSFTAHNLVKTLSRLAKGNRLVLISlHQPRSdiFRLFDLVLLMTSGTPIYLGAAQHMVQ 306
Cdd:COG4987 497 EPTEGLDAATEQALLADLLEALAGRTVLLIT-HRLAG--LERMDRILVLEDGRIVEQGTHEELLA 558
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
92-302 |
2.62e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 105.58 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHggkikSGQIWINGQP---SSPQLVRKCVAHVRQHNQLLPNLT 166
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGelTPS-----SGEVRLNGRPlaaWSPWELARRRAVLPQHSSLAFPFT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VREtlafIAQM-RLPRTFSQAQRDKRVEDViaeLRLRQCADTRvGNMYvRGLSGGERRRVsigvQL------LWN----- 234
Cdd:COG4559 92 VEE----VVALgRAPHGSSAAQDRQIVREA---LALVGLAHLA-GRSY-QTLSGGEQQRV----QLarvlaqLWEpvdgg 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 235 PGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHqprsdifrlfDL---------VLLMTSGTPIYLGAAQ 302
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH----------DLnlaaqyadrILLLHQGRLVAQGTPE 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
92-299 |
2.77e-25 |
|
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: 105.17 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggKIKSGQIWINGQP---SSPQLVRKCVAHV--RQHNQLLPNLT 166
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP--PTYGNDVRLFGERrggEDVWELRKRIGLVspALQLRFPRDET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETL--AFIAQMRLPRTFSQAQRDkRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:COG1119 97 VLDVVlsGFFDSIGLYREPTDEQRE-RARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 245 SGLDSFTAHNLVKTLSRLAKGNR--LVLISlHQPrSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGAptLVLVT-HHV-EEIPPGITHVLLLKDGRVVAAG 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
92-303 |
4.04e-25 |
|
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: 105.12 E-value: 4.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkIK--SGQIWINGQP----SSPQLVRKCVAhvR--QHNQLLP 163
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF-----YRptSGRILFDGRDitglPPHRIARLGIA--RtfQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVRE--TLAFIAQMR------LPRTFSQAQRDK----RVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQL 231
Cdd:COG0411 93 ELTVLEnvLVAAHARLGrgllaaLLRLPRARREEReareRAEELLERVGLADRADEPAGN-----LSYGQQRRLEIARAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 232 LWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRL--VLISlHqprsD---IFRLFD--LVL----LMTSGTP----- 295
Cdd:COG0411 168 ATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGItiLLIE-H----DmdlVMGLADriVVLdfgrVIAEGTPaevra 242
|
250
....*....|....
gi 767915028 296 ------IYLGAAQH 303
Cdd:COG0411 243 dprvieAYLGEEAA 256
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
84-299 |
4.99e-25 |
|
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: 103.95 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 84 CQNSCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQ---PSSPQlvRKCVAHVRQHNQ 160
Cdd:cd03299 7 SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFI---KPDSGKILLNGKditNLPPE--KRDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 161 LLPNLTVRETLAFiaQMRLpRTFSQAQRDKRVEDVIAELRLRQcadtrVGNMYVRGLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:cd03299 82 LFPHMTVYKNIAY--GLKK-RKVDKKEIERKVLEIAEMLGIDH-----LLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 241 DEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
92-293 |
5.34e-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: 104.79 E-value: 5.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGGKIK--SGQIWINGQPSSPQLVRkcVAHVRQHNQLLPNLTVRE 169
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLI-----AGLEKptSGEVLVDGKPVTGPGPD--RGVVFQEPALLPWLTVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:COG1116 100 NVALGLELRgVPK----AERRERARELLELVGLAGFEDA-----YPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915028 249 SFTAHNLVKTLSRLAKGNRL--VLISlHqprsDIF---RLFDLVLLMTSG 293
Cdd:COG1116 171 ALTRERLQDELLRLWQETGKtvLFVT-H----DVDeavFLADRVVVLSAR 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
93-306 |
1.02e-24 |
|
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: 103.35 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGGKIK--SGQIWINGQP----SSPQL--VRKCVAHVRQHNQLLPN 164
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLI-----VGLLRpdSGEVLIDGEDisglSEAELyrLRRRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFiaQMRLPRTFSQAQRDKRVEDVIAELRLRQCADtrvgnMYVRGLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:cd03261 92 LTVFENVAF--PLREHTRLSEEEIREIVLEKLEAVGLRGAED-----LYPAELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 245 SGLDSFTA---HNLVKTLSRlAKGNRLVLISlHQpRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQ 306
Cdd:cd03261 165 AGLDPIASgviDDLIRSLKK-ELGLTSIMVT-HD-LDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
92-293 |
1.64e-24 |
|
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: 108.77 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RghggKIKSGQIWINGQPS---SPQLVRKCVAHVRQHNQLLpNLTV 167
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlY----EPTSGRILIDGIDLrqiDPASLRRQIGVVLQDVFLF-SGTI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAF------IAQMRlprtfsQAQRDKRVEDVIAELRLRqcADTRVGNMYvRGLSGGERRRVSIGVQLLWNPGILILD 241
Cdd:COG2274 566 RENITLgdpdatDEEII------EAARLAGLHDFIEALPMG--YDTVVGEGG-SNLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915028 242 EPTSGLDSFTAHNLVKTLSRLAKGNRLVLISlHqpRSDIFRLFDLVLLMTSG 293
Cdd:COG2274 637 EATSALDAETEAIILENLRRLLKGRTVIIIA-H--RLSTIRLADRIIVLDKG 685
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
92-272 |
1.89e-24 |
|
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: 107.68 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKIKSGQIWINGQPSSpQLVRKCVAHVRQH---------NQLL 162
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL---LRPTSGSILFDGKDLT-KLSRRSLRELRRRvqmvfqdpySSLN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLAFIaqMRLPRTFSQAQRDKRVEDVIAELRLrqcaDTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:COG1123 357 PRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGL----PPDLADRYPHELSGGQRQRVAIARALALEPKLLILDE 430
|
170 180 190
....*....|....*....|....*....|..
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLAKGNRL--VLIS 272
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDLQRELGLtyLFIS 462
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
92-302 |
3.91e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.16 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggKIK--SGQIWINGQPS---SPQLVRKCVAHVRQHNQLLPNLT 166
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG-----ELSpdSGEVRLNGRPLadwSPAELARRRAVLPQHSSLSFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VREtlafIAQM-RLPRTFSQAQRDKRVEDVIAELRLRQCADtRvgnmYVRGLSGGERRRVsigvQL------LWN----P 235
Cdd:PRK13548 93 VEE----VVAMgRAPHGLSRAEDDALVAAALAQVDLAHLAG-R----DYPQLSGGEQQRV----QLarvlaqLWEpdgpP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 236 GILILDEPTSGLDSFTAHNLVKTLSRLAKGNRL-VLISLHqprsdifrlfDL---------VLLMTSGTPIYLGAAQ 302
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAHERGLaVIVVLH----------DLnlaaryadrIVLLHQGRLVADGTPA 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
92-302 |
4.54e-24 |
|
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: 106.53 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR-GHGGKIkSGQIWINGQP---SSPQLVRKCVAHVRQH--NQLLPnL 165
Cdd:COG1123 22 VDGVSLTIAPGETVALVGESGSGKSTLALALMGLlPHGGRI-SGEVLLDGRDlleLSEALRGRRIGMVFQDpmTQLNP-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQMRLprtFSQAQRDKRVEDVIAELRLRqcadtRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:COG1123 100 TVGDQIAEALENLG---LSRAEARARVLELLEAVGLE-----RRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 246 GLDSFTAHNLVKTLSRLAK--GNRLVLISlHQPrSDIFRLFDLVLLMTSGTPIYLGAAQ 302
Cdd:COG1123 172 ALDVTTQAEILDLLRELQRerGTTVLLIT-HDL-GVVAEIADRVVVMDDGRIVEDGPPE 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
93-274 |
6.27e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.51 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKIKSGQIWINGQPSSpQLVRKCVAHVRQH-------NQLLPNL 165
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG---EERPTSGQVLVNGQDLS-RLKRREIPYLRRRigvvfqdFRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIaqMRLpRTFSQAQRDKRVEDVIAELRLRQCADtrvgnMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:COG2884 95 TVYENVALP--LRV-TGKSRKEIRRRVREVLDLVGLSDKAK-----ALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|..
gi 767915028 246 GLDSFTAHNLVKTLSRLakgNRL---VLISLH 274
Cdd:COG2884 167 NLDPETSWEIMELLEEI---NRRgttVLIATH 195
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
91-302 |
1.03e-23 |
|
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: 100.34 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWING------QPSSPQLVRKCVAHVRQHNQLLPN 164
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV---EPTSGSVLIDGtdinklKGKALRQLRRQIGMIFQQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRET-----LAFIAQMR-LPRTFSQAQRDKRVEdVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGIL 238
Cdd:cd03256 93 LSVLENvlsgrLGRRSTWRsLFGLFPKEEKQRALA-ALERVGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 239 ILDEPTSGLDSFTAHNLVKTLSRLAKG-NRLVLISLHQPrsDIFRLF-DLVLLMTSGTPIYLGAAQ 302
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQV--DLAREYaDRIVGLKDGRIVFDGPPA 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
92-247 |
1.53e-23 |
|
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: 99.43 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP----SSPQLVRKCVAHVRQHNQLLPNLTV 167
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL---PPRSGSIRFDGRDitglPPHERARAGIGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLafiaqmrlpRTFSQAQRDKRVEDVIAEL-----RLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:cd03224 93 EENL---------LLGAYARRRAKRKARLERVyelfpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLDE 158
|
....*
gi 767915028 243 PTSGL 247
Cdd:cd03224 159 PSEGL 163
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
92-326 |
3.28e-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: 98.95 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQPSSPQLVRK-CVAHVRQHNQLLPNLTVRET 170
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP---DSGTILFGGEDATDVPVQErNVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 LAFIAQMRlPRTF--SQAQRDKRVEDViaeLRLRQCadTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03296 95 VAFGLRVK-PRSErpPEAEIRAKVHEL---LKLVQL--DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 249 SFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGtpiylgaaqHMVQyftaIGYPCPRYSNPADFYV 326
Cdd:cd03296 169 AKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG---------RIEQ----VGTPDEVYDHPASPFV 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
94-274 |
3.61e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 98.25 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSpQLVRKCVAHVRQH-------NQLLPNLT 166
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEE---LPTSGTIRVNGQDVS-DLRGRAIPYLRRKigvvfqdFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFiaQMRLPRTFSQAQRdKRVEDVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:cd03292 95 VYENVAF--ALEVTGVPPREIR-KRVPAALELVGLSHKHRA-----LPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180
....*....|....*....|....*...
gi 767915028 247 LDSFTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
92-299 |
3.98e-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: 98.56 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQ-PSS--PQLVRKCVAHVRQHNQLLPNLTVR 168
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQP---TSGEVRVAGLvPWKrrKKFLRRIGVVFGQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMRlprtfsqaqrdkRVEDVIAELRLRQCAD----TRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:cd03267 114 DSFYLLAAIY------------DLPPARFKKRLDELSElldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 245 SGLDSFTAHNLVKTLSRLakgNRL----VLISLHQPRsDIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03267 182 IGLDVVAQENIRNFLKEY---NRErgttVLLTSHYMK-DIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
92-275 |
4.24e-23 |
|
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: 97.67 E-value: 4.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQpsSPQLVRKCVAHVR---QHNQLLPNLTVR 168
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI---KPDSGEITFDGK--SYQKNIEALRRIGaliEAPGFYPNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAqmRLPRTfsqaqRDKRVEDVIAELRLRQCADTRVGnmyvrGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03268 91 ENLRLLA--RLLGI-----RKKRIDEVLDVVGLKDSAKKKVK-----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180
....*....|....*....|....*..
gi 767915028 249 SFTAHNLVKTLSRLAKGNRLVLISLHQ 275
Cdd:cd03268 159 PDGIKELRELILSLRDQGITVLISSHL 185
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
92-293 |
4.34e-23 |
|
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: 98.42 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQ------PSSPQLVRKCVAHVRQHNQLLPNL 165
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLE---RPTSGSVLVDGTdltllsGKELRKARRRIGMIFQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAF---IAQMrlprtfSQAQRDKRVEDVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:cd03258 98 TVFENVALpleIAGV------PKAEIEERVLELLELVGLEDKADA-----YPAQLSGGQKQRVGIARALANNPKVLLCDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLAK--GNRLVLISlHQpRSDIFRLFDLVLLMTSG 293
Cdd:cd03258 167 ATSALDPETTQSILALLRDINRelGLTIVLIT-HE-MEVVKRICDRVAVMEKG 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
92-294 |
9.20e-23 |
|
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: 96.56 E-value: 9.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQLVRKCVAHVRQH--NQLLPNlTVRE 169
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI---KESSGSILLNGKPIKAKERRKSIGYVMQDvdYQLFTD-SVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAFiaqmRLPRTfsqAQRDKRVEDVIAELRLRQCADtrvgnMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 249
Cdd:cd03226 92 ELLL----GLKEL---DAGNEQAETVLKDLDLYALKE-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767915028 250 FTAHNLVKTLSRLAKGNRLVLISLHQPRSdIFRLFDLVLLMTSGT 294
Cdd:cd03226 160 KNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGA 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
92-299 |
1.01e-22 |
|
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: 95.58 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP---SSPQLVRKCVAHVRQhnqllpnltvr 168
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLL---KPSSGEILLDGKDlasLSPKELARKIAYVPQ----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 etlaFIAQMRlprtfsqaqrdkrvedvIAELRLRQCADtrvgnmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03214 81 ----ALELLG-----------------LAHLADRPFNE----------LSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 249 SFTAHNLVKTLSRLAK-GNRLVLISLHqprsDI---FRLFDLVLLMTSGTPIYLG 299
Cdd:cd03214 130 IAHQIELLELLRRLAReRGKTVVMVLH----DLnlaARYADRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
93-275 |
1.15e-22 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 96.44 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP---SSPQL--VRKCVAHVRQHNQLLPNLTV 167
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLE---EPDSGTIIIDGLKltdDKKNIneLRQKVGMVFQQFNLFPHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAfIAQMRLpRTFSQAQRDKRVEDVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:cd03262 94 LENIT-LAPIKV-KGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL 166
|
170 180
....*....|....*....|....*...
gi 767915028 248 DSFTAHNLVKTLSRLAKGNRLVLISLHQ 275
Cdd:cd03262 167 DPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
92-271 |
2.43e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.39 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RghggkIKSGQIWINGQPS---SPQLVRKCVAHVRQHNQLLpNLT 166
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyD-----PTSGRILIDGVDIrdlTLESLRRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFiaqmrlprtfsqAQRDKRVEDVIAELRLRQCA----------DTRVGNmyvRG--LSGGERRRVSIGVQLLWN 234
Cdd:COG1132 430 IRENIRY------------GRPDATDEEVEEAAKAAQAHefiealpdgyDTVVGE---RGvnLSGGQRQRIAIARALLKD 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 767915028 235 PGILILDEPTSGLDSFTAHNLVKTLSRLAKGnRLVLI 271
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMKG-RTTIV 530
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
95-299 |
6.03e-22 |
|
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: 94.74 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIWINgqpSSPQLVRKCVAHVRQHNQLLPNLTVRETLA 172
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllEPDAGFATVDGFDVV---KEPAEARRRLGFVSDSTGLYDRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 173 FIAqmRLPRTFSQAQRDkRVEDVIAELRLRQCADTRVGnmyvrGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTA 252
Cdd:cd03266 101 YFA--GLYGLKGDELTA-RLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767915028 253 HNLVKTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03266 173 RALREFIRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
85-326 |
6.29e-22 |
|
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: 96.17 E-value: 6.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 85 QNSCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSP-------QLVRKCVAHVRQ 157
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI---EPTSGKVLIDGQDIAAmsrkelrELRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 158 HNQLLPNLTVRETLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGVQLLWNPG 236
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQgVPR----AEREERAAEALELVGLEGWEHK-----YPDELSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 237 ILILDEPTSGLDSFTAHNLVKTLSRLAK--GNRLVLISlHQPrSDIFRLFDLVLLMTSGTPIYLGAAQHMVQyftaigyp 314
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDELLRLQAelQKTIVFIT-HDL-DEALRLGDRIAIMKDGRLVQVGTPEEILT-------- 250
|
250
....*....|..
gi 767915028 315 cprysNPADFYV 326
Cdd:cd03294 251 -----NPANDYV 257
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
93-261 |
6.84e-22 |
|
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: 95.05 E-value: 6.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkIK--SGQIWINGQP----SSPQL--VRKCVAHVRQHNQLLPN 164
Cdd:COG1127 22 DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL-----LRpdSGEILVDGQDitglSEKELyeLRRRIGMLFQGGALFDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFiaQMRLPRTFSQAQRDKRVEDVIAELRLRQCADtrvgnMYVRGLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:COG1127 97 LTVFENVAF--PLREHTDLSEAEIRELVLEKLELVGLPGAAD-----KMPSELSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180
....*....|....*....|
gi 767915028 245 SGLDSFTA---HNLVKTLSR 261
Cdd:COG1127 170 AGLDPITSaviDELIRELRD 189
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
92-251 |
9.55e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 95.31 E-value: 9.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkIK--SGQIWINGQP-SSPQLVRkcvAHVRQHNQLLPNLTVR 168
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGF-----LApsSGEITLDGVPvTGPGADR---GVVFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:COG4525 95 DNVAFGLRLRgVPK----AERRARAEELLALVGLADFARRRIWQ-----LSGGMRQRVGIARALAADPRFLLMDEPFGAL 165
|
....
gi 767915028 248 DSFT 251
Cdd:COG4525 166 DALT 169
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
92-274 |
9.94e-22 |
|
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: 94.60 E-value: 9.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITgRGHggKIKSGQIWINGQP----SSPQLvRKCVAHVRQhNQLLPNLTV 167
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFY--DVDSGRILIDGHDvrdyTLASL-RRQIGLVSQ-DVFLFNDTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFiaqmrlprtfsqAQRDKRVEDVIAELR----------LRQCADTRVGnmyVRG--LSGGERRRVSIGVQLLWNP 235
Cdd:cd03251 93 AENIAY------------GRPGATREEVEEAARaanahefimeLPEGYDTVIG---ERGvkLSGGQRQRIAIARALLKDP 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 767915028 236 GILILDEPTSGLDSFTAHNLVKTLSRLAKgNRLVLISLH 274
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMK-NRTTFVIAH 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
92-305 |
1.31e-21 |
|
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: 94.09 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQP---SSPQLVRKCVAHVRQHNQLLpNLTVR 168
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP---ENGRVLVDGHDlalADPAWLRRQVGVVLQENVLF-NRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQcaDTRVGNMYVrGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03252 94 DNIALADPGMSMERVIEAAKLAGAHDFISELPEGY--DTIVGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 249 SFTAHNLVKTLSRLAKGnRLVLISLHqpRSDIFRLFDLVLLMTSGTPIYLGAAQHMV 305
Cdd:cd03252 171 YESEHAIMRNMHDICAG-RTVIIIAH--RLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
92-293 |
2.14e-21 |
|
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: 93.04 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKIKSGQIWINGQPSS---PQLVRKCVAHVRQHNQLLpNLTVR 168
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL---YKPTSGSVLLDGTDIRqldPADLRRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFiaqmrlprtFSQAQRDKRVEDV-----IAELRLRQCA--DTRVGNMYvRGLSGGERRRVSIGVQLLWNPGILILD 241
Cdd:cd03245 96 DNITL---------GAPLADDERILRAaelagVTDFVNKHPNglDLQIGERG-RGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915028 242 EPTSGLDSFTAHNLVKTLSRLAKGNRLVLISlHqpRSDIFRLFDLVLLMTSG 293
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDKTLIIIT-H--RPSLLDLVDRIIVMDSG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
92-248 |
3.48e-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: 92.32 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWING------QPSspqlvRKCVAHVRQHNQLLPNL 165
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE---EPTSGRIYIGGrdvtdlPPK-----DRDIAMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQcadtrVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:cd03301 88 TVYDNIAFGLKLR---KVPKDEIDERVREVAELLQIEH-----LLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
...
gi 767915028 246 GLD 248
Cdd:cd03301 160 NLD 162
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
92-304 |
5.31e-21 |
|
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: 92.75 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVI------TgrghggkikSGQIWINGQPSS---PQLVRKCVAHVRQHNQLL 162
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrliepT---------SGEIFIDGEDIReqdPVELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLrqcADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:cd03295 88 PHMTVEENIALVPKLL---KWPKEKIRERADELLALVGL---DPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLAK--GNRLVLISlHqprsDI---FRLFDLVLLMTSGTPIYLGAAQHM 304
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQelGKTIVFVT-H----DIdeaFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
92-293 |
5.73e-21 |
|
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: 91.57 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkI---KSGQIWINGQPSSPqLVRKCVAHVRQHNQLLPNLTVR 168
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG------IilpDSGEVLFDGKPLDI-AARNRIGYLPEERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMR-LPRtfSQAQRdkRVEDVIAELRLRQCADTRVgnmyvRGLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:cd03269 89 DQLVYLAQLKgLKK--EEARR--RIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915028 248 DSFTAHNLVKTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSG 293
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKG 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
92-247 |
5.87e-21 |
|
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: 92.35 E-value: 5.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP----SSPQLVRKCVAHVRQHNQLLPNLTV 167
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLL---PPRSGSIRFDGEDitglPPHRIARLGIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLafiaQMRLPRTFSQAQRDKRVEDViAEL--RLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:COG0410 96 EENL----LLGAYARRDRAEVRADLERV-YELfpRLKERRRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
..
gi 767915028 246 GL 247
Cdd:COG0410 166 GL 167
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
93-293 |
8.06e-21 |
|
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: 92.17 E-value: 8.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHggkikSGQIWINGQPSSPQL---VRKCVAHVRQH--NQLLPNL 165
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALAGleRPW-----SGEVTFDGRPVTRRRrkaFRRRVQMVFQDpyASLHPRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAF-IAQMRLPRtfsqaqRDKRVEDVIAELRLrqcaDTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:COG1124 97 TVDRILAEpLRIHGLPD------REERIAELLEQVGL----PPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915028 245 SGLD-SFTAH--NLVKTLsRLAKGNRLVLISlHQPRSdIFRLFDLVLLMTSG 293
Cdd:COG1124 167 SALDvSVQAEilNLLKDL-REERGLTYLFVS-HDLAV-VAHLCDRVAVMQNG 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
93-276 |
8.08e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.09 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQLVRKCVAHVRQHNQLLPNLTVRETLA 172
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL---PPAAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 173 FIAQMRlprtfsqAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSfTA 252
Cdd:PRK13539 96 FWAAFL-------GGEELDIAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALDA-AA 162
|
170 180
....*....|....*....|....*.
gi 767915028 253 HNLVKTL--SRLAKGNrLVLISLHQP 276
Cdd:PRK13539 163 VALFAELirAHLAQGG-IVIAATHIP 187
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
92-274 |
1.48e-20 |
|
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: 91.06 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGR---ASLL----DVItgrghggkikSGQIWINGQPSS---PQLVRKCVAHVRQHNQL 161
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKstvVSLLerfyDPT----------SGEILLDGVDIRdlnLRWLRSQIGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 162 LPNlTVRETLAFiaqMRLPRTFSQAQRDKRV---EDVIAELRlrQCADTRVGNmyvRG--LSGGERRRVSIGVQLLWNPG 236
Cdd:cd03249 89 FDG-TIAENIRY---GKPDATDEEVEEAAKKaniHDFIMSLP--DGYDTLVGE---RGsqLSGGQKQRIAIARALLRNPK 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 767915028 237 ILILDEPTSGLDSFTAHNLVKTLSRLAKGnRLVLISLH 274
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKG-RTTIVIAH 196
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
92-262 |
1.68e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 93.62 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGG--KIKSGQIWINGQPsspqlvrkcVAHVR----------QHN 159
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMI-----AGfeTPDSGRILLDGRD---------VTGLPpekrnvgmvfQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 160 QLLPNLTVRETLAF-IAQMRLPRtfsqAQRDKRVEDVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGVQLLWNPGIL 238
Cdd:COG3842 87 ALFPHLTVAENVAFgLRMRGVPK----AEIRARVAELLELVGLEGLADR-----YPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180
....*....|....*....|....
gi 767915028 239 ILDEPTSGLDSFTAHNLVKTLSRL 262
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRL 181
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
90-299 |
1.81e-20 |
|
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: 90.24 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 90 LGIQNLSF--KVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQP-SSPQLVRKCVAHVRQHNQLLPNLT 166
Cdd:cd03298 10 YGEQPMHFdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETP---QSGRVLINGVDvTAAPPADRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETlafIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:cd03298 87 VEQN---VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767915028 247 LDSFTAHNLVKTLSRLAKGNRL-VLISLHQPrSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMtVLMVTHQP-EDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
90-248 |
3.08e-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: 89.99 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 90 LGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQLVRK-CVAHVRQHNQLLPNLTVR 168
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE---TPTSGEILLDGKDITNLPPHKrPVNTVFQNYALFPHLTVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFiaQMRLPRTfSQAQRDKRVEDVIAELRLRQCAdtrvgNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03300 91 ENIAF--GLRLKKL-PKAEIKERVAEALDLVQLEGYA-----NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
92-306 |
3.38e-20 |
|
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: 89.91 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkIK--SGQIWINGQPSSPQLV----RKCVAHVRQHNQLLPNL 165
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL-----VKpdSGKILLDGQDITKLPMhkraRLGIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQCADTRVGnmyvrGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:cd03218 91 TVEENILAVLEIR---GLSKKEREEKLEELLEEFHITHLRKSKAS-----SLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRsDIFRLFDLVLLMTSGTPIYLGAAQHMVQ 306
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDRGIGVLITDHNVR-ETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
92-306 |
4.97e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQ--PSSPQLVRKCVAHVRQHNQLLPNLTVRE 169
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHP---DAGSISLCGEpvPSRARHARQRVGVVPQFDNLDPDFTVRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAFIAqmrlpRTF--SQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:PRK13537 100 NLLVFG-----RYFglSAAAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 248 DSFTAHNLVKTL-SRLAKGNRLVLISLHQPRSDifRLFDLVLLMTSGTPIYLGAAQHMVQ 306
Cdd:PRK13537 170 DPQARHLMWERLrSLLARGKTILLTTHFMEEAE--RLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
92-289 |
7.58e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP-SSPQLVRkcvAHVRQHNQLLPNLTVRET 170
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFV---PYQHGSITLDGKPvEGPGAER---GVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 LAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQcadtrVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 250
Cdd:PRK11248 91 VAFGLQLA---GVEKMQRLEIAHQMLKKVGLEG-----AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767915028 251 TAHNLVKTLSRL-AKGNRLVLISLHQPRSDIFRLFDLVLL 289
Cdd:PRK11248 163 TREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
92-305 |
8.34e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.43 E-value: 8.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGkikSGQIWINGQ--PSSPQLVRKCVAHVRQHNQLLPNLTVRE 169
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD---AGKITVLGVpvPARARLARARIGVVPQFDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAFIAqmrlpRTFSQAQRDkrVEDVIAEL----RLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK13536 134 NLLVFG-----RYFGMSTRE--IEAVIPSLlefaRLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 246 GLDSFTAHNLVKTL-SRLAKGNRLVLISLHQPRSDifRLFDLVLLMTSGTPIYLGAAQHMV 305
Cdd:PRK13536 202 GLDPHARHLIWERLrSLLARGKTILLTTHFMEEAE--RLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
86-274 |
9.39e-20 |
|
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: 87.37 E-value: 9.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 86 NSCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKIKSGQIWINGQPssPQLVRKCVahvrqhnqllpnl 165
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG---DLKPQQGEITLDGVP--VSDLEKAL------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 tvRETLAFIAQMrlPRTFsqaqrdkrvedviaelrlrqcaDTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:cd03247 74 --SSLISVLNQR--PYLF----------------------DTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180
....*....|....*....|....*....
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTLIWITHH 156
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
87-248 |
1.02e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 87 SCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP---SSP-QLVRKCVAHV---RQHN 159
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGAD---PADSGEIRLDGKPvriRSPrDAIRAGIAYVpedRKGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 160 QLLPNLTVRE--TLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLR-QCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPG 236
Cdd:COG1129 340 GLVLDLSIREniTLASLDRLSRGGLLDRRRERALAEEYIKRLRIKtPSPEQPVGN-----LSGGNQQKVVLAKWLATDPK 414
|
170
....*....|..
gi 767915028 237 ILILDEPTSGLD 248
Cdd:COG1129 415 VLILDEPTRGID 426
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
95-274 |
1.41e-19 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 87.09 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKIKSGQIWINGQP-----SSPQLVRKCVAHVRQH--NQLLPNlTV 167
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNG---LLRPQSGAVLIDGEPldysrKGLLERRQRVGLVFQDpdDQLFAA-DV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFiaqmrLPRTF--SQAQRDKRVEDVIAELRLRQCADtRVGNMyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:TIGR01166 87 DQDVAF-----GPLNLglSEAEVERRVREALTAVGASGLRE-RPTHC----LSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180
....*....|....*....|....*....
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
92-274 |
1.63e-19 |
|
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: 88.12 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQP--SSPqlvRKCVAH---VRQHNQLLPNLT 166
Cdd:TIGR03864 17 LDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVA---QSGQISVAGHDlrRAP---RAALARlgvVFQQPTLDLDLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCADTRVgnmyvRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:TIGR03864 91 VRQNLRYHAALHgLSR----AEARARIAELLARLGLAERADDKV-----RELNGGHRRRVEIARALLHRPALLLLDEPTV 161
|
170 180 190
....*....|....*....|....*....|
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRL-VLISLH 274
Cdd:TIGR03864 162 GLDPASRAAITAHVRALARDQGLsVLWATH 191
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
95-304 |
3.11e-19 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 89.79 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQ--PSSPQLV-----RKCVAHVRQHNQLLPNLTV 167
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLT---RPDEGEIVLNGRtlFDSRKGIflppeKRRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLafiaqmRLPRTFSQA-QRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:TIGR02142 93 RGNL------RYGMKRARPsERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 247 LDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQHM 304
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
94-274 |
7.08e-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: 90.65 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGR---ASLL----DVitgrghggkiKSGQIWINGQP---SSPQLVRKCVAHVRQHNQLLp 163
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKstlARLLfrfyDV----------TSGRILIDGQDirdVTQASLRAAIGIVPQDTVLF- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVRETLAF------IAQMRlprtfsQAQRDKRVEDVIAelRLRQCADTRVGNmyvRG--LSGGERRRVSIGVQLLWNP 235
Cdd:COG5265 445 NDTIAYNIAYgrpdasEEEVE------AAARAAQIHDFIE--SLPDGYDTRVGE---RGlkLSGGEKQRVAIARTLLKNP 513
|
170 180 190
....*....|....*....|....*....|....*....
gi 767915028 236 GILILDEPTSGLDSFTAHNLVKTLSRLAKGnRLVLISLH 274
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVARG-RTTLVIAH 551
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
92-274 |
7.79e-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: 85.88 E-value: 7.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP--SSPQLVRKCVAHVRQHNQLLPNLTVRE 169
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL---KPTSGRATVAGHDvvREPREVRRRIGIVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAFIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03265 93 NLYIHARLYgVPG----AERRERIDELLDFVGLLEAADRLVKT-----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180
....*....|....*....|....*..
gi 767915028 249 SFTAHNLVKTLSRL-AKGNRLVLISLH 274
Cdd:cd03265 164 PQTRAHVWEYIEKLkEEFGMTILLTTH 190
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
94-299 |
9.29e-19 |
|
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: 86.74 E-value: 9.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGGKIK--SGQIWINGQPSSPQ------LVRKCVAHVRQH--NQLLP 163
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHL-----NGLLKptSGTVTIDGRDITAKkkkklkDLRKKVGLVFQFpeHQLFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NlTVRETLAFIaqmrlPRTF--SQAQRDKRVEDVIA------ELRLRQCADtrvgnmyvrgLSGGERRRVSI-GVqLLWN 234
Cdd:TIGR04521 98 E-TVYKDIAFG-----PKNLglSEEEAEERVKEALElvgldeEYLERSPFE----------LSGGQMRRVAIaGV-LAME 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 235 PGILILDEPTSGLDSFTAHNLVKTLSRLAK--GNRLVLISlHQpRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:TIGR04521 161 PEVLILDEPTAGLDPKGRKEILDLFKRLHKekGLTVILVT-HS-MEDVAEYADRVIVMHKGKIVLDG 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
92-271 |
1.60e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKIKSGQIWINGQ---PSSP-QLVRKCVAHV---RQHNQLLPN 164
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFG---VDKRAGGEIRLNGKdisPRSPlDAVKKGMAYItesRRDNGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFIAQMRLPR------TFSQAQRDKRVEDVIAELRLRqCADTrvgNMYVRGLSGGERRRVSIGVQLLWNPGIL 238
Cdd:PRK09700 356 FSIAQNMAISRSLKDGGykgamgLFHEVDEQRTAENQRELLALK-CHSV---NQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190
....*....|....*....|....*....|...
gi 767915028 239 ILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLI 271
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILM 464
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
93-277 |
1.78e-18 |
|
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: 85.18 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASL------LDVITgrghggkikSGQIWINGQPSSP-------QLVRKCVAHVRQHN 159
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLlgllagLDRPT---------SGTVRLAGQDLFAldedaraRLRARHVGFVFQSF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 160 QLLPNLTVRETLAFIAQMR-LPRTFSQAQrdkrvedviAELRlrqcadtRVG-----NMYVRGLSGGERRRVSIGVQLLW 233
Cdd:COG4181 100 QLLPTLTALENVMLPLELAgRRDARARAR---------ALLE-------RVGlghrlDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915028 234 NPGILILDEPTSGLDSFTAHNLVKTLSRLAK--GNRLVLISlHQPR 277
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVT-HDPA 208
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
92-305 |
2.34e-18 |
|
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: 85.02 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkIK--SGQIWINGQPSSPQLV----RKCVAHVRQHNQLLPNL 165
Cdd:TIGR04406 17 VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGL-----VRpdAGKILIDGQDITHLPMheraRLGIGYLPQEASIFRKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQMRlpRTFSQAQRDKRVEDVIAELRLRQCADTRVGnmyvrGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:TIGR04406 92 TVEENIMAVLEIR--KDLDRAEREERLEALLEEFQISHLRDNKAM-----SLSGGERRRVEIARALATNPKFILLDEPFA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRsDIFRLFDLVLLMTSGTPIYLGAAQHMV 305
Cdd:TIGR04406 165 GVDPIAVGDIKKIIKHLKERGIGVLITDHNVR-ETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
92-293 |
2.69e-18 |
|
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: 84.15 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLL-------DVITGRGHggkikSGQIWINGQP-----SSPQLVRKCVAHVRQHN 159
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLrllnrlnDLIPGAPD-----EGEVLLDGKDiydldVDVLELRRRVGMVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 160 QLLPnLTVRETLAFIAQMRLprtfsqaQRDKRVEDVIAELRLRQCA-DTRVG-NMYVRGLSGGERRRVSIGVQLLWNPGI 237
Cdd:cd03260 91 NPFP-GSIYDNVAYGLRLHG-------IKLKEELDERVEEALRKAAlWDEVKdRLHALGLSGGQQQRLCLARALANEPEV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 238 LILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLIS--LHQprsdIFRLFDLVLLMTSG 293
Cdd:cd03260 163 LLLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ----AARVADRTAFLLNG 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
91-306 |
2.72e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.86 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITgRGHggKIKSGQIWINGQPSSP---QLVRKCVAHVRQhNQLLPNLTV 167
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQ-RVF--DPQSGRILIDGTDIRTvtrASLRRNIAVVFQ-DAGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETL------AFIAQMRLPRTFSQAQrdkrveDVIaeLRLRQCADTRVGNmyvRG--LSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK13657 426 EDNIrvgrpdATDEEMRAAAERAQAH------DFI--ERKPDGYDTVVGE---RGrqLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 240 LDEPTSGLDSFTAHNLVKTLSRLAKGnRLVLISLHqpRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQ 306
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKG-RTTFIIAH--RLSTVRNADRILVFDNGRVVESGSFDELVA 558
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
92-293 |
2.86e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKikSGQIWINGQP---SSP-QLVRKCVAHV---RQHNQLLPN 164
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRW--EGEIFIDGKPvkiRNPqQAIAQGIAMVpedRKRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRE--TLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQC-ADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILD 241
Cdd:PRK13549 356 MGVGKniTLAALDRFTGGSRIDDAAELKTILESIQRLKVKTAsPELAIAR-----LSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767915028 242 EPTSGLDSFTAHNLVKTLSRLAK-GNRLVLISLHQPrsDIFRLFDLVLLMTSG 293
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELP--EVLGLSDRVLVMHEG 481
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
87-293 |
3.86e-18 |
|
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: 82.48 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 87 SCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP---SSP-QLVRKCVAHV---RQHN 159
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLR---PPASGEITLDGKPvtrRSPrDAIRAGIAYVpedRKRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 160 QLLPNLTVRETLAFIAQmrlprtfsqaqrdkrvedviaelrlrqcadtrvgnmyvrgLSGGERRRVSIGVQLLWNPGILI 239
Cdd:cd03215 88 GLVLDLSVAENIALSSL----------------------------------------LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 240 LDEPTSGLDSFTAHNLVKTLSRLAKGNRLVL-ISlhqprSD---IFRLFDLVLLMTSG 293
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLlIS-----SEldeLLGLCDRILVMYEG 180
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
92-293 |
4.43e-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: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKIKSGQIWINGQPSS---PQLVRKCVAHVRQHNQLLPnltvr 168
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGL---LRPTSGRVRLDGADISqwdPNELGDHVGYLPQDDELFS----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 etlafiaqmrlprtfsqaqrdkrveDVIAElrlrqcadtrvgNMyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03246 90 -------------------------GSIAE------------NI----LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915028 249 SFTAHNLVKTLSRL-AKGNRLVLISlHQPRsdIFRLFDLVLLMTSG 293
Cdd:cd03246 129 VEGERALNQAIAALkAAGATRIVIA-HRPE--TLASADRILVLEDG 171
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
92-262 |
4.53e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.71 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSpQLVRKCVAHVR--------QHNQLLP 163
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLD---TPTSGDVIFNGQPMS-KLSSAAKAELRnqklgfiyQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVRETLA---FIAQMRlprtfsQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:PRK11629 101 DFTALENVAmplLIGKKK------PAEINSRALEMLAAVGLEHRANHRPSE-----LSGGERQRVAIARALVNNPRLVLA 169
|
170 180
....*....|....*....|..
gi 767915028 241 DEPTSGLDSFTAHNLVKTLSRL 262
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGEL 191
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
92-275 |
5.71e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.16 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkIK--SGQIWINGQPSSPQLVRKcvahvrqhnqLLPNLTVRE 169
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGI-----LApdSGEVLWDGEPLDPEDRRRigylp-eergLYPKMKVGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAFIAQMR-LPRtfSQAQRdkRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:COG4152 91 QLVYLARLKgLSK--AEAKR--RADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180
....*....|....*....|....*..
gi 767915028 249 SFTAHNLVKTLSRLAKGNRLVLISLHQ 275
Cdd:COG4152 162 PVNVELLKDVIRELAAKGTTVIFSSHQ 188
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
93-326 |
6.84e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.85 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQ------PSspqlvRKCVAHVRQHNQLLPNLT 166
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLE---DITSGDLFIGEKrmndvpPA-----ERGVGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFiaQMRLPRTfSQAQRDKRVEDVIAELRLRQCADTRVgnmyvRGLSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:PRK11000 92 VAENMSF--GLKLAGA-KKEEINQRVNQVAEVLQLAHLLDRKP-----KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 247 LDSFTAHNLVKTLSRLAKgnRLvlislhqPRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQyftaIGYPCPRYSNPADFYV 326
Cdd:PRK11000 164 LDAALRVQMRIEISRLHK--RL-------GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQ----VGKPLELYHYPANRFV 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
92-278 |
7.51e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 7.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRAS----LLDVITGRGhggkiksgQIWINGQPSSpQLVRKCVAHVRQHNQ------- 160
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQG--------EIWFDGQPLH-NLNRRQLLPVRHRIQvvfqdpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 161 --LLPNLTVRETLAFIAQMRLPrTFSQAQRDKRVEDVIAELRLRqcADTRvgNMYVRGLSGGERRRVSIGVQLLWNPGIL 238
Cdd:PRK15134 373 ssLNPRLNVLQIIEEGLRVHQP-TLSAAQREQQVIAVMEEVGLD--PETR--HRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767915028 239 ILDEPTSGLDSFTAHNLVKTLSRLAKGNRL--VLIS--LHQPRS 278
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFIShdLHVVRA 491
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
92-274 |
7.99e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.97 E-value: 7.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP-----SSPQLVRKCVAHVRQH--NQLL-P 163
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL---KPTSGEVLIKGEPikydkKSLLEVRKTVGIVFQNpdDQLFaP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 nlTVRETLAFiAQMRLprTFSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEP 243
Cdd:PRK13639 95 --TVEEDVAF-GPLNL--GLSKEEVEKRVKEALKAVGMEGFENKPPHH-----LSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 767915028 244 TSGLDSFTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
94-293 |
8.90e-18 |
|
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: 82.78 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP----SSPQLVR---KCVAHVRQHNQLLPNLT 166
Cdd:TIGR02211 23 GVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLD---NPTSGEVLFNGQSlsklSSNERAKlrnKKLGFIYQFHHLLPDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFIAqmrLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:TIGR02211 100 ALENVAMPL---LIGKKSVKEAKERAYEMLEKVGLEHRINHRPSE-----LSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915028 247 LDSFTAH---NLVKTLSRlAKGNRLVLISlHQPRsdIFRLFDLVLLMTSG 293
Cdd:TIGR02211 172 LDNNNAKiifDLMLELNR-ELNTSFLVVT-HDLE--LAKKLDRVLEMKDG 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
92-318 |
9.82e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.19 E-value: 9.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITgRGHggKIKSGQIWINGQP----SSPQLvRKCVAHVRQHNQLLpNLTV 167
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAW--DPQQGEILLNGQPiadySEAAL-RQAISVVSQRVHLF-SATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFIAqmrlprtfSQAQrDKRVEDVIAELRLRQCADTRVG-NMYV----RGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:PRK11160 431 RDNLLLAA--------PNAS-DEALIEVLQQVGLEKLLEDDKGlNAWLgeggRQLSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLAKGNRLVLISlHqprsdifRL-----FDLVLLMTSGTPIYLGAAQHMVQyftaigyPCPR 317
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHAQNKTVLMIT-H-------RLtgleqFDRICVMDNGQIIEQGTHQELLA-------QQGR 566
|
.
gi 767915028 318 Y 318
Cdd:PRK11160 567 Y 567
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
92-248 |
1.09e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 85.38 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkIKSGQIWINGQpsspqlvrkCVAH----------VRQHNQL 161
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFET---PDSGRIMLDGQ---------DITHvpaenrhvntVFQSYAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 162 LPNLTVRETLAFIAQM-RLPRtfsqAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:PRK09452 98 FPHMTVFENVAFGLRMqKTPA----AEITPRVMEALRMVQLEEFAQRKPHQ-----LSGGQQQRVAIARAVVNKPKVLLL 168
|
....*...
gi 767915028 241 DEPTSGLD 248
Cdd:PRK09452 169 DESLSALD 176
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
92-248 |
1.16e-17 |
|
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: 84.33 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCG-----RAsLLDVITGRGhggkIKSGQIWINGQP----SSPQL--VR-KCVAHVRQH- 158
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGkstlaRA-ILGLLPPPG----ITSGEILFDGEDllklSEKELrkIRgREIQMIFQDp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 159 -NQLLPNLTVRETLAFIaqMRLPRTFSQAQRDKRVEDVIAELRLRqcADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGI 237
Cdd:COG0444 96 mTSLNPVMTVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLP--DPERRLDRYPHELSGGMRQRVMIARALALEPKL 171
|
170
....*....|.
gi 767915028 238 LILDEPTSGLD 248
Cdd:COG0444 172 LIADEPTTALD 182
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
92-302 |
2.43e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.00 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQ---PSSPQLVRKCVahVRQHNQLLPNLTVR 168
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLE---KPTEGQIFIDGEdvtHRSIQQRDICM--VFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:PRK11432 97 ENVGYGLKML---GVPKEERKQRVKEALELVDLAGFEDR-----YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 249 SFTAHNLVKTLSRLAKgnRLVLISLH--QPRSDIFRLFDLVLLMTSGTPIYLGAAQ 302
Cdd:PRK11432 169 ANLRRSMREKIRELQQ--QFNITSLYvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQ 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
95-252 |
6.42e-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: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP--SSPQLVRKCVAHVRQHNQLLPNLTVRETLA 172
Cdd:TIGR01188 12 VNFKVREGEVFGFLGPNGAGKTTTIRMLTTLL---RPTSGTARVAGYDvvREPRKVRRSIGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 173 FIAQMR-LPRtfsqAQRDKRVEDVIAELRLRQCADTRVGNMyvrglSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 251
Cdd:TIGR01188 89 MMGRLYgLPK----DEAEERAEELLELFELGEAADRPVGTY-----SGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
.
gi 767915028 252 A 252
Cdd:TIGR01188 160 R 160
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
92-295 |
9.82e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.44 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITgrgHGGKIKSGQIWINGQP----SSPQLVRkCVAHVRQHNQLLPNLTV 167
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFA---RLLTPQSGTVFLGDKPismlSSRQLAR-RLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFIAQMRLPRTFSQAQRDK-RVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:PRK11231 94 RELVAYGRSPWLSLWGRLSAEDNaRVNQAMEQTRINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 247 LDSFTAHNLVKTLSRLAKGNRLVLISLHqprsDI---FRLFD-LVLL-----MTSGTP 295
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQGKTVVTVLH----DLnqaSRYCDhLVVLanghvMAQGTP 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
96-293 |
1.02e-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: 82.07 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 96 SFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIK-SGQIWINGQPS---SPQlvRKCVAHVRQHNQLLPNLTVRE 169
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGleRPDSGRIRlGGEVLQDSARGiflPPH--RRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAFiAQMRLPRTFSQAQRDkrveDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 249
Cdd:COG4148 97 NLLY-GRKRAPRAERRISFD----EVVELLGIGHLLDRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915028 250 FTAHNLVKTLSRLAKGNRL--VLISlHQPRsDIFRLFDLVLLMTSG 293
Cdd:COG4148 167 ARKAEILPYLERLRDELDIpiLYVS-HSLD-EVARLADHVVLLEQG 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
94-276 |
1.46e-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: 83.18 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITG----RGhggkiksGQIWINGQPS---SPQLVRKCVAHVRQHNQLLpNLT 166
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGlldpLQ-------GEVTLDGVPVsslDQDEVRRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFIAQMRLPRTFSQAQRDKRVEDVIAelRLRQCADTRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:TIGR02868 425 VRENLRLARPDATDEELWAALERVGLADWLR--ALPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|
gi 767915028 247 LDSFTAHNLVKTLSRLAKGNRLVLISlHQP 276
Cdd:TIGR02868 502 LDAETADELLEDLLAALSGRTVVLIT-HHL 530
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
94-277 |
1.65e-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: 78.55 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkIKSGQIWINGQPSS---PQLVRKCvAHVRQHNQLLPNLTVRET 170
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR---PDSGEVRWNGTPLAeqrDEPHENI-LYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 LAFIAqmrlpRTFSQAQRDkrVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDS- 249
Cdd:TIGR01189 94 LHFWA-----AIHGGAQRT--IEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKa 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 767915028 250 --------FTAHnlvktlsrLAKGNrLVLISLHQPR 277
Cdd:TIGR01189 162 gvallaglLRAH--------LARGG-IVLLTTHQDL 188
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
93-248 |
1.74e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 81.28 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVI------TgrghggkikSGQIWINGQP----SSPQL--VRKCVAHVRQHNQ 160
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllerpT---------SGSVLVDGVDltalSERELraARRKIGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 161 LLPNLTVRETLAF---IAQMrlprtfSQAQRDKRVEDVIAelrlrqcadtRVG-----NMYVRGLSGGERRRVSIGVQLL 232
Cdd:COG1135 93 LLSSRTVAENVALpleIAGV------PKAEIRKRVAELLE----------LVGlsdkaDAYPSQLSGGQKQRVGIARALA 156
|
170
....*....|....*.
gi 767915028 233 WNPGILILDEPTSGLD 248
Cdd:COG1135 157 NNPKVLLCDEATSALD 172
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
86-306 |
1.99e-16 |
|
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: 78.81 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 86 NSCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSP---QLVRKCVAHVRQHNQLL 162
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFY---DPQKGQILIDGIDIRDisrKSLRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNlTVRETLAFiaqmrlprtFSQAQRDKRVEDVIAEL-------RLRQCADTRVGNmyvRG--LSGGERRRVSIGVQLLW 233
Cdd:cd03254 90 SG-TIMENIRL---------GRPNATDEEVIEAAKEAgahdfimKLPNGYDTVLGE---NGgnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915028 234 NPGILILDEPTSGLDSFTAHNLVKTLSRLAKGnRLVLISLHqpRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQ 306
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKG-RTSIIIAH--RLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
94-275 |
3.13e-16 |
|
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: 82.46 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkIKSGQIWINGQP---SSPQLVRKCVAHVRQHNQLLpNLTVRET 170
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE---PDSGQILLDGHDladYTLASLRRQVALVSQDVVLF-NDTIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 LAFIAQMRLPRT-FSQAQRDKRVEDVIAelRLRQCADTRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 249
Cdd:TIGR02203 426 IAYGRTEQADRAeIERALAAAYAQDFVD--KLPLGLDTPIGENGVL-LSGGQRQRLAIARALLKDAPILILDEATSALDN 502
|
170 180
....*....|....*....|....*.
gi 767915028 250 FTAHNLVKTLSRLAKGnRLVLISLHQ 275
Cdd:TIGR02203 503 ESERLVQAALERLMQG-RTTLVIAHR 527
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
95-294 |
3.21e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkIK---SGQIWINGQPSSPQLVRKcvAH------VRQHNQLLPNL 165
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAG------IVppdSGTLEIGGNPCARLTPAK--AHqlgiylVPQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFiaqmRLPRTfsqAQRDKRVEDVIAELRLRQCADTRVGNMYVrglsgGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK15439 102 SVKENILF----GLPKR---QASMQKMKQLLAALGCQLDLDSSAGSLEV-----ADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915028 246 GLDSFTAHNLVKTL-SRLAKGNRLVLISLHQPrsDIFRLFDLVLLMTSGT 294
Cdd:PRK15439 170 SLTPAETERLFSRIrELLAQGVGIVFISHKLP--EIRQLADRISVMRDGT 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
94-249 |
3.24e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.51 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQPSSPQLVR-KCVAHVRQHNQLLPNLTVRETLA 172
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ---TSGHIRFHGTDVSRLHARdRKVGFVFQHYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 173 FIAQMrLPRTF--SQAQRDKRVEDVIAELRLrqcadTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 249
Cdd:PRK10851 97 FGLTV-LPRRErpNAAAIKAKVTQLLEMVQL-----AHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
91-298 |
4.54e-16 |
|
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: 82.75 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQL--VRKCVAHVRQHNQLLPNLTVR 168
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLL---PPTSGTVLVGGKDIETNLdaVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMRlPRTFSQAQRDkrvedviAELRLRQCADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:TIGR01257 1022 EHILFYAQLK-GRSWEEAQLE-------MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 249 SFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIfrLFDLVLLMT------SGTPIYL 298
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADL--LGDRIAIISqgrlycSGTPLFL 1147
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
95-275 |
5.36e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 78.25 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVIT--GRGHGGKIKSGQIWING-QPSSPQ--LVRKC---VAHVRQHNQLLPNLT 166
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINllEQPEAGTIRVGDITIDTaRSLSQQkgLIRQLrqhVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLafiaqMRLPRTFSQAQRDKrvedviAELRLRQCAdTRVG-----NMYVRGLSGGERRRVSIGVQLLWNPGILILD 241
Cdd:PRK11264 102 VLENI-----IEGPVIVKGEPKEE------ATARARELL-AKVGlagkeTSYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190
....*....|....*....|....*....|....
gi 767915028 242 EPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQ 275
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHE 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
92-248 |
7.68e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.50 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQ------PSSpqlvRKCvAHVRQHNQLLPNL 165
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLE---RITSGEIWIGGRvvnelePAD----RDI-AMVFQNYALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAF---IaqmrlpRTFSQAQRDKRVEDVIAELRLRQCADTRVgnmyvRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:PRK11650 92 SVRENMAYglkI------RGMPKAEIEERVAEAARILELEPLLDRKP-----RELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
....*.
gi 767915028 243 PTSGLD 248
Cdd:PRK11650 161 PLSNLD 166
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
92-304 |
1.02e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.97 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP---SSPQL--VRKCVAHVRQH--NQLLpN 164
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL---KPSSGRILFDGKPidySRKGLmkLRESVGMVFQDpdNQLF-S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAF-IAQMRLPRTFSQaqrdKRVEDViaelrLRQCADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEP 243
Cdd:PRK13636 98 ASVYQDVSFgAVNLKLPEDEVR----KRVDNA-----LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915028 244 TSGLDSFTAHNLVKTLSRLAKGNRL-VLISLHQprSDIFRLF-DLVLLMTSGTPIYLGAAQHM 304
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKELGLtIIIATHD--IDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
92-277 |
1.10e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.24 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG---RghggkiKSGQIWINGQPSS----PQLVRKCVAHVRQHNQLLPN 164
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivpR------DAGNIIIDDEDISllplHARARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFIAQMRlpRTFSQAQRDKRVEDVIAELRLRQCADTrVGnmyvRGLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:PRK10895 93 LSVYDNLMAVLQIR--DDLSAEQREDRANELMEEFHIEHLRDS-MG----QSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190
....*....|....*....|....*....|...
gi 767915028 245 SGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPR 277
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR 198
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
79-294 |
1.18e-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: 75.97 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 79 WTSPSCQNSceLGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkIKSGQIWINGQpsspqlvrkcVAHVRQh 158
Cdd:cd03250 10 WDSGEQETS--FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---KLSGSVSVPGS----------IAYVSQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 159 NQLLPNLTVRETLAFIAQMrlprtfsqaqRDKRVEDVIaelrlRQCA------------DTRVGnmyVRG--LSGGERRR 224
Cdd:cd03250 74 EPWIQNGTIRENILFGKPF----------DEERYEKVI-----KACAlepdleilpdgdLTEIG---EKGinLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 225 VSIGVQLLWNPGILILDEPTSGLDSFTAHNLV-KTLSRLAKGNRLVLISLHQPrsDIFRLFDLVLLMTSGT 294
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQL--QLLPHADQIVVLDNGR 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
92-306 |
1.21e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.53 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSsPQL----VRKCVAHVRQHNQLLPNlTV 167
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF---DVSEGDIRFHDIPL-TKLqldsWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFIAQMRLPRTFSQAQRDKRVEDVIaeLRLRQCADTRVGNmyvRG--LSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK10789 406 ANNIALGRPDATQQEIEHVARLASVHDDI--LRLPQGYDTEVGE---RGvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGnRLVLISLHqprsdifRLFDL-----VLLMTSGTPIYLGAAQHMVQ 306
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEG-RTVIISAH-------RLSALteaseILVMQHGHIAQRGNHDQLAQ 538
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
90-299 |
1.33e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 90 LGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIWINGQPSSpQLVRKCVAHVRQHNQLLPNLTV 167
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfyKPTGGTILLRGQHIEGLPGH-QIARMGVVRTFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLaFIAQMRLPRT-----------FSQAQRDK--RVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWN 234
Cdd:PRK11300 98 IENL-LVAQHQQLKTglfsgllktpaFRRAESEAldRAATWLERVGLLEHANRQAGN-----LAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 235 PGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
92-248 |
1.55e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.72 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQPSS--PQLVRKcVAHVRQHNQLLPNLTVRE 169
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP---TAGQIMLDGVDLShvPPYQRP-INMMFQSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAF-IAQMRLPRtfsqAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:PRK11607 111 NIAFgLKQDKLPK----AEIASRVNEMLGLVHMQEFAKRKPHQ-----LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
93-272 |
1.67e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkIK--SGQIWINGQP---SSPQLVRKC-VAHVRQHNQLLPNLT 166
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGL-----YQpdSGEILIDGKPvriRSPRDAIALgIGMVHQHFMLVPNLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAfIAQMRLPRTF-SQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:COG3845 97 VAENIV-LGLEPTKGGRlDRKAARARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190
....*....|....*....|....*....|.
gi 767915028 246 GLdsfT---AHNLVKTLSRLAK-GNRLVLIS 272
Cdd:COG3845 171 VL---TpqeADELFEILRRLAAeGKSIIFIT 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
92-293 |
2.18e-15 |
|
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: 79.48 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKikSGQIWINGQP----SSPQLVRKCVAHV---RQHNQLLPN 164
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKF--EGNVFINGKPvdirNPAQAIRAGIAMVpedRKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRE--TLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRqcadTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:TIGR02633 354 LGVGKniTLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVK----TASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLA-KGNRLVLISLHQPrsDIFRLFDLVLLMTSG 293
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELA--EVLGLSDRVLVIGEG 479
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
92-248 |
2.59e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 75.82 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVI----TGRghggkikSGQIWINGQ---------PSSPQLVRKCVAHVRQH 158
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLnlleTPD-------SGQLNIAGHqfdfsqkpsEKAIRLLRQKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 159 NQLLPNLTVRETLaFIAQMR-LPRTFSQAQrdKRVEDVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGVQLLWNPGI 237
Cdd:COG4161 91 YNLWPHLTVMENL-IEAPCKvLGLSKEQAR--EKAMKLLARLRLTDKADR-----FPLHLSGGQQQRVAIARALMMEPQV 162
|
170
....*....|.
gi 767915028 238 LILDEPTSGLD 248
Cdd:COG4161 163 LLFDEPTAALD 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
92-289 |
2.69e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.58 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkiksgqiwiNGQPSSPQLVRKC---VAHVRQHNQL---LPnL 165
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAG--------------VLRPTSGTVRRAGgarVAYVPQRSEVpdsLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRE--TLAFIAQMRLPRTFSQAQRdKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEP 243
Cdd:NF040873 73 TVRDlvAMGRWARRGLWRRLTRDDR-AAVDDALERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767915028 244 TSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLL 289
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDL-ELVRRADPCVLL 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
90-248 |
3.46e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 90 LGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RghggKIKSGQIWINGQP---SSPQLVRKC-VAHV---RQHNQL 161
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGlR----PPASGSIRLDGEDitgLSPRERRRLgVAYIpedRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 162 LPNLTVRETLAFIAQMRLPRT----FSQAQRDKRVEDVIAELRLRqcadTRVGNMYVRGLSGGERRRVSIGVQLLWNPGI 237
Cdd:COG3845 348 VPDMSVAENLILGRYRRPPFSrggfLDRKAIRAFAEELIEEFDVR----TPGPDTPARSLSGGNQQKVILARELSRDPKL 423
|
170
....*....|.
gi 767915028 238 LILDEPTSGLD 248
Cdd:COG3845 424 LIAAQPTRGLD 434
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
92-248 |
4.25e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 76.66 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkI---KSGQIWINGQpsSPQLVRKcvAHVR-------QHNQL 161
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTG------IlvpTSGEVRVLGY--VPFKRRK--EFARrigvvfgQRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 162 LPNLTVRETLAFIAQM-RLPRtfsqAQRDKRVEDVIAELRLRQCADTRVgnmyvRGLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:COG4586 108 WWDLPAIDSFRLLKAIyRIPD----AEYKKRLDELVELLDLGELLDTPV-----RQLSLGQRMRCELAAALLHRPKILFL 178
|
....*...
gi 767915028 241 DEPTSGLD 248
Cdd:COG4586 179 DEPTIGLD 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
93-287 |
4.57e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGkikSGQIWINGQPSSPQLVRKC----VAHVRQHNQLLPNLTVR 168
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD---AGSILIDGQEMRFASTTAAlaagVAIIYQELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLaFIAQmrLPRTF---SQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK11288 98 ENL-YLGQ--LPHKGgivNRRLLNYEAREQLEHLGVDIDPDTPLKY-----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHqpRSD-IFRLFDLV 287
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEGRVILYVSH--RMEeIFALCDAI 210
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
92-294 |
5.27e-15 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 74.99 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRgHGGKIKSGQIWINGQPSSPQLV----RKCVAHVRQHNQLLPNLTV 167
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH-PSYEVTSGTILFKGQDLLELEPderaRAGLFLAFQYPEEIPGVSN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 REtlaFIaqmrlpRTFSQAQRDKRVEDVIAELRLRQCADTR------VGNMYVR----GLSGGERRRVSIGVQLLWNPGI 237
Cdd:TIGR01978 95 LE---FL------RSALNARRSARGEEPLDLLDFEKLLKEKlalldmDEEFLNRsvneGFSGGEKKRNEILQMALLEPKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 238 LILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRsdIFRLF--DLVLLMTSGT 294
Cdd:TIGR01978 166 AILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR--LLNYIkpDYVHVLLDGR 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
92-275 |
5.39e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.13 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLL------DVITGrghgGKIKSGQIWINGQPSSPQLVRKCVAHVRQHNQLLPNL 165
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLrcinklEEITS----GDLIVDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFiAQMRLpRTFSQAQRDKRVEDVIAELRLRQCAdtrvgNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK09493 93 TALENVMF-GPLRV-RGASKEEAEKQARELLAKVGLAERA-----HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190
....*....|....*....|....*....|
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHQ 275
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
92-306 |
6.97e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.21 E-value: 6.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVItGRGHggKIKSGQIWINGQP----SSPQLVRKcVAHVRQHNQLLPNLTV 167
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQ--PPSEGEILLDAQPleswSSKAFARK-VAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 REtlaFIAQMRLP-----RTFSQAQRdKRVEDVIAELRLRQCAdtrvgNMYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:PRK10575 103 RE---LVAIGRYPwhgalGRFGAADR-EKVEEAISLVGLKPLA-----HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915028 243 PTSGLDsfTAHN-----LVKTLSRLaKGnrLVLIS-LHqprsDI---FRLFDLVLLMTSGTPIYLGAAQHMVQ 306
Cdd:PRK10575 174 PTSALD--IAHQvdvlaLVHRLSQE-RG--LTVIAvLH----DInmaARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
93-248 |
1.14e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkIKSGQIWINGQpsspqlVRkcVAHVRQHNQLLPNLTVRETL- 171
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE---PDSGEVSIPKG------LR--IGYLPQEPPLDDDLTVLDTVl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 -AFIAQMRLPRTFSQAQR---------------------------DKRVEDVIAELRLRQC-ADTRVGNmyvrgLSGGER 222
Cdd:COG0488 84 dGDAELRALEAELEELEAklaepdedlerlaelqeefealggweaEARAEEILSGLGFPEEdLDRPVSE-----LSGGWR 158
|
170 180
....*....|....*....|....*.
gi 767915028 223 RRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
90-326 |
1.15e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.61 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 90 LGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKiksGQIWING----QPSSPQLV---RKCVAHVRQHNQLL 162
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTR---GQVLIDGvdiaKISDAELRevrRKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLAFiaQMRLPRTFSQAQRDKRVEdviaelRLRQCADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:PRK10070 119 PHMTVLDNTAF--GMELAGINAEERREKALD------ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGtpiylgaaqHMVQyftaIGYPCPRYSNPA 322
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNG---------EVVQ----VGTPDEILNNPA 257
|
....
gi 767915028 323 DFYV 326
Cdd:PRK10070 258 NDYV 261
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
96-248 |
1.25e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.85 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 96 SFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQP---SSPQlvRKCVAHVRQHNQLLPNLTVRETLA 172
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTP---ASGSLTLNGQDhttTPPS--RRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 173 FIAQ--MRLprtfSQAQRDKrVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:PRK10771 94 LGLNpgLKL----NAAQREK-LHAIARQMGIEDLLARLPGQ-----LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
92-306 |
1.60e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.48 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG------RGHGGKIkSGQIWINGQP----SSPQLVRKcVAHVRQHNQL 161
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggAPRGARV-TGDVTLNGEPlaaiDAPRLARL-RAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 162 LPNLTVRETLAFiaqMRLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNMyVRGLSGGERRRVSIGVQL--LW------ 233
Cdd:PRK13547 95 AFAFSAREIVLL---GRYPHARRAGALTHRDGEIAWQALALAGATALVGRD-VTTLSGGELARVQFARVLaqLWpphdaa 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 234 -NPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRL-VLISLHQPRSDIfRLFDLVLLMTSGTPIYLGAAQHMVQ 306
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPADVLT 244
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
94-248 |
1.82e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.51 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVI----TGRghggkikSGQIWINGQ---------PSSPQLVRKCVAHVRQHNQ 160
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnlleMPR-------SGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 161 LLPNLTVRETLafI-AQMRLpRTFSQAQRDKRVEDVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK11124 93 LWPHLTVQQNL--IeAPCRV-LGLSKDQALARAEKLLERLRLKPYADR-----FPLHLSGGQQQRVAIARALMMEPQVLL 164
|
....*....
gi 767915028 240 LDEPTSGLD 248
Cdd:PRK11124 165 FDEPTAALD 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
91-248 |
1.91e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKIKSGQIWINGQ---PSSPQ-LVRKCVAHV---RQHNQLLP 163
Cdd:PRK10762 267 GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYG---ALPRTSGYVTLDGHevvTRSPQdGLANGIVYIsedRKRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVRETLAFIAQMRLPRTFSQAQRDKR---VEDVIAELRLRQ-CADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK10762 344 GMSVKENMSLTALRYFSRAGGSLKHADEqqaVSDFIRLFNIKTpSMEQAIGL-----LSGGNQQKVAIARGLMTRPKVLI 418
|
....*....
gi 767915028 240 LDEPTSGLD 248
Cdd:PRK10762 419 LDEPTRGVD 427
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
92-299 |
2.32e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.93 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWING-----QPSSPQLVRKCVAHVRQH--NQLLPN 164
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL---KPTSGKIIIDGvditdKKVKLSDIRKKVGLVFQYpeYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 lTVRETLAFiaqmrLPRTF--SQAQRDKRVEDVIAELRLRQcadTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:PRK13637 100 -TIEKDIAF-----GPINLglSEEEIENRVKRAMNIVGLDY---EDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
91-296 |
2.55e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.10 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIWINGQPSSPQL--VRKCVAHVRQ--HNQLLPN 164
Cdd:PRK13641 22 GLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAllKPSSGTITIAGYHITPETGNKNLkkLRKKVSLVFQfpEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 lTVRETLAFiaqmrLPRTFSqAQRDKRVEDVIAELRlRQCADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:PRK13641 102 -TVLKDVEF-----GPKNFG-FSEDEAKEKALKWLK-KVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767915028 245 SGLDSFTAHNLVKTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSGTPI 296
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGKLI 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
93-272 |
3.14e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITG---RGhggkikSGQIWINGQP---SSPQLVRKC-VAHVRQHNQLLPNL 165
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGvyqPD------SGEILLDGEPvrfRSPRDAQAAgIAIIHQELNLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLaFIAqmRLPRTF---SQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:COG1129 95 SVAENI-FLG--REPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGD-----LSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190
....*....|....*....|....*....|.
gi 767915028 243 PTSGLDSFTAHNLVKTLSRL-AKGNRLVLIS 272
Cdd:COG1129 167 PTASLTEREVERLFRIIRRLkAQGVAIIYIS 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
93-248 |
3.22e-14 |
|
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: 75.88 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLldvitGRGHGGKIKS-GQIWINGQPSSpQLVRKCVAHVRQHNQ---------LL 162
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTL-----GLALLRLIPSeGEIRFDGQDLD-GLSRRALRPLRRRMQvvfqdpfgsLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLA---FIAQMRLPRtfsqAQRDKRVEDVIAELRLrqcaDTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILI 239
Cdd:COG4172 377 PRMTVGQIIAeglRVHGPGLSA----AERRARVAEALEEVGL----DPAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
....*....
gi 767915028 240 LDEPTSGLD 248
Cdd:COG4172 449 LDEPTSALD 457
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
99-303 |
3.34e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 99 VRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKSGQIWINGQPSS-----PQLVRKCVAH---VRQHNQLLPNLTVRET 170
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQregrlARDIRKSRANtgyIFQQFNLVNRLSVLEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 LAFIAQMRLP------RTFSQAQRDKRVEdviaelrlrqcADTRVGNMY-----VRGLSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK09984 107 VLIGALGSTPfwrtcfSWFTREQKQRALQ-----------ALTRVGMVHfahqrVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 240 LDEPTSGLDSFTAHNLVKTLSRLAKGNRL-VLISLHQPRSDIfRLFDLVLLMTSGTPIYLGAAQH 303
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQVDYAL-RYCERIVALRQGHVFYDGSSQQ 239
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
92-277 |
3.45e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.75 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggKIK--SGQIWINGQPSSP----QLVRKCVAHVRQHNQLLPNL 165
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVG-----LVKpdSGRIFLDGEDITHlpmhKRARLGIGYLPQEASIFRKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQMRlprTFSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:COG1137 94 TVEDNILAVLELR---KLSKKEREERLEELLEEFGITHLRKSKAYS-----LSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190
....*....|....*....|....*....|..
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHQPR 277
Cdd:COG1137 166 GVDPIAVADIQKIIRHLKERGIGVLITDHNVR 197
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
96-248 |
3.77e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.00 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 96 SFKVRSGQMLAIIGSSGCGRASL------LDVITgrghggkikSGQIWINGQPSSpQLVRKCVAHVRQHNQ--------- 160
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLgrlllrLEEPT---------SGEILFDGQDIT-GLSGRELRPLRRRMQmvfqdpyas 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 161 LLPNLTVRETLAfiAQMRLPRTFSQAQRDKRVEDVIAELRLRQcadtRVGNMYVRGLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:COG4608 108 LNPRMTVGDIIA--EPLRIHGLASKAERRERVAELLELVGLRP----EHADRYPHEFSGGQRQRIGIARALALNPKLIVC 181
|
....*...
gi 767915028 241 DEPTSGLD 248
Cdd:COG4608 182 DEPVSALD 189
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
96-248 |
3.99e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.85 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 96 SFKVRSGQMLAIIGSSGCGR---ASLLDVITgrghggKIKSGQIWINGQ------PSSPQLVRKCVAHVRQ--HNQLLPN 164
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKstlARLLTMIE------TPTGGELYYQGQdllkadPEAQKLLRQKIQIVFQnpYGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAfiAQMRLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNMYvrglSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:PRK11308 109 KKVGQILE--EPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMF----SGGQRQRIAIARALMLDPDVVVADEPV 182
|
....
gi 767915028 245 SGLD 248
Cdd:PRK11308 183 SALD 186
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
89-274 |
4.04e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.44 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 89 ELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITgRGHggKIKSGQIWING---QPSSPQLVRKCVAHVRQhNQLLPNL 165
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT-RFY--DIDEGEILLDGhdlRDYTLASLRNQVALVSQ-NVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQMRLPR-TFSQAQRDKRVEDVIAelRLRQCADTRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:PRK11176 432 TIANNIAYARTEQYSReQIEEAARMAYAMDFIN--KMDNGLDTVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEAT 508
|
170 180 190
....*....|....*....|....*....|
gi 767915028 245 SGLDSFTAHNLVKTLSRLAKgNRLVLISLH 274
Cdd:PRK11176 509 SALDTESERAIQAALDELQK-NRTSLVIAH 537
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
92-302 |
4.26e-14 |
|
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: 75.55 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKsgqiwINGQPSS---PQLVRKCVAHVRQHNQLLPNlT 166
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGvwPPTAGSVR-----LDGADLSqwdREELGRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETlafIAqmrlpRtFSQAQRDKRVE--------DVIaeLRLRQCADTRVGnmyVRG--LSGGERRRVSIGVQLLWNPG 236
Cdd:COG4618 422 IAEN---IA-----R-FGDADPEKVVAaaklagvhEMI--LRLPDGYDTRIG---EGGarLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 237 ILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRsdIFRLFDLVLLMTSGTPIYLGAAQ 302
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDGRVQAFGPRD 551
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
92-275 |
4.72e-14 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 71.98 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggKIKSGQIWINGQPSSPQLV------RKCVAHVRQHNQLLpNL 165
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQ--TLEGKVHWSNKNESEPSFEatrsrnRYSVAYAAQKPWLL-NA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQMrlprtfsQAQRDKRVEDVIA---ELRLRQCAD-TRVGNmyvRG--LSGGERRRVSIGVQLLWNPGILI 239
Cdd:cd03290 94 TVEENITFGSPF-------NKQRYKAVTDACSlqpDIDLLPFGDqTEIGE---RGinLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 767915028 240 LDEPTSGLDSFTAHNLVKT--LSRLAKGNRLVLISLHQ 275
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEgiLKFLQDDKRTLVLVTHK 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
99-277 |
5.43e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.73 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 99 VRSGQMLAIIGSSGCGRASLLDVITGRGHGGkikSGQIWINGQPSS-------PQLVRKCVAHVRQHNQLLPNLTVRETL 171
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGS---SGEVSLVGQPLHqmdeearAKLRAKHVGFVFQSFMLIPTLNALENV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAqmrLPRTFSQAQRDKRVEDVIAELRLRQcadtRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 251
Cdd:PRK10584 110 ELPA---LLRGESSRQSRNGAKALLEQLGLGK----RLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*...
gi 767915028 252 AHNLVKTLSRLAK--GNRLVLISlHQPR 277
Cdd:PRK10584 182 GDKIADLLFSLNRehGTTLILVT-HDLQ 208
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
92-293 |
5.54e-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: 72.53 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSpQLVRKCVAHVRQHNQLL--------- 162
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLE---KPAQGTVSFRGQDLY-QLDRKQRRAFRRDVQLVfqdspsavn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLAfiAQMRLPRTFSQAQRDKRVEDVIAELRLRqcadTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:TIGR02769 103 PRMTVRQIIG--EPLRHLTSLDESEQKARIAELLDMVGLR----SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767915028 243 PTSGLDSFTAHNLVKTLSRL--AKGNRLVLISlHQPRSdIFRLFDLVLLMTSG 293
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLqqAFGTAYLFIT-HDLRL-VQSFCQRVAVMDKG 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
89-273 |
7.32e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.36 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 89 ELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQLV---RKCVAHVRQH--NQLLp 163
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLL---LPEAGTITVGGMVLSEETVwdvRRQVGMVFQNpdNQFV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVRETLAFIAQMR-LPRTfsqaQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:PRK13635 96 GATVQDDVAFGLENIgVPRE----EMVERVDQALRQVGMEDFLNREPHR-----LSGGQKQRVAIAGVLALQPDIIILDE 166
|
170 180 190
....*....|....*....|....*....|.
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLAKGNRLVLISL 273
Cdd:PRK13635 167 ATSMLDPRGRREVLETVRQLKEQKGITVLSI 197
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
92-275 |
9.81e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.54 E-value: 9.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITgrgHGGKIKSGQIWINGQ----------------PSSPQLVRKCVAHV 155
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCIN---FLEKPSEGSIVVNGQtinlvrdkdgqlkvadKNQLRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 156 RQHNQLLPNLTVRETLafiaqMRLPRT---FSQAQRDKRVEDVIAELRLrqcaDTRVGNMYVRGLSGGERRRVSIGVQLL 232
Cdd:PRK10619 98 FQHFNLWSHMTVLENV-----MEAPIQvlgLSKQEARERAVKYLAKVGI----DERAQGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767915028 233 WNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQ 275
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
95-276 |
1.05e-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: 70.21 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP---SSPQLVRKCvAHVRQHNQLLPNLTVRETL 171
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLS---PPLAGRVLLNGGPldfQRDSIARGL-LYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFiaqmrlprtFSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 251
Cdd:cd03231 95 RF---------WHADHSDEQVEEALARVGLNGFEDRPVAQ-----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....*
gi 767915028 252 AHNLVKTLSRLAKGNRLVLISLHQP 276
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
93-275 |
1.11e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 72.91 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQP----SSPQLV--RKCVAHVRQHNQLLPNLT 166
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE---RPTSGRVLVDGQDltalSEKELRkaRRQIGMIFQHFNLLSSRT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFiaQMRLPRTfSQAQRDKRVEDVIAelrlrqcadtRVG-----NMYVRGLSGGERRRVSIGVQLLWNPGILILD 241
Cdd:PRK11153 99 VFDNVAL--PLELAGT-PKAEIKARVTELLE----------LVGlsdkaDRYPAQLSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 767915028 242 EPTSGLDSFTAHNLvktLSRLAKGNR-----LVLISlHQ 275
Cdd:PRK11153 166 EATSALDPATTRSI---LELLKDINRelgltIVLIT-HE 200
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
92-262 |
1.46e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIWINGQPSSpQLVRKCVAHVRQHNQLLPNLTVRE 169
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGdpRATSGRIVFDGKDITDWQTA-KIMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLA---FIAQmrlpRTFSQaQRDKRVEDVIAELRLRQCadTRVGNMyvrglSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:PRK11614 100 NLAmggFFAE----RDQFQ-ERIKWVYELFPRLHERRI--QRAGTM-----SGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170
....*....|....*.
gi 767915028 247 LDSFTAHNLVKTLSRL 262
Cdd:PRK11614 168 LAPIIIQQIFDTIEQL 183
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
92-276 |
1.80e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.60 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrGHGGKIKSGQIWINGQPSS-------PQLVRKCVAHVRQHNQLLPN 164
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNIL---GCLDKPTSGTYRVAGQDVAtldadalAQLRREHFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLafiaqmRLPRTF---SQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLwNPGILIL- 240
Cdd:PRK10535 101 LTAAQNV------EVPAVYaglERKQRLLRAQELLQRLGLEDRVEYQPSQ-----LSGGQQQRVSIARALM-NGGQVILa 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 767915028 241 DEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQP 276
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
92-264 |
2.16e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPS---SPQLVRKCVAHVRQHNQLLPNlTVR 168
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLI---SPTSGTLLFEGEDIstlKPEIYRQQVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMRlprtfSQAQRDKRVEDVIAELRLrqcaDTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:PRK10247 99 DNLIFPWQIR-----NQQPDPAIFLDDLERFAL----PDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170
....*....|....*.
gi 767915028 249 SFTAHNLVKTLSRLAK 264
Cdd:PRK10247 170 ESNKHNVNEIIHRYVR 185
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
92-274 |
3.07e-13 |
|
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: 69.42 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITgrgHGGKIKSGQIWINGQPSSP---QLVRKCVAHVRQHNQLLPNlTVR 168
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLE---NFYQPQGGQVLLDGKPISQyehKYLHSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRlrQCADTRVGNmyvRG--LSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:cd03248 106 DNIAYGLQSCSFECVKEAAQKAHAHSFISELA--SGYDTEVGE---KGsqLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180
....*....|....*....|....*...
gi 767915028 247 LDSFTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:cd03248 181 LDAESEQQVQQALYDWPERRTVLVIAHR 208
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
93-275 |
3.26e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.57 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITG----RGHggkiksgqIWINGQP---SSPQLVRKCVAHVRQhNQLLPNL 165
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyQGS--------LKINGIElreLDPESWRKHLSWVGQ-NPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAF----IAQMRLPRTFSQAQRDKRVEdviaelRLRQCADTRVGNMyVRGLSGGERRRVSIGVQLLWNPGILILD 241
Cdd:PRK11174 438 TLRDNVLLgnpdASDEQLQQALENAWVSEFLP------LLPQGLDTPIGDQ-AAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190
....*....|....*....|....*....|....
gi 767915028 242 EPTSGLDSFTAHNLVKTLSRLAKGNRLVLISlHQ 275
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQ 543
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
92-304 |
3.47e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.08 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIK-SGQIWING----QPSSPQLvRKCVAHVRQHNQLLPN 164
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRliEIYDSKIKvDGKVLYFGkdifQIDAIKL-RKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFIAQmrlprtfSQAQRDKR-----VEDVIAELRLRQCADTRVgNMYVRGLSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK14246 105 LSIYDNIAYPLK-------SHGIKEKReikkiVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 240 LDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISlHQPRSdIFRLFDLVLLMTSGTPIYLGAAQHM 304
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQQ-VARVADYVAFLYNGELVEWGSSNEI 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
92-248 |
3.59e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR--GHGGKIKSGQiwiNgqpsspqlVRkcVAHVRQHNQLL-PNLTVR 168
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGElePDSGTVKLGE---T--------VK--IGYFDQHQEELdPDKTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLafiaqmrlprtfSQAQRDKRvedviaELRLRQC----------ADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGIL 238
Cdd:COG0488 398 DEL------------RDGAPGGT------EQEVRGYlgrflfsgddAFKPVGV-----LSGGEKARLALAKLLLSPPNVL 454
|
170
....*....|
gi 767915028 239 ILDEPTSGLD 248
Cdd:COG0488 455 LLDEPTNHLD 464
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
93-275 |
3.70e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.02 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITgrgHGGKIKSGQIWING----QPSSPQLVRKcVAHVRQHNQLLPNLTVR 168
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS---RLMTPAHGHVWLDGehiqHYASKEVARR-IGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 EtlaFIAQMRLPRTFSQAQRDKRVEDVIAElRLRQCADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:PRK10253 100 E---LVARGRYPHQPLFTRWRKEDEEAVTK-AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190
....*....|....*....|....*....|.
gi 767915028 249 SFTAHNLVKTLSRL--AKGNRL--VLISLHQ 275
Cdd:PRK10253 176 ISHQIDLLELLSELnrEKGYTLaaVLHDLNQ 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
85-316 |
3.81e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.17 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 85 QNSCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQ---LVRKCVAHVRQH--N 159
Cdd:PRK13648 18 QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE---KVKSGEIFYNNQAITDDnfeKLRKHIGIVFQNpdN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 160 QLLPNlTVRETLAF-IAQMRLPrtFSQAQRdkRVEDVIAELRLRQCADTRVgnmyvRGLSGGERRRVSIGVQLLWNPGIL 238
Cdd:PRK13648 95 QFVGS-IVKYDVAFgLENHAVP--YDEMHR--RVSEALKQVDMLERADYEP-----NALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 239 ILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLfDLVLLMTSGTPIYLGAAQHM---VQYFTAIGYPC 315
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGTVYKEGTPTEIfdhAEELTRIGLDL 243
|
.
gi 767915028 316 P 316
Cdd:PRK13648 244 P 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
92-299 |
6.98e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 68.33 E-value: 6.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkIKSGQIWINGQPSSPqlvrkcvahVRQHNQLLPNLTVRETL 171
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP---PDSGTVTVRGRVSSL---------LGLGGGFNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAQMrlpRTFSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFT 251
Cdd:cd03220 106 YLNGRL---LGLSRKEIDEKIDEIIEFSELGDFIDLPVKT-----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915028 252 AHNLVKTLSRLAKGNRLVLISLHQPRSdIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
92-248 |
9.25e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.97 E-value: 9.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIkSGQIWINGQPSSPQLVRKCVAH----V---RQHNQLLPN 164
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRNI-SGTVFKDGKEVDVSTVSDAIDAglayVtedRKGYGLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRE--TLAfiaqmRLPRTFSQAQRDKRVEDVIAElRLRQCADTRVGNMY--VRGLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:NF040905 355 DDIKRniTLA-----NLGKVSRRGVIDENEEIKVAE-EYRKKMNIKTPSVFqkVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
....*...
gi 767915028 241 DEPTSGLD 248
Cdd:NF040905 429 DEPTRGID 436
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
92-302 |
1.23e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLL-------DVITGRGHGGKIKSGQIWINGQPSSPQLVRKCVAHVRQHNQLLPN 164
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrllELNEEARVEGEVRLFGRNIYSPDVDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFIAQM-RLPRtfSQAQRDKRVEDVIAELRLRQCADTRVgNMYVRGLSGGERRRVSIGVQLLWNPGILILDEP 243
Cdd:PRK14267 100 LTIYDNVAIGVKLnGLVK--SKKELDERVEWALKKAALWDEVKDRL-NDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 244 TSGLDSFTAHNLVKTLSRLAKGNRLVLISlHQPrSDIFRLFDLVLLMTSGTPIYLGAAQ 302
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEYTIVLVT-HSP-AQAARVSDYVAFLYLGKLIEVGPTR 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
85-293 |
1.23e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.60 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 85 QNSCELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQLV---RKCVAHVRQH--N 159
Cdd:PRK13650 16 EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL---EAESGQIIIDGDLLTEENVwdiRHKIGMVFQNpdN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 160 QLLpNLTVRETLAF-IAQMRLPRTFSQAQRDKRVEDV-IAELRLRQCADtrvgnmyvrgLSGGERRRVSIGVQLLWNPGI 237
Cdd:PRK13650 93 QFV-GATVEDDVAFgLENKGIPHEEMKERVNEALELVgMQDFKEREPAR----------LSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 238 LILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIfRLFDLVLLMTSG 293
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNG 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
92-294 |
1.52e-12 |
|
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: 67.52 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRAS----LLDVITgrghggkIKSGQIWINGQPSS---PQLVRKCVAHVRQHNQLLPN 164
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE-------LSSGSILIDGVDISkigLHDLRSRISIIPQDPVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 lTVRETLAFiaqmrlprtFSQAQrDKRVEDVIAELRLRQCADTRVGNMYVR------GLSGGERRRVSIGVQLLWNPGIL 238
Cdd:cd03244 93 -TIRSNLDP---------FGEYS-DEELWQALERVGLKEFVESLPGGLDTVveeggeNLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 239 ILDEPTSGLDSFTAHNLVKTLsRLAKGNRLVLISLHqprsdifRL-----FDLVLLMTSGT 294
Cdd:cd03244 162 VLDEATASVDPETDALIQKTI-REAFKDCTVLTIAH-------RLdtiidSDRILVLDKGR 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
92-314 |
1.85e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.72 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQLVRKCVAHVRQHNQLLPNLTVRETL 171
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLI---KSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAQmrlprtFSQAQ--RDKRVEDV--------IAELRLRQCADTRVGNMYVR---------GLSGGERRRVSIGVQLL 232
Cdd:PRK13631 119 SMVFQ------FPEYQlfKDTIEKDImfgpvalgVKKSEAKKLAKFYLNKMGLDdsylerspfGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 233 WNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLM------TSGTPIYLGAAQHMVQ 306
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMdkgkilKTGTPYEIFTDQHIIN 271
|
....*...
gi 767915028 307 YfTAIGYP 314
Cdd:PRK13631 272 S-TSIQVP 278
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
92-293 |
1.85e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.80 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGR----ASLLDVITGrghGGKIKSGQIWINGQPSSPQLVR-KCVAHVRQH-----NQL 161
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKsltcAAALGILPA---GVRQTAGRVLLDGKPVAPCALRgRKIATIMQNprsafNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 162 LPNLT-VRETLAFIAQMRLPRTFSQAQRDKRVEDViaelrlrqcadTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:PRK10418 96 HTMHThARETCLALGKPADDATLTAALEAVGLENA-----------ARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 241 DEPTSGLDSFTAHNLVKTLSRLAKGNRL-VLISLHqprsD---IFRLFDLVLLMTSG 293
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALgMLLVTH----DmgvVARLADDVAVMSHG 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
94-290 |
1.98e-12 |
|
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: 65.53 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKIKSGQIWINGQPsspqlvrkcvahVRQHNqllPNLTVRETLAF 173
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSG---LYKPDSGEILVDGKE------------VSFAS---PRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 174 IAQmrlprtfsqaqrdkrvedviaelrlrqcadtrvgnmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAH 253
Cdd:cd03216 80 VYQ----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190
....*....|....*....|....*....|....*...
gi 767915028 254 NLVKTLSRL-AKGNRLVLISlHQPRsDIFRLFDLVLLM 290
Cdd:cd03216 120 RLFKVIRRLrAQGVAVIFIS-HRLD-EVFEIADRVTVL 155
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
92-274 |
3.15e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggkIKSGQIWINGQPSSPQLVRKCVAHVRQHNQ-------LLPN 164
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVR---LASGKISILGQPTRQALQKNLVAYVPQSEEvdwsfpvLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFIAQMRLPRTFSQAQRDKRVEDV-IAELRLRQCADtrvgnmyvrgLSGGERRRVSIGVQLLWNPGILILDEP 243
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAALARVdMVEFRHRQIGE----------LSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190
....*....|....*....|....*....|.
gi 767915028 244 TSGLDSFTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
92-277 |
3.27e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.01 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR-GHggKIKSGQIWINGQpsspqlvrkcvahvrqhnqllpNLTVRET 170
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpKY--EVTSGSILLDGE----------------------DILELSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 ---------LAF--------IAQMRLPRTFSQAQRD---------KRVEDVIAELRLRQCADTRvgnmYV-RGLSGGERR 223
Cdd:COG0396 72 deraragifLAFqypveipgVSVSNFLRTALNARRGeelsareflKLLKEKMKELGLDEDFLDR----YVnEGFSGGEKK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767915028 224 RVSIgVQ-LLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPR 277
Cdd:COG0396 148 RNEI-LQmLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQR 201
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
92-299 |
3.73e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.32 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIWINgQPSSPQLvRKCVAHVRQH--NQLLpNLTV 167
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTISKILTGllKPQSGEIKIDGITIS-KENLKEI-RKKIGIIFQNpdNQFI-GATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAF-IAQMRLPRtfsqaqrdKRVEDVIAELRlrqcadTRVGnM--YVR----GLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:PRK13632 102 EDDIAFgLENKKVPP--------KKMKDIIDDLA------KKVG-MedYLDkepqNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 241 DEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFrLFDLVLLMTSGTPIYLG 299
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQG 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
95-293 |
4.28e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.33 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGkikSGQIWINGQP----SSPQLVRKcVAHVRQHNQLLPNLTVREt 170
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT---AGTVLVAGDDvealSARAASRR-VASVPQDTSLSFEFDVRQ- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 lafIAQM-RLPRT--FSQAQRDKR--VEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK09536 97 ---VVEMgRTPHRsrFDTWTETDRaaVERAMERTGVAQFADRPVTS-----LSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767915028 246 GLDsftAHNLVKTLS---RLAKGNRLVLISLHqprsDI---FRLFDLVLLMTSG 293
Cdd:PRK09536 169 SLD---INHQVRTLElvrRLVDDGKTAVAAIH----DLdlaARYCDELVLLADG 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
92-294 |
4.52e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 65.63 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRgHGGKIKSGQIWINGQpsspqlvrkcvahvrqhnqLLPNLTVRE-- 169
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEVTEGEILFKGE-------------------DITDLPPEEra 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 ----TLAFiaqmrlprtfsqaQRDKRVEDVIAELRLRQCADtrvgnmyvrGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:cd03217 76 rlgiFLAF-------------QYPPEIPGVKNADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRsdIFRLF--DLVLLMTSGT 294
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIITHYQR--LLDYIkpDRVHVLYDGR 182
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
94-306 |
4.84e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 66.97 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFkvRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIWINGQPSSPQL--VRKCVAHVRQ--HNQLLPNlTV 167
Cdd:PRK13634 27 NVSI--PSGSYVAIIGHTGSGKSTLLQHLNGllQPTSGTVTIGERVITAGKKNKKLkpLRKKVGIVFQfpEHQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFiaqmrLPRTF--SQAQRDKRVEDVIA------ELRLRQCADtrvgnmyvrgLSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK13634 104 EKDICF-----GPMNFgvSEEDAKQKAREMIElvglpeELLARSPFE----------LSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 240 LDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQ 306
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
92-274 |
5.34e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 65.67 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWING------QPSSPQLVRKCVAHVRQHNQLLPNL 165
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIE---RPSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAfiaqmrLPRTFSQAQRD---KRVEDVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:PRK10908 95 TVYDNVA------IPLIIAGASGDdirRRVSAALDKVGLLDKAKN-----FPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|..
gi 767915028 243 PTSGLDSFTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
92-293 |
7.83e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.36 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQ---LVRKCVAHVRQH--NQLLpNLT 166
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL---KPTSGSVLIRGEPITKEnirEVRKFVGLVFQNpdDQIF-SPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAF-IAQMRLprtfSQAQRDKRVEDVIAELRLRQCADtRVGNMyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK13652 96 VEQDIAFgPINLGL----DEETVAHRVSSALHMLGLEELRD-RVPHH----LSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRL-VLISLHQpRSDIFRLFDLVLLMTSG 293
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMtVIFSTHQ-LDLVPEMADYIYVMDKG 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
94-272 |
8.13e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RGHGGkiKSGQIWINGQPSSPQLVR----KCVAHVRQHNQLLPNLTVR 168
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGT--YEGEIIFEGEELQASNIRdterAGIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLaFIAQ-------MRLPRTFSQAQRdkrvedVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILD 241
Cdd:PRK13549 101 ENI-FLGNeitpggiMDYDAMYLRAQK------LLAQLKLDINPATPVGN-----LGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190
....*....|....*....|....*....|....
gi 767915028 242 EPTSGL-DSFTAH--NLVKTLSrlAKGNRLVLIS 272
Cdd:PRK13549 169 EPTASLtESETAVllDIIRDLK--AHGIACIYIS 200
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
92-275 |
8.76e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.21 E-value: 8.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGR---ASLLDvitgrgHGGKIKSGQIWINGQPSSP---QLVRKCVAHVRQHNQLLpNL 165
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKstvAALLQ------NLYQPTGGQVLLDGVPLVQydhHYLHRQVALVGQEPVLF-SG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRlrQCADTRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFP--NGYDTEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190
....*....|....*....|....*....|
gi 767915028 246 GLDSFTAHNLVKTLSRlakGNRLVLISLHQ 275
Cdd:TIGR00958 647 ALDAECEQLLQESRSR---ASRTVLLIAHR 673
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
93-276 |
1.24e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQPsspqlVRKCVAHVRQhnQLL---------P 163
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARP---DAGEVLWQGEP-----IRRQRDEYHQ--DLLylghqpgikT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVRETLAFIAQMrlprtfSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEP 243
Cdd:PRK13538 88 ELTALENLRFYQRL------HGPGDDEALWEALAQVGLAGFEDVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|...
gi 767915028 244 TSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQP 276
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
94-248 |
1.26e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSPQ--LVRKCVAHVRQHNQLLPNLTVRETL 171
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL---PASEGEAWLFGQPVDAGdiATRRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 172 AFIAQM-RLPRtfsqAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:NF033858 361 ELHARLfHLPA----AEIAARVAEMLERFDLADVADALPDS-----LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
51-299 |
1.32e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 51 LEVRDLNYQVDLASQVPWFeqlaqfkmpWTSPSCQNScelgIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHG 128
Cdd:PRK15079 9 LEVADLKVHFDIKDGKQWF---------WQPPKTLKA----VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGlvKATD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 129 GKIK-SGQIWINGQPSSPQLVRKCVAHVRQH--NQLLPNLTVRETLAFIAQMRLPRtFSQAQRDKRVEDVIAELRLRQca 205
Cdd:PRK15079 76 GEVAwLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEIIAEPLRTYHPK-LSRQEVKDRVKAMMLKVGLLP-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 206 dtRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFD 285
Cdd:PRK15079 153 --NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISD 230
|
250
....*....|....
gi 767915028 286 LVLLMTSGTPIYLG 299
Cdd:PRK15079 231 RVLVMYLGHAVELG 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
91-293 |
1.76e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RghggKIKSGQIWINGQPSSPQLVRKCVA-------HVRQHNQLL 162
Cdd:PRK15439 278 GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGlR----PARGGRIMLNGKEINALSTAQRLArglvylpEDRQSSGLY 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLAFIAQMRLPrTFSQAQRDKRV-EDVIAELRLRqCADtrvGNMYVRGLSGGERRRVSIGVQLLWNPGILILD 241
Cdd:PRK15439 354 LDAPLAWNVCALTHNRRG-FWIKPARENAVlERYRRALNIK-FNH---AEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 242 EPTSGLDSFTAHNLVKTLSRLAKGNRLVL-ISlhqprSD---IFRLFDLVLLMTSG 293
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQNVAVLfIS-----SDleeIEQMADRVLVMHQG 479
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
92-248 |
2.12e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 64.67 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLL-------DVItgrgHGGKIkSGQIWINGQ----PS-SPQLVRKCVAHVRQHn 159
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLI----PGARV-EGEILLDGEdiydPDvDVVELRRRVGMVFQK- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 160 qllPN---LTVRETLAFiaqmrLPRTfsQAQRDKRVEDVIAELRLRQCA------DtRVgNMYVRGLSGGERRRVSIGVQ 230
Cdd:COG1117 101 ---PNpfpKSIYDNVAY-----GLRL--HGIKSKSELDEIVEESLRKAAlwdevkD-RL-KKSALGLSGGQQQRLCIARA 168
|
170
....*....|....*...
gi 767915028 231 LLWNPGILILDEPTSGLD 248
Cdd:COG1117 169 LAVEPEVLLMDEPTSALD 186
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
94-262 |
2.30e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.79 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghGGKIK--SGQIWINGQpSSPQL-------VRKCVAHVRQHNQLLPN 164
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLI-----GGQIApdHGEILFDGE-NIPAMsrsrlytVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFI--AQMRLPRTFSQAQRDKRVEDViaelRLRQCAdtrvgNMYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:PRK11831 99 MNVFDNVAYPlrEHTQLPAPLLHSTVMMKLEAV----GLRGAA-----KLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180
....*....|....*....|
gi 767915028 243 PTSGLDSFTAHNLVKTLSRL 262
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISEL 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
92-308 |
2.59e-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: 66.36 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRgHGGKIKSGQI-----------WINGQPSSPQLVRKCVAHVRQHNQ 160
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM-DQYEPTSGRIiyhvalcekcgYVERPSKVGEPCPVCGGTLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 161 LLPNLTVRETLAF---IAQMrLPRTFSQAQRDKRVEDVI---------AELRLRQCAD----TRVGN--MYV-RGLSGGE 221
Cdd:TIGR03269 95 DFWNLSDKLRRRIrkrIAIM-LQRTFALYGDDTVLDNVLealeeigyeGKEAVGRAVDliemVQLSHriTHIaRDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 222 RRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLI-SLHQPRSdIFRLFDLVLLMTSGTPIYLGA 300
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVlTSHWPEV-IEDLSDKAIWLENGEIKEEGT 252
|
....*...
gi 767915028 301 AQHMVQYF 308
Cdd:TIGR03269 253 PDEVVAVF 260
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
94-323 |
2.63e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.14 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIWINGQPSSPQL--VRKCVAHVRQ--HNQLLPNlTV 167
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTVGDIVVSSTSKQKEIkpVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFiaqmrLPRTFSQAQRDkrVEDVIAElRLRQCADTRvgNMYVRG---LSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:PRK13643 103 LKDVAF-----GPQNFGIPKEK--AEKIAAE-KLEMVGLAD--EFWEKSpfeLSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 245 SGLDSFTAHNLVKTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQ---YFTAIGYPCPRYSNP 321
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHIISCGTPSDVFQevdFLKAHELGVPKATHF 251
|
..
gi 767915028 322 AD 323
Cdd:PRK13643 252 AD 253
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
92-302 |
3.32e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.37 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkiksgqIWINGQ-----PSS------PQLVRkcvahvrqhnq 160
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-----------LWPYGSgriarPAGarvlflPQRPY----------- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 161 lLPNLTVRETLAFIAQmrlPRTFSqaqrDKRVEDVIAELRLRQCADtR--VGNMYVRGLSGGERRRVSIGVQLLWNPGIL 238
Cdd:COG4178 437 -LPLGTLREALLYPAT---AEAFS----DAELREALEAVGLGHLAE-RldEEADWDQVLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767915028 239 ILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISlHqpRSDIFRLFDLVLLMTSGTPIYLGAAQ 302
Cdd:COG4178 508 FLDEATSALDEENEAALYQLLREELPGTTVISVG-H--RSTLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
92-314 |
4.36e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRA----SLLDVItgRGHGGKIKSGQIWIN---------GQPSSPQL--VRKC-VAHV 155
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL--EQAGGLVQCDKMLLRrrsrqvielSEQSAAQMrhVRGAdMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 156 RQH--NQLLPNLTVRETLAfiAQMRLPRTFSQAQRDKRVEDVIAELRLRQcADTRVGNmYVRGLSGGERRRVSIGVQLLW 233
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIA--ESIRLHQGASREEAMVEAKRMLDQVRIPE-AQTILSR-YPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 234 NPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQhmvQYFTAIGY 313
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE---QIFHAPQH 262
|
.
gi 767915028 314 P 314
Cdd:PRK10261 263 P 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
92-248 |
7.83e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPSSpQLVRKCVAHVRQHNQLL--------- 162
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLE---SPSQGNVSWRGEPLA-KLNRAQRKAFRRDIQMVfqdsisavn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLAfiAQMRLPRTFSQAQRDKRVEDVIAELRLR-QCADTRVGNMyvrglSGGERRRVSIGVQLLWNPGILILD 241
Cdd:PRK10419 104 PRKTVREIIR--EPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQL-----SGGQLQRVCLARALAVEPKLLILD 176
|
....*..
gi 767915028 242 EPTSGLD 248
Cdd:PRK10419 177 EAVSNLD 183
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
92-273 |
8.85e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.28 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKSGQIWINGQPSSPQL---VRKCVAHVRQH--NQLLpNLT 166
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTvwdIREKVGIVFQNpdNQFV-GAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFIAQMR-LPRTfsqaQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK13640 102 VGDDVAFGLENRaVPRP----EMIKIVRDVLADVGMLDYIDSEPAN-----LSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180
....*....|....*....|....*...
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISL 273
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVISI 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
92-293 |
9.21e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RGHggkiKSGQIWINGQP----SSPQLVRKCVAHV---RQHNQLLP 163
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGiREK----SAGTITLHGKKinnhNANEAINHGFALVteeRRSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVrETLAFIAQMRLPRTFSQAQRDKRVED----VIAELRLRQCA-DTRVGNmyvrgLSGGERRRVSIGVQLLWNPGIL 238
Cdd:PRK10982 340 YLDI-GFNSLISNIRNYKNKVGLLDNSRMKSdtqwVIDSMRVKTPGhRTQIGS-----LSGGNQQKVIIGRWLLTQPEIL 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 239 ILDEPTSGLD---SFTAHNLVKTLSRLAKGnrLVLISLHQPrsDIFRLFDLVLLMTSG 293
Cdd:PRK10982 414 MLDEPTRGIDvgaKFEIYQLIAELAKKDKG--IIIISSEMP--ELLGITDRILVMSNG 467
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
92-247 |
1.37e-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: 64.08 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RGHGGkiKSGQIWINGQPSSPQLVR----KCVAHVRQHNQLLPNLT 166
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGT--WDGEIYWSGSPLKASNIRdterAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFIAQMRLP-RTFSQAQRDKRVEDVIAELRLRQCADTRVgnmyVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:TIGR02633 95 VAENIFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTRP----VGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
|
..
gi 767915028 246 GL 247
Cdd:TIGR02633 171 SL 172
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
95-302 |
1.42e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkikSGQIWINGQP----SSPQLvrkcvAHVR----QHNQLLPNLT 166
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG----SGSIQFAGQPleawSAAEL-----ARHRaylsQQQTPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAfiaqMRLPRTFSQAQRDKRVEDVIAELRLrqcaDTRVGNMyVRGLSGGERRRVSI-GVQL-LW---NPG--ILI 239
Cdd:PRK03695 86 VFQYLT----LHQPDKTRTEAVASALNEVAEALGL----DDKLGRS-VNQLSGGEWQRVRLaAVVLqVWpdiNPAgqLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 240 LDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHqprsDI---FRLFDLVLLMTSGTPIYLGAAQ 302
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSH----DLnhtLRHADRVWLLKQGKLLASGRRD 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
92-293 |
1.82e-10 |
|
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: 60.89 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASL-------LDVITGRghggkiksgqIWINGQPSSpqlvrkcvahvrqhnqLLPN 164
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLilalfrfLEAEEGK----------IEIDGIDIS----------------TIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFIAQMrlPRTFSQAQR------DKRV-EDVIAELRLRQCADTrvgnmyvrgLSGGERRRVSIGVQLLWNPGI 237
Cdd:cd03369 78 EDLRSSLTIIPQD--PTLFSGTIRsnldpfDEYSdEEIYGALRVSEGGLN---------LSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 238 LILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISlHQPRSDIfrLFDLVLLMTSG 293
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIA-HRLRTII--DYDKILVMDAG 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
91-308 |
2.01e-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: 64.65 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKIKSGQIWINGQP--SSPQLVRKCVAHVRQHNQLLPNLTVR 168
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG---DTTVTSGDATVAGKSilTNISDVHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMR-LPrtfsqAQRDKRVED-VIAELRLRQCADtRVGNMYvrglSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:TIGR01257 2031 EHLYLYARLRgVP-----AEEIEKVANwSIQSLGLSLYAD-RLAGTY----SGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915028 247 LDSFTAHNLVKTLSRLAKGNRLVLISLHQpRSDIFRLFDLVLLMTSGTPIYLGAAQHMVQYF 308
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIIREGRAVVLTSHS-MEECEALCTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
92-275 |
4.33e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRG--HGGKIKSGQIWINGQP-SSPQL----VRKCVAHVRQHNQLLPn 164
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlNPEVTITGSIVYNGHNiYSPRTdtvdLRKEIGMVFQQPNPFP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFiaQMRLprtfsQAQRDKRVEDVIAELRLRQCA-----DTRVGNMYVrGLSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK14239 100 MSIYENVVY--GLRL-----KGIKDKQVLDEAVEKSLKGASiwdevKDRLHDSAL-GLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 767915028 240 LDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLI--SLHQ 275
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVtrSMQQ 209
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
106-293 |
6.06e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.43 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 106 AIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQPSS--------PQLVRKcVAHVRQHNQLLPNLTVRETLAFiaQM 177
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRP---QKGRIVLNGRVLFdaekgiclPPEKRR-IGYVFQDARLFPHYKVRGNLRY--GM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 178 RlprTFSQAQRDKRVEDV-IAELRLRqcadtrvgnmYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLV 256
Cdd:PRK11144 102 A---KSMVAQFDKIVALLgIEPLLDR----------YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 767915028 257 KTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSG 293
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
92-302 |
6.11e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 60.31 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIWINGQ---PSSPQLVRKCVAHVRQHNQLLPNLT 166
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEARVSGEVYLDGQdifKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFIAQM-RLPRtfSQAQRDKRVEDVIAELRLRQCADTRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK14247 99 IFENVALGLKLnRLVK--SKKELQERVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDifRLFDLVLLMTSGTPIYLGAAQ 302
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDMTIVLVTHFPQQAA--RISDYVAFLYKGQIVEWGPTR 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
94-248 |
7.48e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITG-RghggKIKSGQIWING----QPSSPQLVRKCVAHVRQ---HNqLLPNL 165
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGaR----KIQQGRVEVLGgdmaDARHRRAVCPRIAYMPQglgKN-LYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAqmrlpRTFSQ--AQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEP 243
Cdd:NF033858 94 SVFENLDFFG-----RLFGQdaAERRRRIDELLRATGLAPFADRPAGK-----LSGGMKQKLGLCCALIHDPDLLILDEP 163
|
....*
gi 767915028 244 TSGLD 248
Cdd:NF033858 164 TTGVD 168
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
92-272 |
7.57e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.39 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIwINGQPSSPQLVRKCVAHVRQHNQL-LPNLTVR 168
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGllRPQKGKVLVSGI-DTGDFSKLQGIRKLVGIVFQNPETqFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQ-MRLPRTfsqaQRDKRVEDVIAELRLRqcadtRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:PRK13644 97 EDLAFGPEnLCLPPI----EIRKRVDRALAEIGLE-----KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180
....*....|....*....|....*.
gi 767915028 248 DSFTAHNLVKTLSRL-AKGNRLVLIS 272
Cdd:PRK13644 168 DPDSGIAVLERIKKLhEKGKTIVYIT 193
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
93-310 |
7.58e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.71 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 93 QNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkI---KSGQIWINGQPSSpqlvrkcvahvrqhnqLL------- 162
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAG------IlepTSGRVEVNGRVSA----------------LLelgagfh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLAFIAQMRlprTFSQAQRDKRVEDVI--AELRlrqcadtRVGNMYVRGLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:COG1134 101 PELTGRENIYLNGRLL---GLSRKEIDEKFDEIVefAELG-------DFIDQPVKTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 241 DEPTS-GLDSFTAHNLVKTLSRLAKGNRLVLISlHQPRSdIFRLFDLVLLMTSGTPIYLGAAQHMVQYFTA 310
Cdd:COG1134 171 DEVLAvGDAAFQKKCLARIRELRESGRTVIFVS-HSMGA-VRRLCDRAIWLEKGRLVMDGDPEEVIAAYEA 239
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
92-299 |
1.45e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKIKSGQIWINGQpSSPQLVRKCVAH-----VRQHNQLLPNLT 166
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG---IHEPTKGTITINNI-NYNKLDHKLAAQlgigiIYQELSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLaFIAqmRLP-------RTFSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK09700 97 VLENL-YIG--RHLtkkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 240 LDEPTSGLDSFTAHNLVKTLSRLAK-GNRLVLISlHQpRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYIS-HK-LAEIRRICDRYTVMKDGSSVCSG 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
92-309 |
1.46e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.97 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGK--IKSGQIWINGQPSSPQL---VRKCVAHVRQHNQLLPN 164
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGvlEPTSGEvnVRVGDEWVDMTKPGPDGrgrAKRYIGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFIAQMRLPRTFSQAQ----------RDKRVEDVIaelrlrqcadtrvgNMYVRGLSGGERRRVSIGVQLLWN 234
Cdd:TIGR03269 380 RTVLDNLTEAIGLELPDELARMKavitlkmvgfDEEKAEEIL--------------DKYPDELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 235 PGILILDEPTSGLDSFT----AHNLVKtlSRLAKGNRLVLISlHQprSDIFR-LFDLVLLMTSGTPIYLGAAQHMVQYFT 309
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITkvdvTHSILK--AREEMEQTFIIVS-HD--MDFVLdVCDRAALMRDGKIVKIGDPEEIVEELT 520
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
95-274 |
1.52e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.36 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIWINgqPSSPQLVRKCVAHVRQH--NQLLPNlTVRET 170
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGiyLPQRGRVKVMGREVN--AENEKWVRSKVGLVFQDpdDQVFSS-TVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 LAFIAQ-MRLprtfSQAQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 249
Cdd:PRK13647 101 VAFGPVnMGL----DKDEVERRVEEALKAVRMWDFRDKPPYH-----LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180
....*....|....*....|....*
gi 767915028 250 FTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIVATH 196
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
95-248 |
1.90e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 95 LSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGkikSGQIWINGQPSSPQLVRKCVAHVRQHNQLLPNLTVRETLAFI 174
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVE---SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 175 AQMrlprtfsQAQRDKRVE-DVIAELRLRQCADTrvgnmYVRGLSGGERRRVSIGvQLLWNPGIL-ILDEPTSGLD 248
Cdd:PRK13543 107 CGL-------HGRRAKQMPgSALAIVGLAGYEDT-----LVRQLSAGQKKRLALA-RLWLSPAPLwLLDEPYANLD 169
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
90-248 |
2.39e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.64 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 90 LGIQNLSFKVRSGQMLAIIGSSGCGRASLL-------DVITGRGHGGKIKSGQIWINGQPSSPQLVRKCVAHVRQHNQLL 162
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRVEGKVTFHGKNLYAPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNlTVRETLAFIAQMR---------LPRTFSQAQRDKRVEDviaelRLRQCADTrvgnmyvrgLSGGERRRVSIGVQLLW 233
Cdd:PRK14243 104 PK-SIYDNIAYGARINgykgdmdelVERSLRQAALWDEVKD-----KLKQSGLS---------LSGGQQQRLCIARAIAV 168
|
170
....*....|....*
gi 767915028 234 NPGILILDEPTSGLD 248
Cdd:PRK14243 169 QPEVILMDEPCSALD 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
96-271 |
3.26e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 96 SFKVRSGQMLAIIGSSGCGRASLLDVITGrghGGKIKSGQIWINGQPSSPQLVRKCVAHV-------RQHNQLLPNLTVR 168
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYG---ATRRTAGQVYLDGKPIDIRSPRDAIRAGimlcpedRKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQmrlpRTFSQAQ--RDKRVEDVIAELRLRQCA-DTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK11288 350 DNINISAR----RHHLRAGclINNRWEAENADRFIRSLNiKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180
....*....|....*....|....*.
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLI 271
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLF 451
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
92-272 |
5.28e-09 |
|
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: 55.15 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRG--HGGKIKSGQiwingqpsspqlvrkcvahvrqhnqllpnltvRE 169
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELepDEGIVTWGS--------------------------------TV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAFIAQmrlprtfsqaqrdkrvedviaelrlrqcadtrvgnmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 249
Cdd:cd03221 64 KIGYFEQ----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180
....*....|....*....|...
gi 767915028 250 FTAHNLVKTLSRLaKGNrLVLIS 272
Cdd:cd03221 104 ESIEALEEALKEY-PGT-VILVS 124
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
31-262 |
6.42e-09 |
|
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: 58.98 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 31 LFSSESDNSLYFTYSGQPN-TLEVRDLNYQVDLASQVpwfeqlaqfkmpwtspscqnscelgIQNLSFKVRSGQMLAIIG 109
Cdd:TIGR01193 453 LVDSEFINKKKRTELNNLNgDIVINDVSYSYGYGSNI-------------------------LSDISLTIKMNSKTTIVG 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 110 SSGCGRASLLDVITGRGHGGkikSGQIWINGQPSSpQLVRkcvAHVRQHNQLLPNL------TVRETLAFIAQmrlpRTF 183
Cdd:TIGR01193 508 MSGSGKSTLAKLLVGFFQAR---SGEILLNGFSLK-DIDR---HTLRQFINYLPQEpyifsgSILENLLLGAK----ENV 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 184 SQAQRDKRVEdvIAELR-----LRQCADTRVgNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKT 258
Cdd:TIGR01193 577 SQDEIWAACE--IAEIKddienMPLGYQTEL-SEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNN 653
|
....
gi 767915028 259 LSRL 262
Cdd:TIGR01193 654 LLNL 657
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
92-286 |
8.69e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.97 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGH-GGKIK-SGQIWINGQPSSPQLV-----RKCVAHVRQHNQLLPn 164
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElESEVRvEGRVEFFNQNIYERRVnlnrlRRQVSMVHPKPNLFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFiaQMRLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:PRK14258 102 MSVYDNVAY--GVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALD-LSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767915028 245 SGLD---SFTAHNLVKTLsRLAKGNRLVLISLHQPRsdIFRLFDL 286
Cdd:PRK14258 179 FGLDpiaSMKVESLIQSL-RLRSELTMVIVSHNLHQ--VSRLSDF 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
94-248 |
8.99e-09 |
|
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: 58.54 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRA----SLLDVItgrGHGGKIKSGQIWINGQP----SSPQL--VR-KCVAHVRQH--NQ 160
Cdd:COG4172 28 GVSFDIAAGETLALVGESGSGKSvtalSILRLL---PDPAAHPSGSILFDGQDllglSERELrrIRgNRIAMIFQEpmTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 161 LLPNLTV----RETLafiaqmRLPRTFSQAQRDKRVEDVIAELRLRQcADTRVgNMYVRGLSGGERRRVSIGVQLLWNPG 236
Cdd:COG4172 105 LNPLHTIgkqiAEVL------RLHRGLSGAAARARALELLERVGIPD-PERRL-DAYPHQLSGGQRQRVMIAMALANEPD 176
|
170
....*....|..
gi 767915028 237 ILILDEPTSGLD 248
Cdd:COG4172 177 LLIADEPTTALD 188
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
94-248 |
1.03e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.06 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRG--HGGKIKSGQIWINGQPSSPQL--VRKCVAHVRQ--HNQLLPNlTV 167
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvpTQGSVRVDDTLITSTSKNKDIkqIRKKVGLVFQfpESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 168 RETLAFiaqmrLPRTFSQAQRDKrveDVIAELRLRQcadtrVG---NMYVRG---LSGGERRRVSIGVQLLWNPGILILD 241
Cdd:PRK13649 104 LKDVAF-----GPQNFGVSQEEA---EALAREKLAL-----VGiseSLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLD 170
|
....*..
gi 767915028 242 EPTSGLD 248
Cdd:PRK13649 171 EPTAGLD 177
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
86-272 |
1.05e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 86 NSCELGIQNLSFKVRSGQM--------------LAIIGSSGCGRASLLDVITGRGhggKIKSGQIWINGQPS---SPQLV 148
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYY---PLTEGEIRLDGRPLsslSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 149 RKCVAHVRQHNQLLPNltvretlAFIAQMRLPRTFSQAQRDKRVEDV-IAELrLRQCAD---TRVGNmyvRG--LSGGER 222
Cdd:PRK10790 414 RQGVAMVQQDPVVLAD-------TFLANVTLGRDISEEQVWQALETVqLAEL-ARSLPDglyTPLGE---QGnnLSVGQK 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915028 223 RRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLIS 272
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
92-293 |
1.19e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkiksgqiwINGQPSSPQLVRKCVAHVRQHNQLLpNLTVRETL 171
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE------------LSHAETSSVVIRGSVAYVPQVSWIF-NATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAQMrlprtfsQAQRDKRVEDVIA---ELRLRQCAD-TRVGNMYVrGLSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:PLN03232 700 LFGSDF-------ESERYWRAIDVTAlqhDLDLLPGRDlTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767915028 248 DSFTAHNLVKT-LSRLAKGNRLVLIS--LHqprsdIFRLFDLVLLMTSG 293
Cdd:PLN03232 772 DAHVAHQVFDScMKDELKGKTRVLVTnqLH-----FLPLMDRIILVSEG 815
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
92-299 |
1.32e-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: 56.79 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR--GHGGKIK-SGQIWINGQPSspqlvrkcvahvrqhnQLLPNlTVR 168
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGElePSEGKIKhSGRISFSSQFS----------------WIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMRLPRTFSQAQRDKRVEDViaeLRLRQCADTRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:cd03291 116 ENIIFGVSYDEYRYKSVVKACQLEEDI---TKFPEKDNTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767915028 249 SFTAHNLV-KTLSRL-AKGNRLVLISlhqpRSDIFRLFDLVLLMTSGTPIYLG 299
Cdd:cd03291 192 VFTEKEIFeSCVCKLmANKTRILVTS----KMEHLKKADKILILHEGSSYFYG 240
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
92-306 |
1.37e-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: 58.42 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHggKIKsGQIWINGQpsspqlvrkcVAHVRQHnQLLPNLTVRETL 171
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD--KVE-GHVHMKGS----------VAYVPQQ-AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAQMRLPRTFSQAQrdkrVEDVIAELRLRQCAD-TRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 250
Cdd:TIGR00957 720 LFGKALNEKYYQQVLE----ACALLPDLEILPSGDrTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915028 251 TA----HNLVKTLSRLAKGNRLVL---ISlHQPRSDIfrlfdlVLLMTSGTPIYLGAAQHMVQ 306
Cdd:TIGR00957 795 VGkhifEHVIGPEGVLKNKTRILVthgIS-YLPQVDV------IIVMSGGKISEMGSYQELLQ 850
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
92-294 |
2.72e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.56 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGQIWINGQPSSPQL--VRKCVAHVRQ--HNQLLPNL 165
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllKPTTGTVTVDDITITHKTKDKYIrpVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFiaqmrlPRTFSQAQrdKRVEDVIAELRLRQCADTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK13646 103 VEREIIFG------PKNFKMNL--DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767915028 246 GLDSFTAHNLVKTLSRLA-KGNRLVLISLHQpRSDIFRLFDLVLLMTSGT 294
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtDENKTIILVSHD-MNEVARYADEVIVMKEGS 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
92-248 |
3.26e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASlldviTGRGHGGKIKS--GQIWINGQ------PSSPQLVRKCVAHVRQ--HNQL 161
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKST-----TGRALLRLVESqgGEIIFNGQridtlsPGKLQALRRDIQFIFQdpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 162 LPNLTVRETLafIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCADTRvgnmYVRGLSGGERRRVSIGVQLLWNPGILILD 241
Cdd:PRK10261 415 DPRQTVGDSI--MEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWR----YPHEFSGGQRQRICIARALALNPKVIIAD 488
|
....*..
gi 767915028 242 EPTSGLD 248
Cdd:PRK10261 489 EAVSALD 495
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
92-279 |
3.97e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWingqpsspqlVRKCVAHVRQHNQLLpNLTVRETL 171
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF---EISEGRVW----------AERSIAYVPQQAWIM-NATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAQmrlprtfsqaQRDKRVEDVIA----ELRLRQCA---DTRVGNMYVrGLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:PTZ00243 742 LFFDE----------EDAARLADAVRvsqlEADLAQLGgglETEIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767915028 245 SGLDSFTAHNLVKT--LSRLAKGNRlvLISLHQ----PRSD 279
Cdd:PTZ00243 811 SALDAHVGERVVEEcfLGALAGKTR--VLATHQvhvvPRAD 849
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
94-248 |
5.02e-08 |
|
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: 56.10 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFkvRSGQMLAIIGSSGCGRASLLDVITGRGhggKIKSGQIWingqpssPQLVRKcVAHVRQHNQLLPNLTVRET--- 170
Cdd:TIGR03719 25 SLSF--FPGAKIGVLGLNGAGKSTLLRIMAGVD---KDFNGEAR-------PQPGIK-VGYLPQEPQLDPTKTVRENvee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 -LAFIAQM--RLPRTFSQ-----AQRDK------RVEDVIA-------ELRLRQCADT-RV--GNMYVRGLSGGERRRVS 226
Cdd:TIGR03719 92 gVAEIKDAldRFNEISAKyaepdADFDKlaaeqaELQEIIDaadawdlDSQLEIAMDAlRCppWDADVTKLSGGERRRVA 171
|
170 180
....*....|....*....|..
gi 767915028 227 IGVQLLWNPGILILDEPTSGLD 248
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
89-275 |
7.11e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 89 ELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKIKSGQIWINGQPSSPQLV--RKCVAHVRQHNQLLPNLT 166
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL---LNPEKGEILFERQSIKKDLCtyQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAFIAQmrlprtFSQAQRDkrVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVsiGVQLLWNPG--ILILDEPT 244
Cdd:PRK13540 91 LRENCLYDIH------FSPGAVG--ITELCRLFSLEHLIDYPCGL-----LSSGQKRQV--ALLRLWMSKakLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|.
gi 767915028 245 SGLDSFTAHNLVKTLSRLAKGNRLVLISLHQ 275
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
206-275 |
1.10e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915028 206 DTRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLaKG--NRLVLISLHQ 275
Cdd:PTZ00265 570 ETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL-KGneNRITIIIAHR 639
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
189-248 |
2.63e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 2.63e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915028 189 DKRVEdvIAELRLRqC--ADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:PRK11819 142 DSQLE--IAMDALR-CppWDAKVTK-----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
92-293 |
2.74e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.48 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghgGKIKSGQIWINGQPSS-------PQLVRKCVAHvrQHNQLLPN 164
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM---IEPTSGELLIDDHPLHfgdysyrSQRIRMIFQD--PSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTVRETLAFiaQMRLPRTFSQAQRDKRVEDVIAELRLRqcadTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:PRK15112 104 QRISQILDF--PLRLNTDLEPEQREKQIIETLRQVGLL----PDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767915028 245 SGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSG 293
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
161-285 |
3.29e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 161 LLPNLTVRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQcaDTRVGNmYVRGLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:PTZ00265 1306 MLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKY--DTNVGP-YGKSLSGGQKQRIAIARALLREPKILLL 1382
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767915028 241 DEPTSGLDSFTAHNLVKTLSRLA-KGNRLVLISLHQ----PRSDIFRLFD 285
Cdd:PTZ00265 1383 DEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRiasiKRSDKIVVFN 1432
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
91-300 |
3.54e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 52.32 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR--GHGGKIKSGQIWINGQPSSPQLV---RKCVAHVRQ--HNQLLP 163
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiiSETGQTIVGDYAIPANLKKIKEVkrlRKEIGLVFQfpEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NlTVRETLAFiAQMRLPRTFSQAQrdKRVEDVIAELRLRQcadtrvgnMYVR----GLSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK13645 106 E-TIEKDIAF-GPVNLGENKQEAY--KKVPELLKLVQLPE--------DYVKrspfELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 240 LDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGA 300
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
92-300 |
3.57e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIksgqIWiNGQP---SSPQLV--RKCVAHVRQH-NQLLP 163
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllRPQKGAV----LW-QGKPldySKRGLLalRQQVATVFQDpEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVRETLAF-IAQMRLPrtfsQAQRDKRVEDVIAEL---RLRQcadtrvgnMYVRGLSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK13638 92 YTDIDSDIAFsLRNLGVP----EAEITRRVDEALTLVdaqHFRH--------QPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 240 LDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPrSDIFRLFDLVLLMTSGTPIYLGA 300
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDI-DLIYEISDAVYVLRQGQILTHGA 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
92-300 |
3.71e-07 |
|
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: 53.76 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR--GHGGKIK-SGQIwingqPSSPQLvrkcvahvrqhNQLLPNlTVR 168
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGElePSEGKIKhSGRI-----SFSPQT-----------SWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQMRLPRTFSQAQRDKRVEDVIaelRLRQCADTRVGNMYVRgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:TIGR01271 505 DNIIFGLSYDEYRYTSVIKACQLEEDIA---LFPEKDKTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767915028 249 SFTAHNLVKT-LSRL-AKGNRLVLISlhqpRSDIFRLFDLVLLMTSGTPIYLGA 300
Cdd:TIGR01271 581 VVTEKEIFEScLCKLmSNKTRILVTS----KLEHLKKADKILLLHEGVCYFYGT 630
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
92-288 |
5.06e-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: 49.84 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkiksgqIWINGQPSSPQLVRKCVAHVRQHnQLLPNLTVRETL 171
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-----------LWPWGSGRIGMPEGEDLLFLPQR-PYLPLGTLREQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 172 AFIAQMRLprtfsqaqrdkrvedviaelrlrqcadtrvgnmyvrglSGGERRRVSIGVQLLWNPGILILDEPTSGLDsft 251
Cdd:cd03223 85 IYPWDDVL--------------------------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALD--- 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 767915028 252 aHNLVKTLSRLAKGNRLVLISL-HQPRSDIFrlFDLVL 288
Cdd:cd03223 124 -EESEDRLYQLLKELGITVISVgHRPSLWKF--HDRVL 158
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
92-251 |
5.06e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.60 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG--RGHGGKIKSGqiwingqpSSPqlvrkcVAHVR-------QHNQLL 162
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGleTPSAGELLAG--------TAP------LAEARedtrlmfQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLAFiaqmrlprTFSQAQRDkRVEDVIAELRLRQCAdtrvgNMYVRGLSGGERRRVSIGVQLLWNPGILILDE 242
Cdd:PRK11247 94 PWKKVIDNVGL--------GLKGQWRD-AALQALAAVGLADRA-----NEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
....*....
gi 767915028 243 PTSGLDSFT 251
Cdd:PRK11247 160 PLGALDALT 168
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
92-320 |
5.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.63 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKiksGQIWINGQPSSPQLV---RKCVAHVRQH--NQLLpNLT 166
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFE---GKVKIDGELLTAENVwnlRRKIGMVFQNpdNQFV-GAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VRETLAF-IAQMRLPRTfsqaQRDKRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK13642 99 VEDDVAFgMENQGIPRE----EMIKRVDEALLAVNMLDFKTREPAR-----LSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGNRLVLISLHQPRSDIFRlFDLVLLMTSGTPIYLGAAQHMV---QYFTAIGYPCPRYSN 320
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFatsEDMVEIGLDVPFSSN 246
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
92-248 |
5.79e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.03 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRA----SLLDVITGRGH-GGKIK-SGQIWINGQPSSPQLVR-KCVAHVRQH--NQLL 162
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRiGGSATfNGREILNLPEKELNKLRaEQISMIFQDpmTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 163 PNLTVRETLAFIAQMRLPRTFSQA-QRDKRVEDV--IAELRLRQcadtrvgNMYVRGLSGGERRRVSIGVQLLWNPGILI 239
Cdd:PRK09473 112 PYMRVGEQLMEVLMLHKGMSKAEAfEESVRMLDAvkMPEARKRM-------KMYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
....*....
gi 767915028 240 LDEPTSGLD 248
Cdd:PRK09473 185 ADEPTTALD 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
190-274 |
5.87e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.86 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 190 KRVEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLV 269
Cdd:COG1245 191 GKLDELAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYV 265
|
....*
gi 767915028 270 LISLH 274
Cdd:COG1245 266 LVVEH 270
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
94-293 |
6.11e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGrghggkIKS---GQIWINGQ------PSSPQLVRKCVAHvrQHNQLLPN 164
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTG------IYTrdaGSILYLGKevtfngPKSSQEAGIGIIH--QELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 165 LTV-------RETLAFIAQMRLPRTFSQAqrDKrvedVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGI 237
Cdd:PRK10762 94 LTIaeniflgREFVNRFGRIDWKKMYAEA--DK----LLARLNLRFSSDKLVGE-----LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 238 LILDEPTSGL-DSFTAhNLVKTLSRL-AKGNRLVLISlHQPRsDIFRLFDLVLLMTSG 293
Cdd:PRK10762 163 IIMDEPTDALtDTETE-SLFRVIRELkSQGRGIVYIS-HRLK-EIFEICDDVTVFRDG 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
216-274 |
7.29e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.63 E-value: 7.29e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 216 GLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
92-271 |
9.00e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.28 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRA-SLLDVITGRGHGGKIKSGQIWINGQ-------PSSPQLVRKCVAHVRQH--NQL 161
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRVMAEKLEFNGQdlqriseKERRNLVGAEVAMIFQDpmTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 162 LPNLTVreTLAFIAQMRLPRTFSQAQRDKRVEDVIaelrlrqcadTRVG--------NMYVRGLSGGERRRVSIGVQLLW 233
Cdd:PRK11022 103 NPCYTV--GFQIMEAIKVHQGGNKKTRRQRAIDLL----------NQVGipdpasrlDVYPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 767915028 234 NPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLI 271
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALV 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
92-271 |
1.36e-06 |
|
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: 48.86 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLL-DVITgrghggkiKSGQIWINGQPSSPQlvrkcvahvrqhnqllPNLTVret 170
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVnEGLY--------ASGKARLISFLPKFS----------------RNKLI--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 laFIAQMrlprtfsqaqrdKRVEDV-IAELRLRQCADTrvgnmyvrgLSGGERRRVSIGVQLLWNPG--ILILDEPTSGL 247
Cdd:cd03238 64 --FIDQL------------QFLIDVgLGYLTLGQKLST---------LSGGELQRVKLASELFSEPPgtLFILDEPSTGL 120
|
170 180
....*....|....*....|....*
gi 767915028 248 DSFTAHNLVKTLSRL-AKGNRLVLI 271
Cdd:cd03238 121 HQQDINQLLEVIKGLiDLGNTVILI 145
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
92-275 |
1.60e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.57 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKIKS-GQIWINGQPSSPQLVrkcvahvrqhNQLLPNLTVRET 170
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGcVDVPDNQFGREASLI----------DAIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 LAFIAQMRLprtfsqaqrdkrvEDVIAELRLrqcadtrvgnmyVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLDSF 250
Cdd:COG2401 116 VELLNAVGL-------------SDAVLWLRR------------FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*..
gi 767915028 251 TAHNLVKTLSRLAK--GNRLVLISLHQ 275
Cdd:COG2401 171 TAKRVARNLQKLARraGITLVVATHHY 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
94-253 |
1.72e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRghggkiksgqiwINGQPSSPQLVRKCVAHVRQHNQLLpNLTVRETLAF 173
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGE------------LPPRSDASVVIRGTVAYVPQVSWIF-NATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 174 IAQMrlprtfsQAQRDKRVEDVIA---ELRLRQCAD-TRVGNmyvRG--LSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:PLN03130 702 GSPF-------DPERYERAIDVTAlqhDLDLLPGGDlTEIGE---RGvnISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
....*.
gi 767915028 248 DsftAH 253
Cdd:PLN03130 772 D---AH 774
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
92-248 |
1.78e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITG---RGH-------GGKIKSGQ-IWIngqpsspqlVRKCVAHVRQ--H 158
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpQGYsndltlfGRRRGSGEtIWD---------IKKHIGYVSSslH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 159 NQLLPNLTVRETL--AFIAQMRLPRTFSQAQRdKRVEDVIAELRLrqcaDTRVGNMYVRGLSGGERRRVSIGVQLLWNPG 236
Cdd:PRK10938 347 LDYRVSTSVRNVIlsGFFDSIGIYQAVSDRQQ-KLAQQWLDILGI----DKRTADAPFHSLSWGQQRLALIVRALVKHPT 421
|
170
....*....|..
gi 767915028 237 ILILDEPTSGLD 248
Cdd:PRK10938 422 LLILDEPLQGLD 433
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
99-274 |
2.34e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 99 VRSGQMLAIIGSSGCGRASLLdvitgrghggKIKSGQIWIN-GQPSSP--------------------QLVRK--CVAHV 155
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAV----------KILSGELIPNlGDYEEEpswdevlkrfrgtelqnyfkKLYNGeiKVVHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 156 RQHNQLLPNL---TVRETLAfiaqmrlprtfsqaQRDKR--VEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQ 230
Cdd:PRK13409 166 PQYVDLIPKVfkgKVRELLK--------------KVDERgkLDEVVERLGLENILDRDISE-----LSGGELQRVAIAAA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767915028 231 LLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKgNRLVLISLH 274
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEH 269
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
99-274 |
2.74e-06 |
|
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: 49.29 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 99 VRSGQMLAIIGSSGCGRASLLdvitgrghggKIKSGQIWIN-GQPSSPQLVRKCVAHVRQ---HNQL--LPNLTVRETLA 172
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTAL----------KILAGKLKPNlGKFDDPPDWDEILDEFRGselQNYFtkLLEGDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 173 FIAQMRLPRTFSQA------QRDKR--VEDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPT 244
Cdd:cd03236 93 PQYVDLIPKAVKGKvgellkKKDERgkLDELVDQLELRHVLDRNIDQ-----LSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|
gi 767915028 245 SGLDSFTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
92-262 |
3.95e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLdvitgrghggKIKSGQIwingQPSSPQLvrKC-----VAHVRQHNQLL-PNL 165
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLL----------KLMLGQL----QADSGRI--HCgtkleVAYFDQHRAELdPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQmrlprTFSQAQRDKRV----EDVI-AELRLRQCadtrvgnmyVRGLSGGERRRVSIGVQLLWNPGILIL 240
Cdd:PRK11147 399 TVMDNLAEGKQ-----EVMVNGRPRHVlgylQDFLfHPKRAMTP---------VKALSGGERNRLLLARLFLKPSNLLIL 464
|
170 180
....*....|....*....|..
gi 767915028 241 DEPTSGLDsftahnlVKTLSRL 262
Cdd:PRK11147 465 DEPTNDLD-------VETLELL 479
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
92-276 |
4.77e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.75 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVItgrghggkiksGQIW--INGQPSSPqlvRKCVAHVRQHNQLLPNLTVRE 169
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRIL-----------GELWpvYGGRLTKP---AKGKLFYVPQRPYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLafIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNMYVRG----LSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:TIGR00954 534 QI--IYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQDwmdvLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|..
gi 767915028 246 GLdsftAHNLVKTLSRLAKGNRLVLISL-HQP 276
Cdd:TIGR00954 612 AV----SVDVEGYMYRLCREFGITLFSVsHRK 639
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
203-248 |
5.93e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.32 E-value: 5.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 767915028 203 QCADtRVG--------NMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:PRK15134 136 NCLD-RVGirqaakrlTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALD 188
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
91-272 |
6.18e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 91 GIQNLSFKVRSGQMLAIIGSSGCG--RASLLDVITGRGHGGKIKSGQIWINGQPSspqLVRKCVAHVRQHNQLLPNLTVR 168
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRA---LRRTIG*HRPVR*GRRESFSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 ETLAFIAQ-MRLPRTFSQAqrdkRVEDVIAELRLRQCADtRVGNMYvrglSGGERRRVSIGVQLLWNPGILILDEPTSGL 247
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARA----RADELLERFSLTEAAG-RAAAKY----SGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
170 180
....*....|....*....|....*
gi 767915028 248 DSFTAHNLVKTLSRLAKGNRLVLIS 272
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGATVLLT 200
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
94-329 |
8.80e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.78 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSgqMLAIIGSSGCGRASLL-------DVITGRGHGGKI------------------KSGQIWINGQPSSPQLV 148
Cdd:PRK14271 41 SMGFPARA--VTSLMGPTGSGKTTFLrtlnrmnDKVSGYRYSGDVllggrsifnyrdvlefrrRVGMLFQRPNPFPMSIM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 149 RKCVAHVRQHnQLLPnltvRETLAFIAQMRLprtfsqaqrdkrvedviAELRLRQCADTRVGNMYVRgLSGGERRRVSIG 228
Cdd:PRK14271 119 DNVLAGVRAH-KLVP----RKEFRGVAQARL-----------------TEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 229 VQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAkgNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQHMvqyf 308
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL---- 249
|
250 260
....*....|....*....|.
gi 767915028 309 taigYPCPRYSNPADFYVDLT 329
Cdd:PRK14271 250 ----FSSPKHAETARYVAGLS 266
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
89-248 |
1.20e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.23 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 89 ELGIQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR--GHGGKI----KSGQIWINGQPSSPQ---LVRKCVAHVRQH- 158
Cdd:PRK11701 19 RKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARlaPDAGEVhyrmRDGQLRDLYALSEAErrrLLRTEWGFVHQHp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 159 -NQLLPNLT----VRETLAFIAQMRLPRTFSQAQR-DKRVEdvIAELRLrqcaDTRvgnmyVRGLSGGERRRVSIGVQLL 232
Cdd:PRK11701 99 rDGLRMQVSaggnIGERLMAVGARHYGDIRATAGDwLERVE--IDAARI----DDL-----PTTFSGGMQQRLQIARNLV 167
|
170
....*....|....*.
gi 767915028 233 WNPGILILDEPTSGLD 248
Cdd:PRK11701 168 THPRLVFMDEPTGGLD 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
94-293 |
1.28e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 94 NLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGgkiKSGQIWINGQP----SSPQLVRKCVAHVRQHNQLLPNLTVRE 169
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQK---DSGSILFQGKEidfkSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 170 TLAFiaqMRLPRTFSQAQRDKRVEDVIA---ELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSG 246
Cdd:PRK10982 93 NMWL---GRYPTKGMFVDQDKMYRDTKAifdELDIDIDPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767915028 247 LDSFTAHNLVKTLSRL-AKGNRLVLISlHQpRSDIFRLFDLVLLMTSG 293
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLkERGCGIVYIS-HK-MEEIFQLCDEITILRDG 210
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
92-301 |
1.92e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.56 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGrgHGG-KIKSGQIWINGQpSSPQLVRKCVAHVR-----QHNQLLPNL 165
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAyKILEGDILFKGE-SILDLEPEERAHLGiflafQYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLafiaqmRLPRTFSQAQRDKRVEDVIAELRLRQCADTRVG------NMYV-RGLSGGERRRVSIGVQLLWNPGIL 238
Cdd:CHL00131 100 SNADFL------RLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGmdpsflSRNVnEGFSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 239 ILDEPTSGLDSFTAHNLVKTLSRLA-KGNRLVLISLHQprsdifRLF-----DLVLLMTSGTPIYLGAA 301
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQ------RLLdyikpDYVHVMQNGKIIKTGDA 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
92-248 |
1.96e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.65 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGhggkiksgqiwingQPSSPQLVRKC---VAHVRQHNQLLPNLtvr 168
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV--------------APDEGVIKRNGklrIGYVPQKLYLDTTL--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 169 etlafiaqmrlPRTFSQAQRDK---RVEDVIAELRLRQCADTRVGNMyvRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK09544 83 -----------PLTVNRFLRLRpgtKKEDILPALKRVQAGHLIDAPM--QKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
...
gi 767915028 246 GLD 248
Cdd:PRK09544 150 GVD 152
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
171-276 |
2.42e-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: 45.04 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 171 LAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRqcadtrvgnmyVRGLSGGERRRVSIGVQL---LWNPGIL-ILDEPTSG 246
Cdd:cd03227 43 LALGGAQSATRRRSGVKAGCIVAAVSAELIFT-----------RLQLSGGEKELSALALILalaSLKPRPLyILDEIDRG 111
|
90 100 110
....*....|....*....|....*....|
gi 767915028 247 LDSFTAHNLVKTLSRLAKGNRLVLISLHQP 276
Cdd:cd03227 112 LDPRDGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
99-249 |
3.23e-05 |
|
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: 45.86 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 99 VRSGQMLAIIGSSGCGRASLLDVITGRghggkIKSGqiwiNGQPSSPqlvRKCVAHVRQHNQLLPNLTVRETLAFIaqmr 178
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGV-----LKPD----EGDIEIE---LDTVSYKPQYIKADYEGTVRDLLSSI---- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 179 LPRTFSQAQRDKrveDVIAELRLRQCADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLDS 249
Cdd:cd03237 86 TKDFYTHPYFKT---EIAKPLQIEQILDREVPE-----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
90-272 |
3.50e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 46.23 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 90 LGIQNLSFKVRSGQMLAIIGSSGCGRASL------LDVITGrghggkiksGQIWINGQPSSPQL----VRKCVAHVRQH- 158
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIakhmnaLLIPSE---------GKVYVDGLDTSDEEnlwdIRNKAGMVFQNp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 159 -NQLLPNLtVRETLAFiaqmrLPRTFSQAQRD--KRVEDVIaelrlrqcadTRVGnMY------VRGLSGGERRRVSIGV 229
Cdd:PRK13633 95 dNQIVATI-VEEDVAF-----GPENLGIPPEEirERVDESL----------KKVG-MYeyrrhaPHLLSGGQKQRVAIAG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767915028 230 QLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAK--GNRLVLIS 272
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILIT 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
217-271 |
4.29e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 4.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 217 LSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLA-KGNRLVLI 271
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHqSGITLVLV 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
187-248 |
4.93e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 4.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767915028 187 QRDKRVEDVIAELRLRqcADTRVGNmyvrgLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:PRK11147 134 QLENRINEVLAQLGLD--PDAALSS-----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
92-277 |
4.98e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRgHGGKIKSGQIWINGQP----SSPQLVRKCVAHVRQH--------N 159
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR-EDYEVTGGTVEFKGKDllelSPEDRAGEGIFMAFQYpveipgvsN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 160 QLLPNLTVRETLAFIAQMRLPR-TFSQAqrdkrVEDVIAELRLRQCADTRVGNMyvrGLSGGERRRVSIGVQLLWNPGIL 238
Cdd:PRK09580 96 QFFLQTALNAVRSYRGQEPLDRfDFQDL-----MEEKIALLKMPEDLLTRSVNV---GFSGGEKKRNDILQMAVLEPELC 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 767915028 239 ILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLHQPR 277
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQR 206
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
274-328 |
5.11e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 46.05 E-value: 5.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767915028 274 HQPRSDIFRLF-DLVLLMTSGTPIYLGAAQHMVQYFTAIGYPCPRYSNPADFYVDL 328
Cdd:pfam19055 1 HQPSYTLFKMFdDLILLAKGGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDI 56
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
164-271 |
6.67e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVRETLAFIAQMRLPrtfsqAQRDKRVEDVIAELRLRQCADTRVGNMYV------RGLSGGERRRV----SIGVQLLw 233
Cdd:TIGR00630 435 ELSIREAHEFFNQLTLT-----PEEKKIAEEVLKEIRERLGFLIDVGLDYLslsraaGTLSGGEAQRIrlatQIGSGLT- 508
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767915028 234 npGIL-ILDEPTSGLDSFTAHNLVKTLSRLAK-GNRLVLI 271
Cdd:TIGR00630 509 --GVLyVLDEPSIGLHQRDNRRLINTLKRLRDlGNTLIVV 546
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
166-295 |
9.65e-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: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 166 TVRETLAFIAQMRLPRTFSQaqrdkrvEDVIAELRLrqcadTRVGNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:COG1245 417 TVEEFLRSANTDDFGSSYYK-------TEIIKPLGL-----EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767915028 246 GLDSFTAHNLVKTLSRLAKGN-RLVLISLHqprsDIFrLFDLV---LLMTSGTP 295
Cdd:COG1245 485 HLDVEQRLAVAKAIRRFAENRgKTAMVVDH----DIY-LIDYIsdrLMVFEGEP 533
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
164-269 |
1.24e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 164 NLTVRETLAFIAQMRLPrtfsqAQRDKRVEDVIAEL--RL--------------RQcADTrvgnmyvrgLSGGERRRV-- 225
Cdd:COG0178 432 ALSIDEALEFFENLELT-----EREAEIAERILKEIrsRLgflvdvgldyltldRS-AGT---------LSGGEAQRIrl 496
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 767915028 226 --SIGVQLLwnpGIL-ILDEPTSGL---DSftaHNLVKTLSRLAK-GNRLV 269
Cdd:COG0178 497 atQIGSGLV---GVLyVLDEPSIGLhqrDN---DRLIETLKRLRDlGNTVI 541
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
217-287 |
4.07e-04 |
|
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: 42.24 E-value: 4.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767915028 217 LSGGERRRV----SIGVQLLwnpGIL-ILDEPTSGLDSFTAHNLVKTLSRL-AKGNRLVLISlHQPrsDIFRLFDLV 287
Cdd:cd03270 138 LSGGEAQRIrlatQIGSGLT---GVLyVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVE-HDE--DTIRAADHV 208
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
217-295 |
4.28e-04 |
|
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: 42.60 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 217 LSGGERRRVSIGVQLLW---NPGILILDEPTSGLDSFTAHNLVKTLSRL-AKGNRLVLISlHQprSDIFRLFDLVL---- 288
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIE-HN--LDVIKCADWIIdlgp 246
|
90
....*....|....*
gi 767915028 289 --------LMTSGTP 295
Cdd:cd03271 247 eggdgggqVVASGTP 261
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
217-274 |
5.02e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.40 E-value: 5.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 217 LSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLA-KGNRLVLISLH 274
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeEGKKTALVVEH 130
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
213-248 |
9.08e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 9.08e-04
10 20 30
....*....|....*....|....*....|....*.
gi 767915028 213 YVRGLSGGERRRVSIGVQLLWNPGILILDEPTSGLD 248
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
217-274 |
2.18e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 2.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767915028 217 LSGGERRRVSIGVQLLW---NPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNRLVLISLH 274
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
209-271 |
2.49e-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: 41.15 E-value: 2.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767915028 209 VGNMYVR------GLSGGERRRVSIGVQLL---WNPGILILDEPTSGLDSFTAHNLVKTLSRL-AKGNRLVLI 271
Cdd:TIGR00630 816 VGLGYIRlgqpatTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLvDKGNTVVVI 888
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
178-276 |
3.13e-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: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 178 RLPRTFSQAQRDKRVEDVIAELRLRQCADTRVGNMYVRGLSGGERRRVSIGVQLL---WNPGILILDEPTSGLDSFTAHN 254
Cdd:pfam13304 198 NLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRR 277
|
90 100
....*....|....*....|..
gi 767915028 255 LVKTLSRLAKGNRLVLISLHQP 276
Cdd:pfam13304 278 LLELLKELSRNGAQLILTTHSP 299
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
92-248 |
3.31e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 92 IQNLSFKVRSGQMLAIIGSSGCGRASLLDVITGR--GHGGKIKsgqiWI-NGQPS-SPQlvrkcvahvrQHNQLLPN-LT 166
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGElePDSGTVK----WSeNANIGyYAQ----------DHAYDFENdLT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767915028 167 VREtlaFIAQMRLPRTFSQAQRdkrvedviAEL-RLRQCADTRvgNMYVRGLSGGERRRVSIGVQLLWNPGILILDEPTS 245
Cdd:PRK15064 401 LFD---WMSQWRQEGDDEQAVR--------GTLgRLLFSQDDI--KKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTN 467
|
...
gi 767915028 246 GLD 248
Cdd:PRK15064 468 HMD 470
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
217-272 |
3.77e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.17 E-value: 3.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767915028 217 LSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVKTLSRLAKGNR--LVLIS 272
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNttILLIS 216
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
217-277 |
6.75e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.36 E-value: 6.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 217 LSGGERRRVSIGVQLLW------NPGILILDEPTSGLDSFT-AHNLVKTL-SRLAKGNRLVLISLHQPR 277
Cdd:cd03240 116 CSGGEKVLASLIIRLALaetfgsNCGILALDEPTTNLDEENiEESLAEIIeERKSQKNFQLIVITHDEE 184
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
208-271 |
7.72e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 7.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767915028 208 RVGNMYVR-G-----LSGGERRRVSIGVQL--------LWnpgilILDEPTSGLDSFTAHNLVKTLSRLA-KGNRLVLI 271
Cdd:PRK00349 816 DVGLGYIKlGqpattLSGGEAQRVKLAKELskrstgktLY-----ILDEPTTGLHFEDIRKLLEVLHRLVdKGNTVVVI 889
|
|
| |
