|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
88-749 |
0e+00 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 633.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 88 LTYSIKSrrkmslsSIFPRRSNRLGAVAEAPTVGESMFTR---TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAN 164
Cdd:TIGR00955 1 LTYSWRN-------SDVFGRVAQDGSWKQLVSRLRGCFCRerpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 165 RIAKGSLK-GTVALNGEALESRLLKVISAYVMQDDLLFPMLTVEETLMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNA 243
Cdd:TIGR00955 74 RSPKGVKGsGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 244 AKTVIGDEG-HRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGL 322
Cdd:TIGR00955 154 ANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 323 LDRMIFLSRGQTVYSGSPSQLPLYFSEFGHPIPETDNRTEFALDLIRELEGSPggTKSLVEFNKSWQSMTK--HHQEKEE 400
Cdd:TIGR00955 234 FDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSE--NESRERIEKICDSFAVsdIGRDMLV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 401 ERNGLSLKEaisasisrGKLVSGASNtnpNPSSmvpTFANQFWVEMATLSKRSFLNSRRMPELIGIRLGTVMVTGFILAT 480
Cdd:TIGR00955 312 NTNLWSGKA--------GGLVKDSEN---MEGI---GYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 481 MFWQLDNSPKGVQERLG-FFAFAMSTTFYTTADALPVFLQERYIFMRETAYNAYRRLSYLVSHALVALPALAFLSLAFAA 559
Cdd:TIGR00955 378 IYLGQGLTQKGVQNINGaLFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 560 ATFWAVGLDGGISGFLFYFLIIFASFWAGNSFVTFLSGVVPHVMLGYTIVVAILAYFLLFSGFFINRDRIPSYWIWFHYL 639
Cdd:TIGR00955 458 ITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYL 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 640 SLVKYPYEAVLQNEFDDPVKCFVrgvqiFDNTplgsvpeplkvklletmsstlgtkiTTSTCLTTGADILQQNGVTDLTK 719
Cdd:TIGR00955 538 SWFRYGNEGLLINQWSDVDNIEC-----TSAN-------------------------TTGPCPSSGEVILETLSFRNADL 587
|
650 660 670
....*....|....*....|....*....|
gi 356576859 720 WNCFWITVAWGFFFRFLFYLSLLLGSKNKR 749
Cdd:TIGR00955 588 YLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
55-654 |
1.48e-85 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 284.08 E-value: 1.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 55 EASGDGSET---PVHHALDIPGIEPRS-LPFVLSFSNLTYSIKSRRKMSLSSIFPRrsnrlgAVAEAPTVGESMFT-RTK 129
Cdd:PLN03211 8 ENQNDGPDRskpPSQDSRDLPSLLLSScYPITLKFMDVCYRVKFENMKNKGSNIKR------ILGHKPKISDETRQiQER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEALESRLLKVIsAYVMQDDLLFPMLTVEET 209
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 210 LMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDST 289
Cdd:PLN03211 161 LVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 290 SAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQLPLYFSEFGHPIPETDNRTEFALDL-- 367
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLan 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 368 -IRELEG-----SPGGTKSLVefnKSWQSMTKHHQEKEEERNGLSLKEAISASISRGKLVSGASNTNpnpssmVPTFANQ 441
Cdd:PLN03211 321 gVCQTDGvsereKPNVKQSLV---ASYNTLLAPKVKAAIEMSHFPQANARFVGSASTKEHRSSDRIS------ISTWFNQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 442 FwvemATLSKRSfLNSRRMPELIGIRLGTVMVTGFILATMFWQLDNspKGVQERLGFFAF-AMSTTFYTTADALPVFLQE 520
Cdd:PLN03211 392 F----SILLQRS-LKERKHESFNTLRVFQVIAAALLAGLMWWHSDF--RDVQDRLGLLFFiSIFWGVFPSFNSVFVFPQE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 521 RYIFMRETAYNAYRRLSYLVSHALVALPALAFLSLAFAAATFWAVGLDGGISGFLFYFLIIFASFWAGNSFVTFLSGVVP 600
Cdd:PLN03211 465 RAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIM 544
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 356576859 601 HVMLGYTIVVAILAYFLLFSGFFINrdRIPSYWIWFHYLSLVKYPYEAVLQNEF 654
Cdd:PLN03211 545 DAKKASTIVTVTMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYRLLINVQY 596
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
128-338 |
6.58e-72 |
|
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: 233.70 E-value: 6.58e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLK-GTVALNGEALESRLLKVISAYVMQDDLLFPMLTV 206
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTsGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAAEFRLPRTLSKSKKSARVqaliDQLGLRNAAKTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGL 286
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRV----EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 356576859 287 DSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
131-739 |
2.12e-71 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 254.65 E-value: 2.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 131 LLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSL-KGTVALNGEALESRLLKvISAYVMQDDLLFPMLTVEET 209
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVItGGDRLVNGRPLDSSFQR-SIGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 210 LMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDEGHrGVSGGERRRVSIGTDIIHDP-ILLFLDEPTSGLDS 288
Cdd:TIGR00956 857 LRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGE-GLNVEQRKRLTIGVELVAKPkLLLFLDEPTSGLDS 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 289 TSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRG-QTVYSGSPSQ----LPLYFSEFG-HPIPETDNRTE 362
Cdd:TIGR00956 936 QTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDLGEnshtIINYFEKHGaPKCPEDANPAE 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 363 FALDLIreleGSPGGTKSLVEFNKSWQSMTKHHQEKEEernglsLKEaISASISRGKLVsgasntnpNPSSMVPTFANQF 442
Cdd:TIGR00956 1016 WMLEVI----GAAPGAHANQDYHEVWRNSSEYQAVKNE------LDR-LEAELSKAEDD--------NDPDALSKYAASL 1076
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 443 WVEMATLSKRSFLNSRRMPELIGIRLGTVMVTGFILATMFWQLDNSPKGVQERLgfFAFAMSTTFYTTA--DALPVFL-Q 519
Cdd:TIGR00956 1077 WYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQM--FAVFMATVLFNPLiqQYLPPFVaQ 1154
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 520 ERYIFMRETAYNAYRRLSYLVSHALVALPALAFLSLAFAAATFWAVGL--------DGGISGFLFYFLiIFASFWAGNSF 591
Cdd:TIGR00956 1155 RDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFywnasktgQVHERGVLFWLL-STMFFLYFSTL 1233
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 592 VTFLSGVVPHVMLGYTIVVAILAYFLLFSGFFINRDRIPSYWIWFHYLSLVKYPYEAVLQNEFDD-PVKCFVRGVQIFdN 670
Cdd:TIGR00956 1234 GQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADvPVTCKVKELLTF-N 1312
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 671 TPLGSVPEPLKVKLLETMSSTLGTKITTSTC----LTTGADILQQNGVTDLTKWNCFWITVAWGFFFR----FLFYL 739
Cdd:TIGR00956 1313 PPSGQTCGEYMKPYLENAGGYLLNPNATDSCsfcqYSYTNDFLEPISSKYSGRWRNFGIFIAFIFFNIiatvFFYWL 1389
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
82-338 |
4.01e-71 |
|
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: 230.52 E-value: 4.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 82 VLSFSNLTYSIKSRRkmslssifprrsnrlgavaeaptvgesmFTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDA 161
Cdd:cd03213 3 TLSFRNLTVTVKSSP----------------------------SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNA 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 162 LANRIAKGSLKGTVALNGEALESRLLKVISAYVMQDDLLFPMLTVEETLMFAAEFRlprtlskskksarvqalidqlglr 241
Cdd:cd03213 55 LAGRRTGLGVSGEVLINGRPLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR------------------------ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 242 naaktvigdeghrGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILG 321
Cdd:cd03213 111 -------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFE 177
|
250
....*....|....*..
gi 356576859 322 LLDRMIFLSRGQTVYSG 338
Cdd:cd03213 178 LFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
126-748 |
1.31e-62 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 228.45 E-value: 1.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 126 TRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRI--AKGSLKGTVALNGEALES--RLLKVISAYVMQDDLLF 201
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgFHIGVEGVITYDGITPEEikKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAAEFRLPRT----LSKSKKSARVQALI-DQLGLRNAAKTVIGDEGHRGVSGGERRRVSIGTDIIHDPIL 276
Cdd:TIGR00956 151 PHLTVGETLDFAARCKTPQNrpdgVSREEYAKHIADVYmATYGLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 277 LFLDEPTSGLDSTSAYMVVKVLQRIAQ-SGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQLPLYFSEFGHPIP 355
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGFKCP 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 356 ETDNRTEFALDLIRELEGSP-GGTKSLV-----EFNKSW------QSMTKHHQEKEEERNGLSLKEAISASISRGKlvsg 423
Cdd:TIGR00956 311 DRQTTADFLTSLTSPAERQIkPGYEKKVprtpqEFETYWrnspeyAQLMKEIDEYLDRCSESDTKEAYRESHVAKQ---- 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 424 aSNTNPNPSSMVPTFANQFWVEMAtlskRSFLNSRRMPELIGIRLGTVMVTGFILATMFWQLDNSPKGVQERLGFFAFAM 503
Cdd:TIGR00956 387 -SKRTRPSSPYTVSFSMQVKYCLA----RNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAI 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 504 stTFYTTADALPVFL--QERYIFMRETAYNAYRRLSYLVSHALVALPALAFLSLAFAAATFWAVGLDGGISGFLFYFLII 581
Cdd:TIGR00956 462 --LFNAFSSLLEIASmyEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLIL 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 582 FASFWAGNSFVTFLSGVVPHVMLGYTIVVAILAYFLLFSGFFINRDRIPSYWIWFHYLSLVKYPYEAVLQNEFDDPVkcf 661
Cdd:TIGR00956 540 FICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNEFHGRR--- 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 662 vrgvqiFDNT---PLGSVPEPLKVKlletmsstlgTKITTSTCLTTGADILQQNGVTDLT-------KWNCFWITVAW-- 729
Cdd:TIGR00956 617 ------FECSqyvPSGGGYDNLGVT----------NKVCTVVGAEPGQDYVDGDDYLKLSfqyynshKWRNFGIIIGFtv 680
|
650
....*....|....*....
gi 356576859 730 GFFFRFLFYLSLLLGSKNK 748
Cdd:TIGR00956 681 FFFFVYILLTEFNKGAKQK 699
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
80-338 |
3.23e-54 |
|
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: 185.14 E-value: 3.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 80 PFVLSFSNLTYSIKSRRKmslssifprrsnrlgavaeaptvgesmftrTKTLLNDISGEARDGEIMAVLGASGSGKSTLI 159
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGG------------------------------KRQLLNNISGYVKPGTLTALMGESGAGKTTLL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 160 DALANRIAKGSLKGTVALNGEALESRLLKvISAYVMQDDLLFPMLTVEETLMFAAEFRlprtlskskksarvqalidqlg 239
Cdd:cd03232 51 DVLAGRKTAGVITGEILINGRPLDKNFQR-STGYVEQQDVHSPNLTVREALRFSALLR---------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 240 lrnaaktvigdeghrGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRI 319
Cdd:cd03232 108 ---------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASI 172
|
250 260
....*....|....*....|
gi 356576859 320 LGLLDRMIFLSR-GQTVYSG 338
Cdd:cd03232 173 FEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
131-656 |
3.50e-54 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 202.77 E-value: 3.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 131 LLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEALESRLLKVISAYVMQDDLLFPMLTVEETL 210
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 211 MFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTS 290
Cdd:PLN03140 975 IYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 291 AYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSR-GQTVYSGSPSQ----LPLYFSEF-GHP-IPETDNRTEF 363
Cdd:PLN03140 1055 AAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLGRnshkIIEYFEAIpGVPkIKEKYNPATW 1134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 364 ALdlirELEGSPGGTKSLVEFNKSWQSMTKHHQEKeeernglSLKEAISAsisrgklvsgasntnPNPSSMVPTFANQF- 442
Cdd:PLN03140 1135 ML----EVSSLAAEVKLGIDFAEHYKSSSLYQRNK-------ALVKELST---------------PPPGASDLYFATQYs 1188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 443 ---WVEMATLSKRSFLNSRRMPELIGIRLGTVMVTGFILATMFWQLDNSPKGVQERLGFFAFAMSTTFY----TTADALP 515
Cdd:PLN03140 1189 qstWGQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTMVIGAMYAAVLFvginNCSTVQP 1268
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 516 VFLQERYIFMRETAYNAYRRLSYLVSHALVALPALAFLSLAFAAATFWAVGLDGGISGFLFYFLIIFASFWAGNSFVTFL 595
Cdd:PLN03140 1269 MVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMT 1348
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 596 SGVVPHVMLGYTIVVAILAYFLLFSGFFINRDRIPSYWIWFHYLSLVKYPYEAVLQNEFDD 656
Cdd:PLN03140 1349 VSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYGD 1409
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
129-343 |
1.77e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.84 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVIS--AYVMQDDLLFPMLTV 206
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTS--GEVRVLGEDVARDPAEVRRriGYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAAEFRlprTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGL 286
Cdd:COG1131 91 RENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGT-----LSGGMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 287 DSTSAYMVVKVLQRIAQSGSIVIMSIHqpsyrILG----LLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG1131 163 DPEARRELWELLRELAAEGKTVLLSTH-----YLEeaerLCDRVAIIDKGRIVADGTPDEL 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
129-343 |
3.73e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 153.47 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVIS--AYVMQDDLLFPMLTV 206
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS--GSILIDGEDVRKEPREARRqiGVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAAEFRLprtLSKSKKSARVQALIDQLGLRNAAKTVIGdeghrGVSGGERRRVSIGTDIIHDPILLFLDEPTSGL 286
Cdd:COG4555 92 RENIRYFAELYG---LFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 287 DSTSAYMVVKVLQRIAQSGSIVIMSIHQPsYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG4555 164 DVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
449-652 |
3.98e-42 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 152.04 E-value: 3.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 449 LSKRSFLNSRRMPELIGIRLGTVMVTGFILATMFWQLDNSpKGVQERLGFFAFAMSTTFYTTADAL-PVFLQERYIFMRE 527
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQ-QGGLNRPGLLFFSILFNAFSALSGIsPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 528 TAYNAYRRLSYLVSHALVALPALAFLSLAFAAATFWAVGLDGGISGFLFYFLIIFASFWAGNSFVTFLSGVVPHVMLGYT 607
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 356576859 608 IVVAILAYFLLFSGFFINRDRIPSYWIWFHYLSLVKYPYEAVLQN 652
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
120-742 |
6.54e-40 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 158.86 E-value: 6.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 120 VGESMFTRTK-TLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKgSLK--GTVALNGEALESRLLKVISAYVMQ 196
Cdd:PLN03140 168 LGINLAKKTKlTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDP-SLKvsGEITYNGYRLNEFVPRKTSAYISQ 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 197 DDLLFPMLTVEETLMFAAE-------FRLPRTLSKSKKSARV--QALIDQ----------------------LGLRNAAK 245
Cdd:PLN03140 247 NDVHVGVMTVKETLDFSARcqgvgtrYDLLSELARREKDAGIfpEAEVDLfmkatamegvksslitdytlkiLGLDICKD 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 246 TVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQ-SGSIVIMSIHQPSYRILGLLD 324
Cdd:PLN03140 327 TIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 325 RMIFLSRGQTVYSGSPSQLPLYFSEFGHPIPETDNRTEFaldlIRELEGSPGGTKSLVEFNKSWQ--SMTKHHQEKEEER 402
Cdd:PLN03140 407 DIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADF----LQEVTSKKDQEQYWADRNKPYRyiSVSEFAERFKSFH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 403 NGLSLKEAISASISRGKLVSGASNTNPNPSSMVPTFANQFWVEMATLSKRSFLNSRRMPELIGIRLgtVMVTGFILATMf 482
Cdd:PLN03140 483 VGMQLENELSVPFDKSQSHKAALVFSKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAA--IASTVFLRTEM- 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 483 wQLDNSPKGvQERLGFFAFAMSTTFYT-------TADALPVFLQERYIFMretaynaYRRLSYLVSHALVALPALAFLSL 555
Cdd:PLN03140 560 -HTRNEEDG-ALYIGALLFSMIINMFNgfaelalMIQRLPVFYKQRDLLF-------HPPWTFTLPTFLLGIPISIIESV 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 556 AFAAATFWAVGLDGGISGFLFYFLIIFASFWAGNSFVTFLSGVVPHVMLGYTIVVAILAYFLLFSGFFINRDRIPSYWIW 635
Cdd:PLN03140 631 VWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEW 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 636 FHYLSLVKYPYEAVLQNEFDDPvkcfvrgvqifdntplgsvpeplkvKLLETMSSTLGTKIttstclttGADILQQNGVT 715
Cdd:PLN03140 711 AYWVSPLSYGFNALAVNEMFAP-------------------------RWMNKMASDNSTRL--------GTAVLNIFDVF 757
|
650 660 670
....*....|....*....|....*....|.
gi 356576859 716 DLTKWncFWITVA--WGF--FFRFLFYLSLL 742
Cdd:PLN03140 758 TDKNW--YWIGVGalLGFtiLFNVLFTLALT 786
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
126-333 |
5.66e-39 |
|
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: 143.38 E-value: 5.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 126 TRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIakGSLKGTVALNGEALESRLLKVIS---AYVMQD-DLLF 201
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSLKELRrkvGLVFQNpDDQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAAEFRlprTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:cd03225 89 FGPTVEEEVAFGLENL---GLPEEEIEERVEEALELVGLEGLRDRSPFT-----LSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQ 333
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL-LLELADRVIVLEDGK 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
125-338 |
1.02e-38 |
|
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: 142.40 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 125 FTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAK-GSLKGTVALNG-EALE-SRLLKVISAYVMQDDLLF 201
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnVSVEGDIHYNGiPYKEfAEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAAEFRlprtlskskksarvqalidqlglrnaaktviGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:cd03233 96 PTLTVRETLDFALRCK-------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQ-SGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADvLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
126-343 |
2.32e-36 |
|
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: 136.48 E-value: 2.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 126 TRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKV--ISAYVMQDDLLFPM 203
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTS--GTAYINGYSIRTDRKAArqSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLMFAAEFRlprTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPT 283
Cdd:cd03263 90 LTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRART-----LSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 284 SGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGllDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALC--DRIAIMSDGKLRCIGSPQEL 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
129-343 |
1.18e-34 |
|
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: 131.69 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALESRLLKVIS---AYVMQ--DDLLFpM 203
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL-NGLLKPT-SGEVLVDGKDITKKNLRELRrkvGLVFQnpDDQLF-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLMFAaefrlPRTL--SKSKKSARVQALIDQLGLRNAAKTVIgdegHRgVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:COG1122 91 PTVEEDVAFG-----PENLglPREEIRERVEEALELVGLEHLADRPP----HE-LSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGTPREV 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
127-342 |
3.25e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.98 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEALESRLLKVisAYVMQD---DLL 200
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIL-----GLLPptsGTVRLFGKPPRRARRRI--GYVPQRaevDWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMlTVEETLM--FAAEFRLPRTLSKSKKsARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLF 278
Cdd:COG1121 90 FPI-TVRDVVLmgRYGRRGLFRRPSRADR-EAVDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQtVYSGSPSQ 342
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLG-AVREYFDRVLLLNRGL-VAHGPPEE 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
132-335 |
1.14e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.93 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALanriakGSL----KGTVALNGEALES---------RLLKVisAYVMQDD 198
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL------GGLdrptSGEVLIDGQDISSlserelarlRRRHI--GFVFQFF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 199 LLFPMLTVEETLMFAAEFrlpRTLSKSKKSARVQALIDQLGLrnaaktvigdeGHRG------VSGGERRRVSIGTDIIH 272
Cdd:COG1136 96 NLLPELTALENVALPLLL---AGVSRKERRERARELLERVGL-----------GDRLdhrpsqLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 273 DPILLFLDEPTSGLDSTSAYMVVKVLQRIA-QSGSIVIMSIHQPsyRILGLLDRMIFLSRGQTV 335
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDGRIV 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
132-284 |
1.91e-32 |
|
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: 122.76 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL---ESRLLKVISAYVMQDDLLFPMLTVEE 208
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE--GTILLDGQDLtddERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 209 TLMFAAEFrlpRTLSKSKKSARVQALIDQLGLRNAAKTVIGDEGHrGVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:pfam00005 79 NLRLGLLL---KGLSKREKDARAEEALEKLGLGDLADRPVGERPG-TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
128-333 |
4.36e-32 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 122.51 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVIS--AYVMQDDLLFPMLT 205
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS--GEIKVLGKDIKKEPEEVKRriGYLPEEPSLYENLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFaaefrlprtlskskksarvqalidqlglrnaaktvigdeghrgvSGGERRRVSIGTDIIHDPILLFLDEPTSG 285
Cdd:cd03230 90 VRENLKL--------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 356576859 286 LDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQ 333
Cdd:cd03230 126 LDPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGR 172
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
127-343 |
7.89e-32 |
|
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: 124.39 E-value: 7.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAkgSLKGTVALNGEALES-------RLLkvisAYVMQD-D 198
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK--PSSGEVLLDGRDLASlsrrelaRRI----AYVPQEpP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 199 LLFPmLTVEETLMFAaefRLP--RTLSKSKKS--ARVQALIDQLGLRNAAktvigdegHRGV---SGGERRRVSIGTDII 271
Cdd:COG1120 86 APFG-LTVRELVALG---RYPhlGLFGRPSAEdrEAVEEALERTGLEHLA--------DRPVdelSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 272 HDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQPSyriLGLL--DRMIFLSRGQTVYSGSPSQL 343
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLN---LAARyaDRLVLLKDGRIVAQGPPEEV 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
129-343 |
1.53e-30 |
|
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: 127.18 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL----ESRLLKVIsAYVMQDDLLFPMl 204
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS--GSILINGVDLsdldPASWRRQI-AWVPQNPYLFAG- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAA----EFRLPRTLskskKSARVQALIDQL--GLrnaaKTVIGDEGhRGVSGGERRRVSIGTDIIHDPILLF 278
Cdd:COG4988 426 TIRENLRLGRpdasDEELEAAL----EAAGLDEFVAALpdGL----DTPLGEGG-RGLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQsGSIVIMSIHQPSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLA--LLAQADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
128-333 |
4.86e-30 |
|
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: 118.36 E-value: 4.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALanriakGSL----KGTVALNGEAL----ESRLLKV----ISaYVM 195
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNIL------GGLdrptSGEVRVDGTDIsklsEKELAAFrrrhIG-FVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 196 QDDLLFPMLTVEETLMFAAEFRlprTLSKSKKSARVQALIDQLGLRNAAktvigdegHRGV---SGGERRRVSIGTDIIH 272
Cdd:cd03255 89 QSFNLLPDLTALENVELPLLLA---GVPKKERRERAEELLERVGLGDRL--------NHYPselSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 273 DPILLFLDEPTSGLDSTSAYMVVKVLQRIA-QSGSIVIMSIHQPsyRILGLLDRMIFLSRGQ 333
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDGK 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
128-343 |
1.56e-29 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 117.22 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKgsLKGTVALNGEAL----ESRLLKVI--SAYVMQDDLLF 201
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP--DSGEVLIDGEDIsglsEAELYRLRrrMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAaeFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:cd03261 90 DSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAE-----LSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLD-TAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
128-343 |
3.04e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 118.29 E-value: 3.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKGSLK---GTVALNGEALESRLLKVIsAYvmqddL----- 199
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTI-----RIILGILApdsGEVLWDGEPLDPEDRRRI-GY-----Lpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 LFPMLTVEETLMFAAefRLpRTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:COG4152 82 LYPKMKVGEQLVYLA--RL-KGLSKAEAKRRADEWLERLGLGDRANKKVEE-----LSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSY--RilgLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELveE---LCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
129-343 |
7.26e-29 |
|
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: 115.74 E-value: 7.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALESRLLKVI------SAYVMQDDLLFP 202
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCL-NGLVEPT-SGSVLIDGTDINKLKGKALrqlrrqIGMIFQQFNLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAAEFRLP--RTLSKS-KKSARVQAL--IDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILL 277
Cdd:cd03256 92 RLSVLENVLSGRLGRRStwRSLFGLfPKEEKQRALaaLERVGLLDKAYQRADQ-----LSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 278 FLDEPTSGLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDL-AREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
127-330 |
8.81e-29 |
|
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: 114.49 E-value: 8.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVisAYVMQDDLLFPMLTV 206
Cdd:cd03293 15 GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS--GEVLVDGEPVTGPGPDR--GYVFQQDALLPWLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAAEFRLprtLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGL 286
Cdd:cd03293 91 LDNVALGLELQG---VPKAEARERAEELLELVGLSGFENAYPHQ-----LSGGMRQRVALARALAVDPDVLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 356576859 287 DS-TSAYMVVKVLQRIAQSGSIVIMSIHQpsyrilglLDRMIFLS 330
Cdd:cd03293 163 DAlTREQLQEELLDIWRETGKTVLLVTHD--------IDEAVFLA 199
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
132-343 |
4.93e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 112.53 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEALESRLLKVIS----AYVMQDDLLFPML 204
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIM-----GLLPprsGSIRFDGRDITGLPPHERAragiGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAAEFRLPRTLSKSKksARVQALIDQLG--LRNAAKTvigdeghrgVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:cd03224 91 TVEENLLLGAYARRRAKRKARL--ERVYELFPRLKerRKQLAGT---------LSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 283 TSGLDSTSAYMVVKVLQRIAQSGSIVIMsIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTILL-VEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
127-338 |
4.95e-28 |
|
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: 112.37 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVIsAYVMQDDLLFPMLTV 206
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS--GEVLFDGKPLDIAARNRI-GYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAAEFRlprTLSKSKKSARVQALIDQLGLRNAAKTVIgdeghRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGL 286
Cdd:cd03269 88 IDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 356576859 287 DSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQME-LVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
129-335 |
5.53e-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: 112.23 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAN--RIAKGS-LKGTVALNGEALESRllKVisAYVMQDDLLFPMLT 205
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDSGEiLIDGRDVTGVPPERR--NI--GMVFQDYALFPHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFAAEfrlPRTLSKSKKSARVQALIDQLGLRNAAKTVIgdeghRGVSGGERRRVSIGTDIIHDPILLFLDEPTSG 285
Cdd:cd03259 89 VAENIAFGLK---LRGVPKAEIRARVRELLELVGLEGLLNRYP-----HELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 356576859 286 LDS-TSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTV 335
Cdd:cd03259 161 LDAkLREELREELKELQRELGITTIYVTHDQE-EALALADRIAVMNEGRIV 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
132-313 |
6.15e-28 |
|
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: 112.12 E-value: 6.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALeSRLLKVISAY-------VMQDDLLFPML 204
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTS--GTIRVNGQDV-SDLRGRAIPYlrrkigvVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAAE--FRLPRTLSKskksaRVQALIDQLGLRNAAKTVigdegHRGVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:cd03292 94 NVYENVAFALEvtGVPPREIRK-----RVPAALELVGLSHKHRAL-----PAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|.
gi 356576859 283 TSGLDSTSAYMVVKVLQRIAQSGSIVIMSIH 313
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
129-343 |
7.78e-28 |
|
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: 112.38 E-value: 7.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEAL----ESRLLKVIS--AYVMQDDL 199
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII-----GLLRpdsGEILVDGQDItglsEKELYELRRriGMLFQGGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 LFPMLTVEETLMFAAEFRlpRTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:COG1127 93 LFDSLTVFENVAFPLREH--TDLSEAEIRELVLEKLELVGLPGAADKMPSE-----LSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQ-PSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDS--AFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
129-315 |
7.83e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.42 E-value: 7.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEALESRLLKVIS--AYVMQDDLLFPM 203
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA-----GLLPpsaGEVLWNGEPIRDAREDYRRrlAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLMFAAEFRLPRTlskskKSARVQALIDQLGLrnaaktvigdEGHRGV-----SGGERRRVSIGTDIIHDPILLF 278
Cdd:COG4133 90 LTVRENLRFWAALYGLRA-----DREAIDEALEAVGL----------AGLADLpvrqlSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQP 315
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
132-342 |
9.03e-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: 112.15 E-value: 9.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVISAYVM----QDDLLFPMLTVE 207
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS--GSVLFDGEDITGLPPHEIARLGIgrtfQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEFRLPRTLS-----KSKKSARVQA--LIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:cd03219 94 ENVMVAAQARTGSGLLlararREEREARERAeeLLERVGLADLADRPAGE-----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSG-SIVI----MSIhqpsyrILGLLDRMIFLSRGQTVYSGSPSQ 342
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGiTVLLvehdMDV------VMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
127-343 |
1.16e-27 |
|
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: 117.70 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRI-AKGSLKGTVALNGEALESRLLKVIS---AYVMQD-DLLF 201
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLpHGGRISGEVLLDGRDLLELSEALRGrriGMVFQDpMTQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAAEFRLprtLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:COG1123 97 NPVTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRVAIAMALALDPDLLIADE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356576859 282 PTSGLDSTSAYMVVKVLQRI-AQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG1123 169 PTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGV-VAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
126-353 |
1.18e-27 |
|
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: 117.70 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 126 TRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKGSLK---GTVALNGEALESRLLKVISA------YVMQ 196
Cdd:COG1123 275 KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLA-----RLLLGLLRptsGSILFDGKDLTKLSRRSLRElrrrvqMVFQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 197 D--DLLFPMLTVEETLMFAAefRLPRTLSKSKKSARVQALIDQLGLrnaaktvigDEGHRGV-----SGGERRRVSIGTD 269
Cdd:COG1123 350 DpySSLNPRMTVGDIIAEPL--RLHGLLSRAERRERVAELLERVGL---------PPDLADRyphelSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 270 IIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQpsyriLGLL----DRMIFLSRGQTVYSGSPSQLp 344
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHD-----LAVVryiaDRVAVMYDGRIVEDGPTEEV- 492
|
....*....
gi 356576859 345 lyFSEFGHP 353
Cdd:COG1123 493 --FANPQHP 499
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
123-315 |
3.56e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 109.88 E-value: 3.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 123 SMFTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKG-SLKGTVALNGEAL-----ESRLLkvisAYVMQ 196
Cdd:COG4136 8 TITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfSASGEVLLNGRRLtalpaEQRRI----GILFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 197 DDLLFPMLTVEETLMFAaefrLPRTLSKSKKSARVQALIDQLGLrnaaktviGDEGHRGV---SGGERRRVSIGTDIIHD 273
Cdd:COG4136 84 DDLLFPHLSVGENLAFA----LPPTIGRAQRRARVEQALEEAGL--------AGFADRDPatlSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 356576859 274 PILLFLDEPTSGLD-STSAYMVVKVLQRIAQSGSIVIMSIHQP 315
Cdd:COG4136 152 PRALLLDEPFSKLDaALRAQFREFVFEQIRQRGIPALLVTHDE 194
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
128-343 |
3.90e-27 |
|
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: 116.79 E-value: 3.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEAL----ESRLLKVIsAYVMQDDLL 200
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLL-----RFLDpqsGSITLGGVDLrdldEDDLRRRI-AVVPQRPHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMlTVEETLMFAA----EFRLPRTLSKskksARVQALIDQL--GLRnaakTVIGdEGHRGVSGGERRRVSIGTDIIHDP 274
Cdd:COG4987 421 FDT-TLRENLRLARpdatDEELWAALER----VGLGDWLAALpdGLD----TWLG-EGGRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 275 ILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSiHQPSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALAGRTVLLIT-HRLA--GLERMDRILVLEDGRIVEQGTHEEL 556
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
127-338 |
6.71e-27 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 108.82 E-value: 6.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGeIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGE-ALESR--LLKVISaYVMQDDLLFPM 203
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSS--GTIRIDGQdVLKQPqkLRRRIG-YLPQEFGVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLMFAAefRLPRtLSKSKKSARVQALIDQLGLRNAAKTVIGdeghrGVSGGERRRVSIGTDIIHDPILLFLDEPT 283
Cdd:cd03264 87 FTVREFLDYIA--WLKG-IPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 284 SGLDSTSAYMVVKVLQRIAqSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03264 159 AGLDPEERIRFRNLLSELG-EDRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
129-338 |
1.97e-26 |
|
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: 106.75 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnRIAKGSlKGTVALNGEALESRLLKVIS---AYVMQddllfpmlt 205
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-GLLKPS-SGEILLDGKDLASLSPKELArkiAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 veetlmfaaefrlprtlskskksarvqaLIDQLGLRNAAktvigdegHRGV---SGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:cd03214 81 ----------------------------ALELLGLAHLA--------DRPFnelSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 283 TSGLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQPSyriLGLL--DRMIFLSRGQTVYSG 338
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErGKTVVMVLHDLN---LAARyaDRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
128-333 |
2.08e-26 |
|
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: 105.79 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVISAYVmqddllfpmltve 207
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTS--GEILIDGKDIAKLPLEELRRRI------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 etlmfaaefrlprtlskskksarvqALIDQLglrnaaktvigdeghrgvSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:cd00267 76 -------------------------GYVPQL------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 356576859 288 STSAYMVVKVLQRIAQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQ 333
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
132-343 |
3.06e-26 |
|
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: 109.79 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEALESRLLKVISAYVMQDDLLFPMLTVEETLM 211
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 212 FAAEFRlprTLSKSKKSARVQALIDQLGLRNAAKTVIGdeghrGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSA 291
Cdd:TIGR01188 89 MMGRLY---GLPKDEAEERAEELLELFELGEAADRPVG-----TYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 356576859 292 YMVVKVLQRIAQSGSIVIMSIHQpSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
129-335 |
4.81e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.68 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEALeSRL-LKVISAY------VMQDD 198
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLY-----GEERptsGQVLVNGQDL-SRLkRREIPYLrrrigvVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 199 LLFPMLTVEETLMFAAEFRlprTLSKSKKSARVQALIDQLGLRNAAKTVIgDEghrgVSGGERRRVSIGTDIIHDPILLF 278
Cdd:COG2884 89 RLLPDRTVYENVALPLRVT---GKSRKEIRRRVREVLDLVGLSDKAKALP-HE----LSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQpsyriLGLLDRM----IFLSRGQTV 335
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHD-----LELVDRMpkrvLELEDGRLV 216
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
129-333 |
1.01e-25 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 104.58 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALA--NRIAKGSLK-GTVALNGEALESRLLKVISAYVMQDDLLFPMLT 205
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAglEEPDSGSILiDGEDLTDLEDELPPLRRRIGMVFQDFALFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFaaefrlprtlskskksarvqalidqlglrnaaktvigdeghrGVSGGERRRVSIGTDIIHDPILLFLDEPTSG 285
Cdd:cd03229 93 VLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 356576859 286 LDSTSAYMVVKVLQRI-AQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQ 333
Cdd:cd03229 131 LDPITRREVRALLKSLqAQLGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
129-338 |
1.58e-25 |
|
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: 104.92 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEALESRLLKVisAYVMQD---DLLFP 202
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL-----GLLKptsGSIRVFGKPLEKERKRI--GYVPQRrsiDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 mLTVEETLM--FAAEFRLPRTLSKSKKsARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:cd03235 85 -ISVRDVVLmgLYGHKGLFRRLSKADK-AKVDEALERVGLSELADRQIGE-----LSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGqTVYSG 338
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLG-LVLEYFDRVLLLNRT-VVASG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
129-333 |
1.63e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 104.90 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESrlLKVIS-----AYVMQDDLLFPM 203
Cdd:COG4619 13 KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS--GEIYLDGKPLSA--MPPPEwrrqvAYVPQEPALWGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 lTVEETLMFAAEFRlprtlSKSKKSARVQALIDQLGLRNAA--KTVigdeghRGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:COG4619 89 -TVRDNLPFPFQLR-----ERKFDRERALELLERLGLPPDIldKPV------ERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSI-HQPSYrILGLLDRMIFLSRGQ 333
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVsHDPEQ-IERVADRVLTLEAGR 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
129-342 |
2.61e-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: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEALESRLLKVISAY--VM-QD-DLLF 201
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT-----GELTpssGEVRLNGRPLAAWSPWELARRraVLpQHsSLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PmLTVEETLMFAaefRLPRTLSKSKKSARVQALIDQLGLRNAAktvigdegHR---GVSGGERRRVS-------IGTDII 271
Cdd:COG4559 89 P-FTVEEVVALG---RAPHGSSAAQDRQIVREALALVGLAHLA--------GRsyqTLSGGEQQRVQlarvlaqLWEPVD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 272 HDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQpsyriLGLL----DRMIFLSRGQTVYSGSPSQ 342
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHD-----LNLAaqyaDRILLLHQGRLVAQGTPEE 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
127-343 |
3.53e-25 |
|
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: 111.46 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnRIAKGSlKGTVALNGEALESRLLKVIS---AYVMQDDLLFPM 203
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL-GLYEPT-SGRILIDGIDLRQIDPASLRrqiGVVLQDVFLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 lTVEETLMFAAEFRLPRTLSKSKKSARVQALIDQL--GLrnaaKTVIGDEGhRGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:COG2274 564 -TIRENITLGDPDATDEEIIEAARLAGLHDFIEALpmGY----DTVVGEGG-SNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQsGSIVIMSIHQPSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS--TIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
128-333 |
7.08e-25 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 102.99 E-value: 7.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALESRLLKVIS-----AYVMQDDLLFP 202
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLEEPD-SGTIIIDGLKLTDDKKNINElrqkvGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAaefrlPRTLSK-SKKSARVQA--LIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:cd03262 90 HLTVLENITLA-----PIKVKGmSKAEAEERAleLLEKVGLADKADAYPAQ-----LSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQ 333
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGF-AREVADRVIFMDDGR 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
130-343 |
1.19e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.25 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTL---IDALaNRIAKGSLK-GTVALNGEALESRLLKVISAYVMQDDLLFPMLT 205
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKL-EEITSGDLIvDGLKVNDPKVDERLIRQEAGMVFQQFYLFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFAaefrlP-RTLSKSKKSARVQA--LIDQLGLRNAAktvigdeGH--RGVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:PRK09493 94 ALENVMFG-----PlRVRGASKEEAEKQAreLLAKVGLAERA-------HHypSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSY-RILGllDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFaEKVA--SRLIFIDKGRIAEDGDPQVL 223
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
129-343 |
2.83e-24 |
|
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: 101.98 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIdALANRIaKGSLKGTVALNGEALES---RLLKVISAyVMQDDLLFPMLT 205
Cdd:TIGR03864 14 RRALDDVSFTVRPGRFVALLGPNGAGKSTLF-SLLTRL-YVAQSGQISVAGHDLRRaprAALARLGV-VFQQPTLDLDLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMF-AAEFRLPRTLSKskksARVQALIDQLGLRNAAktvigDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:TIGR03864 91 VRQNLRYhAALHGLSRAEAR----ARIAELLARLGLAERA-----DDKVRELNGGHRRRVEIARALLHRPALLLLDEPTV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSI-VIMSIH-----QPSyrilgllDRMIFLSRGQTVYSGSPSQL 343
Cdd:TIGR03864 162 GLDPASRAAITAHVRALARDQGLsVLWATHlvdeiEAS-------DRLVVLHRGRVLADGAAAEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
134-343 |
3.83e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 104.80 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 134 DISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEAL-----------ESRLLkvisAYVMQDDL 199
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIA-----GLERpdsGRIRLGGEVLqdsargiflppHRRRI----GYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 LFPMLTVEETLMFAAEfRLPRTLSKskksARVQALIDQLGLrnaaktvigdeGH---RGV---SGGERRRVSIGTDIIHD 273
Cdd:COG4148 88 LFPHLSVRGNLLYGRK-RAPRAERR----ISFDEVVELLGI-----------GHlldRRPatlSGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 274 PILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSI-VIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG4148 152 PRLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSLD-EVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
127-338 |
4.39e-24 |
|
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: 101.43 E-value: 4.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALES---RLLKVIS---AYVMQDDL- 199
Cdd:cd03257 16 GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTS--GSIIFDGKDLLKlsrRLRKIRRkeiQMVFQDPMs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 -LFPMLTVEETLMFAAEFRLPRTlSKSKKSARVQALIDQLGLrnaAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLF 278
Cdd:cd03257 94 sLNPRMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGL---PEEVLNRYPHE-LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRI-AQSGSIVIMSIHQpsyriLGLL----DRMIFLSRGQTVYSG 338
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHD-----LGVVakiaDRVAVMYAGKIVEEG 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
141-338 |
9.33e-24 |
|
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: 100.06 E-value: 9.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 141 DGEIMAVLGASGSGKSTLIdalanRIAKGSLK---GTVALNGEALESRLLKVIS-------AYVMQDDLLFPMLTVEETL 210
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLL-----RCIAGLEKpdgGTIVLNGTVLFDSRKKINLppqqrkiGLVFQQYALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 211 MFAAefrlpRTLSKSKKSARVQALIDQLGLrnaakTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTS 290
Cdd:cd03297 97 AFGL-----KRKRNREDRISVDELLDLLGL-----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 356576859 291 AYMVVKVLQRIAQSGSI-VIMSIHQPSyRILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03297 167 RLQLLPELKQIKKNLNIpVIFVTHDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
127-335 |
1.15e-23 |
|
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: 100.65 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnRIAKGSlKGTVALNGEALESRLLKVISA---YVMQDDL--LF 201
Cdd:COG1124 16 RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALA-GLERPW-SGEVTFDGRPVTRRRRKAFRRrvqMVFQDPYasLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLmfaAEfrlP-RTLSKSKKSARVQALIDQLGLrnaaktvigDEGHRG-----VSGGERRRVSIGTDIIHDPI 275
Cdd:COG1124 94 PRHTVDRIL---AE---PlRIHGLPDREERIAELLEQVGL---------PPSFLDryphqLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 276 LLFLDEPTSGLD-STSAyMVVKVLQRI-AQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQTV 335
Cdd:COG1124 159 LLLLDEPTSALDvSVQA-EILNLLKDLrEERGLTYLFVSHDLAV-VAHLCDRVAVMQNGRIV 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
125-335 |
2.28e-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: 98.48 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 125 FTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAkgSLKGTVALNGEALESRLLKVISAYVMQD--DLLFp 202
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK--ESSGSILLNGKPIKAKERRKSIGYVMQDvdYQLF- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAAEfrlprtlSKSKKSARVQALIDQLGLrNAAKtvigdEGH-RGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:cd03226 86 TDSVREELLLGLK-------ELDAGNEQAETVLKDLDL-YALK-----ERHpLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQTV 335
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGAIV 205
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
128-343 |
4.82e-23 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 100.23 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKV--ISAYVMQDDLLFPMLT 205
Cdd:TIGR03522 14 TQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDS--GSVQVCGEDVLQNPKEVqrNIGYLPEHNPLYLDMY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMF-AAEFRLPRTLSKSkksaRVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:TIGR03522 92 VREYLQFiAGIYGMKGQLLKQ----RVEEMIELVGLRPEQHKKIGQ-----LSKGYRQRVGLAQALIHDPKVLILDEPTT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSIvIMSIH--QpsyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:TIGR03522 163 GLDPNQLVEIRNVIKNIGKDKTI-ILSTHimQ---EVEAICDRVIIINKGKIVADKKLDEL 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
129-343 |
6.99e-23 |
|
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: 97.64 E-value: 6.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSLK----GTVALNGEALESRLLKVIS-----AYVMQDDL 199
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIPGapdeGEVLLDGKDIYDLDVDVLElrrrvGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 LFPMlTVEETLMFAAefRLPRTLSKSKKSARVQALIDQLGLRNAAKtvigDEGH-RGVSGGERRRVSIGTDIIHDPILLF 278
Cdd:cd03260 92 PFPG-SIYDNVAYGL--RLHGIKLKEELDERVEEALRKAALWDEVK----DRLHaLGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMS--IHQpSYRIlglLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQ-AARV---ADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
132-343 |
9.00e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 97.44 E-value: 9.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEALESRLLKVISAYVMQDDLLFPMLTVEETL- 210
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSVDDELTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 211 MFAAEFRLPRtlskSKKSARVQALIDQLGLRNAAktvigDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTS 290
Cdd:cd03265 96 IHARLYGVPG----AERRERIDELLDFVGLLEAA-----DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 291 AYMVVKVLQRI-AQSGSIVIMSIHqpsY--RILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03265 167 RAHVWEYIEKLkEEFGMTILLTTH---YmeEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
132-356 |
1.65e-22 |
|
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: 97.02 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL-----ESRLLkvisAYVMQDDLLFPMLTV 206
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS--GKILLNGKDItnlppEKRDI----SYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAaeFRLpRTLSKSKKSARVQALIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGL 286
Cdd:cd03299 89 YKNIAYG--LKK-RKVDKKEIERKVLEIAEMLGIDH-----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 287 DSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSqlplyfSEFGHPIPE 356
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE------EVFKKPKNE 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
142-338 |
2.15e-22 |
|
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: 96.02 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 142 GEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGE---ALESRLLKVisAYVMQDDLLFPMLTVEETLMFAaefRL 218
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQS--GRVLINGVdvtAAPPADRPV--SMLFQENNLFAHLTVEQNVGLG---LS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 219 PRTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHD-PILLfLDEPTSGLD-STSAYMVVK 296
Cdd:cd03298 97 PGLKLTAEDRQAIEVALARVGLAGLEKRLPGE-----LSGGERQRVALARVLVRDkPVLL-LDEPFAALDpALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 356576859 297 VLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPE-DAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
132-338 |
2.74e-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: 95.90 E-value: 2.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVA---LNGEALESRL-LKVISAyvmqDDLLFPMLTVE 207
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdVVKEPAEARRrLGFVSD----STGLYDRLTAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEFRlprTLSKSKKSARVQALIDQLGLRNAAKTVIGdeghrGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:cd03266 97 ENLEYFAGLY---GLKGDELTARLEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 356576859 288 STSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03266 169 VMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
134-343 |
4.92e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 98.26 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 134 DISGEARDGEIMAVLGASGSGKSTLIDALAN--RIAKGSLkgtvALNGEALESRLLKVIS-------AYVMQDDLLFPML 204
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGltRPDEGEI----VLNGRTLFDSRKGIFLppekrriGYVFQEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAAEFRLPrtlskSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:TIGR02142 91 SVRGNLRYGMKRARP-----SERRISFERVIELLGIGHLLGRLPGR-----LSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSIVIMSI-HQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVsHSLQ-EVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
127-333 |
5.30e-22 |
|
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: 93.60 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnRIAKGSlKGTVALNGEALE----SRLLKVIsAYVMQDDLLFP 202
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLL-RLYDPT-SGEILIDGVDLRdldlESLRKNI-AYVPQDPFLFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MlTVEETLMfaaefrlprtlskskksarvqalidqlglrnaaktvigdeghrgvSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:cd03228 90 G-TIRENIL---------------------------------------------SGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 356576859 283 TSGLDSTSAYMVVKVLQRIAQsGSIVIMSIHQPSYriLGLLDRMIFLSRGQ 333
Cdd:cd03228 124 TSALDPETEALILEALRALAK-GKTVIVIAHRLST--IRDADRIIVLDDGR 171
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
128-338 |
5.53e-22 |
|
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: 94.59 E-value: 5.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL--ESRLLKVISAYVmQDDLLFPMLT 205
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS--GEITFDGKSYqkNIEALRRIGALI-EAPGFYPNLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETL-MFAAEFRLPRtlskskksARVQALIDQLGLRNAAKTVIGdeghrGVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:cd03268 89 ARENLrLLARLLGIRK--------KRIDEVLDVVGLKDSAKKKVK-----GFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
129-322 |
1.14e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.79 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKgsLKGTVALNGEALESRLLKVISAYVMQDDLLFPMLTVEE 208
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP--AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 TLMFAAEFRLPRTLSkskksarVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDII-HDPILLfLDEPTSGLD 287
Cdd:PRK13539 93 NLEFWAAFLGGEELD-------IAAALEAVGLAPLAHLPFGY-----LSAGQKRRVALARLLVsNRPIWI-LDEPTAALD 159
|
170 180 190
....*....|....*....|....*....|....*
gi 356576859 288 STSAYMVVKVLQRIAQSGSIVIMSIHQPsyriLGL 322
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAATHIP----LGL 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
132-329 |
1.32e-21 |
|
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: 99.28 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL----ESRLLKVIsAYVMQDDLLFPMlTVE 207
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE--GSIAVNGVPLadadADSWRDQI-AWVPQHPFLFAG-TIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAaefRLPRTLSKSKKSARvQALIDQL--GLRNAAKTVIGDEGhRGVSGGERRRVSIGTDIIHDPILLFLDEPTSG 285
Cdd:TIGR02857 414 ENIRLA---RPDASDAEIREALE-RAGLDEFvaALPQGLDTPIGEGG-AGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 356576859 286 LDSTSAYMVVKVLQRIAQsGSIVIMSIHQPSyrILGLLDRMIFL 329
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQ-GRTVLLVTHRLA--LAALADRIVVL 529
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
129-342 |
1.94e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALES---RLLKVISAyVM--QDDLLFPm 203
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDS--GEVRLNGRPLADwspAELARRRA-VLpqHSSLSFP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLMFAaefRLPRTLSKSKKSARVQALIDQLGLrnaakTVIGDEGHRGVSGGERRRVSIG------TDIIHDPILL 277
Cdd:PRK13548 91 FTVEEVVAMG---RAPHGLSRAEDDALVAAALAQVDL-----AHLAGRDYPQLSGGEQQRVQLArvlaqlWEPDGPPRWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 278 FLDEPTSGLDSTSAYMVVKVLQRIAQS---GSIVIMsiHQpsyriLGLL----DRMIFLSRGQTVYSGSPSQ 342
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHErglAVIVVL--HD-----LNLAaryaDRIVLLHQGRLVADGTPAE 227
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
132-313 |
3.11e-21 |
|
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: 92.10 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEALE-SR--LLKVIS--AYVMQ--DDLLF 201
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLN-----GLLRpqsGAVLIDGEPLDySRkgLLERRQrvGLVFQdpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMlTVEETLMFAaefrlPRTL--SKSKKSARVQ---ALIDQLGLRNAAKTVIgdeghrgvSGGERRRVSIGTDIIHDPIL 276
Cdd:TIGR01166 83 AA-DVDQDVAFG-----PLNLglSEAEVERRVRealTAVGASGLRERPTHCL--------SGGEKKRVAIAGAVAMRPDV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 356576859 277 LFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIH 313
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
127-343 |
3.74e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 92.99 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALES-----RLLKVISaYVMQDDLLF 201
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS--GKILLDGQDITKlpmhkRARLGIG-YLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAAEFRlprTLSKSKKSARVQALIDQLGLRNAAKTVIGdeghrGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:cd03218 88 RKLTVEENILAVLEIR---GLSKKEREEKLEELLEEFHITHLRKSKAS-----SLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVR-ETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
130-368 |
5.55e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.21 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEALESRL----LKVisAYVMQDDLLFP 202
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIA-----GLETpdsGRIVLNGRDLFTNLppreRRV--GFVFQHYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAAEFRLPrtlSKSKKSARVQALIDQLGLrnaaktviGDEGHR---GVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:COG1118 89 HMTVAENIAFGLRVRPP---SKAEIRARVEELLELVQL--------EGLADRypsQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRI--AQSGSIVIMSiHQP--SYRilgLLDRMIFLSRGQTVYSGSPSQLplyfseFGHPip 355
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRLhdELGGTTVFVT-HDQeeALE---LADRVVVMNQGRIEQVGTPDEV------YDRP-- 225
|
250
....*....|...
gi 356576859 356 etdnRTEFALDLI 368
Cdd:COG1118 226 ----ATPFVARFL 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
132-287 |
5.71e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 95.16 E-value: 5.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALA--NRIAkgslKGTVALNGealesrllKVISA---------YVMQDDLL 200
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgfETPD----SGRILLDG--------RDVTGlppekrnvgMVFQDYAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLTVEETLMFAAEFrlpRTLSKSKKSARVQALIDQLGLrnaaktviGDEGHRGV---SGGERRRVSIGTDIIHDPILL 277
Cdd:COG3842 89 FPHLTVAENVAFGLRM---RGVPKAEIRARVAELLELVGL--------EGLADRYPhqlSGGQQQRVALARALAPEPRVL 157
|
170
....*....|
gi 356576859 278 FLDEPTSGLD 287
Cdd:COG3842 158 LLDEPLSALD 167
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
131-343 |
6.34e-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: 92.55 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 131 LLNDISGEARDGEIMAVLGASGSGKSTLIDaLANRIAKGSlKGTVALNGEAL---ESRLLKVISAYVMQDDLLFPMlTVE 207
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTK-LIQRFYVPE-NGRVLVDGHDLalaDPAWLRRQVGVVLQENVLFNR-SIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEFRLPRTLSKSKKSARVQALIDQLglRNAAKTVIGDEGhRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:cd03252 94 DNIALADPGMSMERVIEAAKLAGAHDFISEL--PEGYDTIVGEQG-AGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 288 STSAYMVVKVLQRIAqSGSIVIMSIHQPSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03252 171 YESEHAIMRNMHDIC-AGRTVIIIAHRLS--TVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
132-342 |
7.37e-21 |
|
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: 92.79 E-value: 7.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEALeSRLlkviSAYVM---------QDDL 199
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLIT-----GFYRptsGRILFDGRDI-TGL----PPHRIarlgiartfQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 LFPMLTVEETLMFAAEFRLPRTLSKSKKS------------ARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIG 267
Cdd:COG0411 90 LFPELTVLENVLVAAHARLGRGLLAALLRlprarreerearERAEELLERVGLADRADEPAGN-----LSYGQQRRLEIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 268 TDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSG--SIVI----MSIhqpsyrILGLLDRMIFLSRGQTVYSGSPS 341
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLiehdMDL------VMGLADRIVVLDFGRVIAEGTPA 238
|
.
gi 356576859 342 Q 342
Cdd:COG0411 239 E 239
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
130-335 |
1.88e-20 |
|
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: 90.96 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL----ESRLLKVISA---YVMQDDLLFP 202
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTS--GTVRLAGQDLfaldEDARARLRARhvgFVFQSFQLLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAAEFRlprtlSKSKKSARVQALIDQLGLrnaaktvigdeGHR------GVSGGERRRVSIGTDIIHDPIL 276
Cdd:COG4181 104 TLTALENVMLPLELA-----GRRDARARARALLERVGL-----------GHRldhypaQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 277 LFLDEPTSGLDSTSAYMVVKVLQRI-AQSGSIVIMSIHQPsyRILGLLDRMIFLSRGQTV 335
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDP--ALAARCDRVLRLRAGRLV 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
129-354 |
2.01e-20 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 91.30 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlKGTVALNGEAL--ES-----RLLKVISAyVMQDDLLf 201
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTY-GNDVRLFGERRggEDvwelrKRIGLVSP-ALQLRFP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLM--FAAEFRLPRTLSKSKKsARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:COG1119 93 RDETVLDVVLsgFFDSIGLYREPTDEQR-ERARELLELLGLAHLADRPFGT-----LSQGEQRRVLIARALVKDPELLIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSI-VIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQL--PLYFSE-FGHPI 354
Cdd:COG1119 167 DEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTHHVEE-IPPGITHVLLLKDGRVVAAGPKEEVltSENLSEaFGLPV 244
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
132-338 |
2.06e-20 |
|
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: 90.34 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLidalaNRIAKGSLK---GTVALNGeaLESRLL------KVISaYVMQDDLLFp 202
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTL-----LKLLAGLYKptsGSVLLDG--TDIRQLdpadlrRNIG-YVPQDVTLF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAAEFRLPRTLSKSKKSARVQALIDQLGlrNAAKTVIGdEGHRGVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:cd03245 91 YGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHP--NGLDLQIG-ERGRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 283 TSGLDSTSAYMVVKVLQRIAqSGSIVIMSIHQPSyrILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
142-343 |
3.82e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.81 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 142 GEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL-----ESRLLKVISayvmQDDLLFPMLTVEETLMFAaeF 216
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPPDS--GRILWNGQDLtalppAERPVSMLF----QENNLFPHLTVAQNIGLG--L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 217 RLPRTLSKSKKsARVQALIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHD-PILLfLDEPTSGLD-STSAYMV 294
Cdd:COG3840 97 RPGLKLTAEQR-AQVEQALERVGLAG-----LLDRLPGQLSGGQRQRVALARCLVRKrPILL-LDEPFSALDpALRQEML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 356576859 295 VKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG3840 170 DLVDELCRERGLTVLMVTHDPE-DAARIADRVLLVADGRIAADGPTAAL 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
132-315 |
3.86e-20 |
|
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: 94.73 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAkgSLKGTVALNGEAL----ESRLLKVISaYVMQDDLLFPMlTVE 207
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD--PLQGEVTLDGVPVssldQDEVRRRVS-VCAQDAHLFDT-TVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEFRLPRTLSKSKKSARVQALIDqlGLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:TIGR02868 427 ENLRLARPDATDEELWAALERVGLADWLR--ALPDGLDTVLGEGGAR-LSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*...
gi 356576859 288 STSAYMVVKVLqRIAQSGSIVIMSIHQP 315
Cdd:TIGR02868 504 AETADELLEDL-LAALSGRTVVLITHHL 530
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
131-353 |
4.58e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.41 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 131 LLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEAL----------------ESRLLKVISAYV 194
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPS-EGSIVVNGQTInlvrdkdgqlkvadknQLRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 195 MQDDLLFPMLTVEETLMFAAefrlPRTLSKSKKSARVQAL--IDQLGLRNAAKtvigDEGHRGVSGGERRRVSIGTDIIH 272
Cdd:PRK10619 98 FQHFNLWSHMTVLENVMEAP----IQVLGLSKQEARERAVkyLAKVGIDERAQ----GKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 273 DPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQLplyfseFGH 352
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGF-ARHVSSHVIFLHQGKIEEEGAPEQL------FGN 242
|
.
gi 356576859 353 P 353
Cdd:PRK10619 243 P 243
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
132-345 |
4.86e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 89.83 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANrIAKGSlKGTVALNGEALES----RLLkvisayVMQDDLLFPMLTVE 207
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG-LAQPT-SGGVILEGKQITEpgpdRMV------VFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEfRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:TIGR01184 73 ENIALAVD-RVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ-----LSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 288 STSAYMVVKVLQRIAQ-SGSIVIMSIHQPSYRILgLLDRMIFLSRGQTVYSGSPSQLPL 345
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEeHRVTVLMVTHDVDEALL-LSDRVVMLTNGPAANIGQILEVPF 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
129-343 |
6.75e-20 |
|
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: 89.60 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnRIAKgSLKGTVALNGE-----ALESrLLKVIsAYVMQDDLLFpm 203
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLF-RFYD-VSSGSILIDGQdirevTLDS-LRRAI-GVVPQDTVLF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 ltvEETLMFAAEF-RLPRT---LSKSKKSARVQALIdqLGLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:cd03253 88 ---NDTIGYNIRYgRPDATdeeVIEAAKAAQIHDKI--MRFPDGYDTIVGERGLK-LSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQsGSIVIMSIHQPSyRILGlLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLS-TIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
132-289 |
9.74e-20 |
|
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: 90.88 E-value: 9.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDAL-----ANRIAKGS--LKGT--VALNGEALESRLLKVIsAYVMQDDL--L 200
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAIlgllpPPGITSGEilFDGEdlLKLSEKELRKIRGREI-QMIFQDPMtsL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLTVEETLMFAaeFRLPRTLSKSKKSARVQALIDQLGLRNAAKtVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:COG0444 100 NPVMTVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLPDPER-RLDRYPHE-LSGGMRQRVMIARALALEPKLLIAD 175
|
....*....
gi 356576859 281 EPTSGLDST 289
Cdd:COG0444 176 EPTTALDVT 184
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
132-313 |
1.02e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.54 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALES----RllkvisAYVMQDDLLFPMLTVE 207
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSS--GEITLDGVPVTGpgadR------GVVFQKDALLPWLNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAaeFRLpRTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:COG4525 95 DNVAFG--LRL-RGVPKAERRARAEELLALVGLADFARRRIWQ-----LSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180
....*....|....*....|....*..
gi 356576859 288 S-TSAYMVVKVLQRIAQSGSIVIMSIH 313
Cdd:COG4525 167 AlTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
130-315 |
1.18e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.29 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAlesRLlkvisAYVMQ---DDLLFPmLTV 206
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS--GTVRRAGGA---RV-----AYVPQrseVPDSLP-LTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFA--AEFRLPRTLSKSKKSARVQALiDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:NF040873 75 RDLVAMGrwARRGLWRRLTRDDRAAVDDAL-ERVGLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|.
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSIVIMSIHQP 315
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
132-343 |
2.01e-19 |
|
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: 88.06 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALAnRIAKGSlKGTVALNGEALesRLLKVIS-----AYVMQDDLLFPMlTV 206
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIP-RFYDVD-SGRILIDGHDV--RDYTLASlrrqiGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAAEFRLPRTLSKSKKSARVQALIDQLglRNAAKTVIGDeghRGV--SGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:cd03251 93 AENIAYGRPGATREEVEEAARAANAHEFIMEL--PEGYDTVIGE---RGVklSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 285 GLDSTSAYMVVKVLQRIAQS-GSIVIMsiHQPSyRILGlLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03251 168 ALDTESERLVQAALERLMKNrTTFVIA--HRLS-TIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
129-343 |
5.54e-19 |
|
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: 86.94 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALES-----RLLKVISaYVMQDDLLFPM 203
Cdd:TIGR04406 14 RKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDA--GKILIDGQDITHlpmheRARLGIG-YLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLMFAAEFRlpRTLSKSKKSARVQALIDQLGLrnaakTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPT 283
Cdd:TIGR04406 91 LTVEENIMAVLEIR--KDLDRAEREERLEALLEEFQI-----SHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 284 SGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHLKERGIGVLITDHNVR-ETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
86-338 |
6.59e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 86.62 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 86 SNLTYSIKSRRK-----MSLSSIFPRRsnrlgavaeaptvgesmfTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLID 160
Cdd:cd03267 4 SNLSKSYRVYSKepgliGSLKSLFKRK------------------YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 161 ALANRIAKGSlkGTVALNGE---ALESRLLKVISAYVMQDDLLFPMLTVEETL-MFAAEFRLPrtlsKSKKSARVQALID 236
Cdd:cd03267 66 ILSGLLQPTS--GEVRVAGLvpwKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFyLLAAIYDLP----PARFKKRLDELSE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 237 QLGLRNAAKTVIgdeghRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRI-AQSGSIVIMSIHQp 315
Cdd:cd03267 140 LLDLEELLDTPV-----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHY- 213
|
250 260
....*....|....*....|...
gi 356576859 316 SYRILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03267 214 MKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
127-353 |
7.28e-19 |
|
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: 86.48 E-value: 7.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEAL------ESRLLKVISAYVMQDDLL 200
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLERPT-SGSVLVDGTDLtllsgkELRKARRRIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLTVEETLMFAAEfrLPRTlSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:cd03258 94 LSSRTVFENVALPLE--IAGV-PKAEIEERVLELLELVGLEDKADAYPAQ-----LSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSI-HQPSYrILGLLDRMIFLSRGQTVYSGSPSQLplyfseFGHP 353
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRELGLTIVLItHEMEV-VKRICDRVAVMEKGEVVEEGTVEEV------FANP 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
100-343 |
1.00e-18 |
|
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: 86.93 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 100 LSSIFPRRSNRLGAVAEAPTVGESMFTRTKTL--LNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSLkGTVAL 177
Cdd:cd03294 6 LYKIFGKNPQKAFKLLAKGKSKEEILKKTGQTvgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCI-NRLIEPTS-GKVLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 178 NGEAL----ESRLLKVIS---AYVMQDDLLFPMLTVEETLMFAAEFrlpRTLSKSKKSARVQALIDQLGLRNAAKTVIGD 250
Cdd:cd03294 84 DGQDIaamsRKELRELRRkkiSMVFQSFALLPHRTVLENVAFGLEV---QGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 251 eghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDST-SAYMVVKVLQRIAQSGSIVIMSIHQPSYRI-LGllDRMIF 328
Cdd:cd03294 161 -----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLiRREMQDELLRLQAELQKTIVFITHDLDEALrLG--DRIAI 233
|
250
....*....|....*
gi 356576859 329 LSRGQTVYSGSPSQL 343
Cdd:cd03294 234 MKDGRLVQVGTPEEI 248
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
129-343 |
1.17e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.55 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL--ESRLLKVISAYVMQDDLLFPMLTV 206
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA--GSISLCGEPVpsRARHARQRVGVVPQFDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLM-FAAEFrlprTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSG 285
Cdd:PRK13537 98 RENLLvFGRYF----GLSAAAARALVPPLLEFAKLENKADAKVGE-----LSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 286 LDSTSAYMVVKVLQRIAQSGSIVIMSIH--QPSYRilgLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARGKTILLTTHfmEEAER---LCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
132-343 |
1.30e-18 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 85.67 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIdALANRIAkGSLKGTVALNGE---ALESRLLKVISAYVMQDDLLFPMlTVEE 208
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVV-SLLERFY-DPTSGEILLDGVdirDLNLRWLRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 TLMFAAEfrlPRTLSKSKKSARvQALIDQL--GLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDEPTSGL 286
Cdd:cd03249 96 NIRYGKP---DATDEEVEEAAK-KANIHDFimSLPDGYDTLVGERGSQ-LSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 287 DSTSAYMVVKVLQRIAQsGSIVIMSIHqpsyRILGL--LDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03249 171 DAESEKLVQEALDRAMK-GRTTIVIAH----RLSTIrnADLIAVLQNGQVVEQGTHDEL 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
132-343 |
1.39e-18 |
|
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: 85.35 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDaLANRIAKGSlKGTVALNGEAL----ESRLLKVIsAYVMQDDLLFPMlTVE 207
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLIN-LLMRFYDPQ-KGQILIDGIDIrdisRKSLRSMI-GVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEFRLPRTLSKSKKSARVQALIDQLglRNAAKTVIGDEGHrGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:cd03254 95 ENIRLGRPNATDEEVIEAAKEAGAHDFIMKL--PNGYDTVLGENGG-NLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 288 STSAYMVVKVLQRIaQSGSIVIMSIHQPSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03254 172 TETEKLIQEALEKL-MKGRTSIIIAHRLS--TIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
127-343 |
1.41e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGE-----ALESRLLKVIsAYVMQDDLLF 201
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEdisllPLHARARRGI-GYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAAEFRlpRTLSKSKKSARVQALIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:PRK10895 91 RRLSVYDNLMAVLQIR--DDLSAEQREDRANELMEEFHIEH-----LRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR-ETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
91-343 |
1.55e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.58 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 91 SIKSRRKMSLSSIFPRRSNRLGAVAeAPTVGESMFTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGS 170
Cdd:PRK13536 17 SPIERKHQGISEAKASIPGSMSTVA-IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 171 lkGTVALNGEAL--ESRLLKVISAYVMQDDLLFPMLTVEETLM-FAAEFRLprtlSKSKKSARVQALIDQLGLRNAAKTV 247
Cdd:PRK13536 96 --GKITVLGVPVpaRARLARARIGVVPQFDNLDLEFTVRENLLvFGRYFGM----STREIEAVIPSLLEFARLESKADAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 248 IGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIH--QPSYRilgLLDR 325
Cdd:PRK13536 170 VSD-----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfmEEAER---LCDR 241
|
250
....*....|....*...
gi 356576859 326 MIFLSRGQTVYSGSPSQL 343
Cdd:PRK13536 242 LCVLEAGRKIAEGRPHAL 259
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
128-333 |
3.15e-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: 82.65 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALES---RLLKVISAYVMQDDLLFPML 204
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS--GRVRLDGADISQwdpNELGDHVGYLPQDDELFSGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLmfaaefrlprtlskskksarvqalidqlglrnaaktvigdeghrgvSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:cd03246 92 IAENIL----------------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyrILGLLDRMIFLSRGQ 333
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGR 172
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
132-343 |
3.31e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.06 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGT-VALNGEAL--ESRLLKVI------SAYVMQDDLLFP 202
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShIELLGRTVqrEGRLARDIrksranTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAAEFRLP------RTLSKSKKSARVQALIdQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPIL 276
Cdd:PRK09984 100 RLSVLENVLIGALGSTPfwrtcfSWFTREQKQRALQALT-RVGMVHFAHQRVST-----LSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356576859 277 LFLDEPTSGLDSTSAYMVVKVLQRIAQSGSI-VIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGItVVVTLHQVDY-ALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
132-343 |
3.91e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.13 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALE---SRLLKV--ISAYVMQ--DDLLF-Pm 203
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHF-NGILKPT-SGEVLIKGEPIKydkKSLLEVrkTVGIVFQnpDDQLFaP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 lTVEETLMFAAefrLPRTLSKSKKSARVQALIDQLGLRNAAKTVigdeGHRgVSGGERRRVSIGTDIIHDPILLFLDEPT 283
Cdd:PRK13639 95 -TVEEDVAFGP---LNLGLSKEEVEKRVKEALKAVGMEGFENKP----PHH-LSGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 284 SGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQ----PSYrilglLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKEGITIIISTHDvdlvPVY-----ADKVYVMSDGKIIKEGTPKEV 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
132-343 |
5.12e-18 |
|
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: 88.23 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIdALANRIAKGSlKGTVALNGEALESRLLKVIS---AYVMQDDLLFPMlTVEE 208
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLV-NLIPRFYEPD-SGQILLDGHDLADYTLASLRrqvALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 TLMFAAEFRLPRT-LSKSKKSARVQALIDQLGlrNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:TIGR02203 425 NIAYGRTEQADRAeIERALAAAYAQDFVDKLP--LGLDTPIGENGVL-LSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 288 STSAYMVVKVLQRIAQS-GSIVIMsiHQPSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:TIGR02203 502 NESERLVQAALERLMQGrTTLVIA--HRLS--TIEKADRIVVMDDGRIVERGTHNEL 554
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
130-343 |
7.13e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.29 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKgSLKGTVAL----NGEALES----------------RLLKV 189
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHF-NGLIK-SKYGTIQVgdiyIGDKKNNhelitnpyskkiknfkELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 190 ISaYVMQddllFPML-----TVEETLMFAaefrlPRTLSKSKKSARVQA--LIDQLGLrnaaKTVIGDEGHRGVSGGERR 262
Cdd:PRK13631 118 VS-MVFQ----FPEYqlfkdTIEKDIMFG-----PVALGVKKSEAKKLAkfYLNKMGL----DDSYLERSPFGLSGGQKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 263 RVSI-GTDIIHDPILLFlDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPS 341
Cdd:PRK13631 184 RVAIaGILAIQPEILIF-DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLEVADEVIVMDKGKILKTGTPY 261
|
..
gi 356576859 342 QL 343
Cdd:PRK13631 262 EI 263
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
141-372 |
9.21e-18 |
|
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: 88.53 E-value: 9.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 141 DGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVISAYVM--QDDLLFPMLTVEETLMFAAEFRl 218
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTS--GTVLVGGKDIETNLDAVRQSLGMcpQHNILFHHLTVAEHILFYAQLK- 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 219 prtlSKSKKSARVQ--ALIDQLGLRNAAktvigDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVK 296
Cdd:TIGR01257 1032 ----GRSWEEAQLEmeAMLEDTGLHHKR-----NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 297 VLQRIaQSGSIVIMSIHQ-PSYRILGllDRMIFLSRGQTVYSGSPSQLPLYFSefghpipetdnrTEFALDLIRELE 372
Cdd:TIGR01257 1103 LLLKY-RSGRTIIMSTHHmDEADLLG--DRIAIISQGRLYCSGTPLFLKNCFG------------TGFYLTLVRKMK 1164
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
130-333 |
1.30e-17 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 82.40 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIDALanriakGSL----KGTVALNGEALE-------SRLLKVISAYVMQDD 198
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLL------GGLdnptSGEVLFNGQSLSklssnerAKLRNKKLGFIYQFH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 199 LLFPMLTVEETLMfaaefrLPRTLS-KSKKSA--RVQALIDQLGLRNAAKtvigdegHRG--VSGGERRRVSIGTDIIHD 273
Cdd:TIGR02211 93 HLLPDFTALENVA------MPLLIGkKSVKEAkeRAYEMLEKVGLEHRIN-------HRPseLSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 274 PILLFLDEPTSGLDSTSAYMVVKVLQRI--AQSGSIVIMSiHQPsyRILGLLDRMIFLSRGQ 333
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELnrELNTSFLVVT-HDL--ELAKKLDRVLEMKDGQ 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
129-353 |
2.30e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.49 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDAL-------ANRIAKG--SLKGTVALNGEALESRLLKVISAYVMQDDL 199
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeAGTIRVGdiTIDTARSLSQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 LFPMLTVEETLMFAaefrlPRTLSKSKKS---ARVQALIDQLGLrnAAKTvigDEGHRGVSGGERRRVSIGTDIIHDPIL 276
Cdd:PRK11264 96 LFPHRTVLENIIEG-----PVIVKGEPKEeatARARELLAKVGL--AGKE---TSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 277 LFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQLplyfseFGHP 353
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSF-ARDVADRAIFMDQGRIVEQGPAKAL------FADP 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
127-343 |
2.46e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKST-------LI--DAlanriakgslkGTVALNGEALES-----RLLKVISa 192
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVkpDS-----------GRIFLDGEDITHlpmhkRARLGIG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 193 YVMQDDLLFPMLTVEETLMFAAEFRlprTLSKSKKSARVQALIDQLGLRNAAKTvigdeghRG--VSGGERRRVSIGTDI 270
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELR---KLSKKEREERLEELLEEFGITHLRKS-------KAysLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 271 IHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSG-SIVImSIHqpSYR-ILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG1137 152 ATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGiGVLI-TDH--NVReTLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
132-353 |
4.08e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.73 E-value: 4.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANriAKGSLKGTVALNGEALESrllkvISAY------VMQDDLLFPMLT 205
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAG--FEQPTAGQIMLDGVDLSH-----VPPYqrpinmMFQSYALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFA-AEFRLPrtlsKSKKSARVQALIDQLGLRNAAKTvigdEGHRgVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:PRK11607 108 VEQNIAFGlKQDKLP----KAEIASRVNEMLGLVHMQEFAKR----KPHQ-LSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356576859 285 GLDST----SAYMVVKVLQRIaqsGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQLplyfseFGHP 353
Cdd:PRK11607 179 ALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQE-EAMTMAGRIAIMNRGKFVQIGEPEEI------YEHP 241
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
129-343 |
4.44e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.22 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDaLANRIAKGSlKGTVALNGE-----ALESrLLKVIsAYVMQDDLLFPM 203
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVN-LLLRFYDPT-SGRILIDGVdirdlTLES-LRRQI-GVVPQDTFLFSG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 lTVEETLMFAaefRLPRTLSKSKKSAR-VQA--LIDQL--GLRnaakTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLF 278
Cdd:COG1132 429 -TIRENIRYG---RPDATDEEVEEAAKaAQAheFIEALpdGYD----TVVGERGVN-LSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQsGSIVIMSIHQPSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLS--TIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
129-343 |
7.16e-17 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 80.36 E-value: 7.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESrllkvISAY------VMQDDLLFP 202
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTS--GEILLDGKDITN-----LPPHkrpvntVFQNYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAaeFRLpRTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:cd03300 86 HLTVFENIAFG--LRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQ-----LSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 283 TSGLDS---TSAYMVVKVLQRiaQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03300 158 LGALDLklrKDMQLELKRLQK--ELGITFVFVTHDQE-EALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
132-311 |
1.31e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.53 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL------ESRLLKVisAYVMQDDLLFPMLT 205
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDS--GEILLDGEPVrfrsprDAQAAGI--AIIHQELNLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSG 285
Cdd:COG1129 96 VAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGD-----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180
....*....|....*....|....*..
gi 356576859 286 LDSTSAYMVVKVLQRIAQSG-SIVIMS 311
Cdd:COG1129 171 LTEREVERLFRIIRRLKAQGvAIIYIS 197
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
132-305 |
1.73e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALaN----------RIAKGSLKGTVALNGEalESRLLKVISAYVMQDDLLF 201
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVL-NlletpdsgqlNIAGHQFDFSQKPSEK--AIRLLRQKVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAaefrlP-RTLSKSKKSARVQA--LIDQLGLRNAAktvigDEGHRGVSGGERRRVSIGTDIIHDP-ILL 277
Cdd:COG4161 95 PHLTVMENLIEA-----PcKVLGLSKEQAREKAmkLLARLRLTDKA-----DRFPLHLSGGQQQRVAIARALMMEPqVLL 164
|
170 180
....*....|....*....|....*...
gi 356576859 278 FlDEPTSGLDSTSAYMVVKVLQRIAQSG 305
Cdd:COG4161 165 F-DEPTAALDPEITAQVVEIIRELSQTG 191
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
132-372 |
2.05e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 79.78 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTL---IDALanriakgsLK---GTVALNG--EALESRLLKVIS--AYVMQD-DLL 200
Cdd:TIGR04520 18 LKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGL--------LLptsGKVTVDGldTLDEENLWEIRKkvGMVFQNpDNQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLTVEETLMFAAE-FRLPRtlskSKKSARVQALIDQLGLRNAAKTvigdEGHRgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:TIGR04520 90 FVGATVEDDVAFGLEnLGVPR----EEMRKRVDEALKLVGMEDFRDR----EPHL-LSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSI-HQPSYRILGllDRMIFLSRGQTVYSGSPSQLplyFS------EFGH 352
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISItHDMEEAVLA--DRVIVMNKGKIVAEGTPREI---FSqvellkEIGL 235
|
250 260
....*....|....*....|
gi 356576859 353 PIPetdnrteFALDLIRELE 372
Cdd:TIGR04520 236 DVP-------FITELAKALK 248
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
129-342 |
2.11e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.48 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALESRLLKVIS-----AYVMQ--DDLLF 201
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHL-NGLLKPT-SGKIIIDGVDITDKKVKLSDirkkvGLVFQypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 pmltvEETLMFAAEFRlPRTL--SKSKKSARVQALIDQLGLrnaAKTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:PRK13637 98 -----EETIEKDIAFG-PINLglSEEEIENRVKRAMNIVGL---DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 280 DEPTSGLDSTS---AYMVVKVLQRiaQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQ 342
Cdd:PRK13637 169 DEPTAGLDPKGrdeILNKIKELHK--EYNMTIILVSHSME-DVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
129-335 |
2.22e-16 |
|
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: 79.85 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANrIAKGSlKGTVALNGEAL------ESRLLKVISAYVMQDDL--L 200
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLG-LEKPA-QGTVSFRGQDLyqldrkQRRAFRRDVQLVFQDSPsaV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLTVEETLmfAAEFRLPRTLSKSKKSARVQALIDQLGLRNAaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:TIGR02769 102 NPRMTVRQII--GEPLRHLTSLDESEQKARIAELLDMVGLRSE----DADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTV 335
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
129-356 |
2.86e-16 |
|
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: 78.88 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIdALANRIAKGSlKGTVALNGEAL----ESRLLKVIsAYVMQDDLLFPML 204
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTM-KMINRLIEPT-SGEIFIDGEDIreqdPVELRRKI-GYVIQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFaaefrLPRTL--SKSKKSARVQALIDQLGLRNAAktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:cd03295 91 TVEENIAL-----VPKLLkwPKEKIRERADELLALVGLDPAE---FADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 283 TSGLDSTSAYMVVKVLQRIAQ-SGSIVIMSIH--QPSYRilgLLDRMIFLSRGQTVYSGSPSQLplyfseFGHPIPE 356
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQeLGKTIVFVTHdiDEAFR---LADRIAIMKNGEIVQVGTPDEI------LRSPAND 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
126-333 |
3.02e-16 |
|
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: 77.89 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 126 TRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKgsLKGTVALNGealesrllKVisAYVMQDDLLFPMlT 205
Cdd:cd03250 15 QETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK--LSGSVSVPG--------SI--AYVSQEPWIQNG-T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFAAEFRLPRTlsksKKSARVQAL---IDQLGLRNaaKTVIGDeghRGV--SGGERRRVSIGTDIIHDPILLFLD 280
Cdd:cd03250 82 IRENILFGKPFDEERY----EKVIKACALepdLEILPDGD--LTEIGE---KGInlSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 356576859 281 EPTSGLDS-TSAYMVVKVLQRIAQSGSIVIMSIHQPSYriLGLLDRMIFLSRGQ 333
Cdd:cd03250 153 DPLSAVDAhVGRHIFENCILGLLLNNKTRILVTHQLQL--LPHADQIVVLDNGR 204
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
132-343 |
4.48e-16 |
|
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: 78.15 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKG---SLKGTVALNGEALESRLLKVIS-AYVMQDDLLFPMLTVE 207
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLL-----RLIAGlerPDSGTILFGGEDATDVPVQERNvGFVFQHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEFRlPRTL--SKSKKSARVQALIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSG 285
Cdd:cd03296 93 DNVAFGLRVK-PRSErpPEAEIRAKVHELLKLVQLDW-----LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 356576859 286 LDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
132-342 |
4.60e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.08 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALA--NRIAKGSLK--GT--VALNGEALeSRLLKVISAYVMQDDLLFPMLT 205
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGclDKPTSGTYRvaGQdvATLDADAL-AQLRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFAAEFRlprTLSKSKKSARVQALIDQLGLrnaaktviGDEGH---RGVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:PRK10535 103 AAQNVEVPAVYA---GLERKQRLLRAQELLQRLGL--------EDRVEyqpSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 283 TSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPsyRILGLLDRMIFLSRGQTVySGSPSQ 342
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP--QVAAQAERVIEIRDGEIV-RNPPAQ 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
132-343 |
5.14e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.90 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVISA---YVMQD-DLLFPMLTVE 207
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEA--GTITVGGMVLSEETVWDVRRqvgMVFQNpDNQFVGATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEFR-LPRTlsksKKSARVQALIDQLGLRNAAKtvigDEGHRgVSGGERRRVSIGTDIIHDPILLFLDEPTSGL 286
Cdd:PRK13635 101 DDVAFGLENIgVPRE----EMVERVDQALRQVGMEDFLN----REPHR-LSGGQKQRVAIAGVLALQPDIIILDEATSML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 287 DSTSAYMVVKVLQRIAQSGSIVIMSI-HQpsyrilglL------DRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13635 172 DPRGRREVLETVRQLKEQKGITVLSItHD--------LdeaaqaDRVIVMNKGEILEEGTPEEI 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
129-341 |
6.24e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.19 E-value: 6.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEAL-----ESRLLKVISaYVMQDDLLFPM 203
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVTSGSILLDGEDIlelspDERARAGIF-LAFQYPVEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKtvigdegHRGV----SGGERRRVSIGTDIIHDPILLFL 279
Cdd:COG0396 92 VSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFL-------DRYVnegfSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPsyRILGLL--DRMIFLSRGQTVYSGSPS 341
Cdd:COG0396 165 DETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGRIVKSGGKE 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
135-342 |
7.84e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.67 E-value: 7.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 135 ISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSL--KGTVALNGEALES---RLLKVISAYVMQDDLLFPMLTVEET 209
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMA-----GLLpgSGSIQFAGQPLEAwsaAELARHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 210 LMfaaefrlpRTLSKSKKSARVQALIDQLglrnAAKTVIGDEGHRGV---SGGERRRVSIGTDI--IHDPI-----LLFL 279
Cdd:PRK03695 90 LT--------LHQPDKTRTEAVASALNEV----AEALGLDDKLGRSVnqlSGGEWQRVRLAAVVlqVWPDInpagqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQ 342
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLN-HTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
129-338 |
8.12e-16 |
|
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: 75.81 E-value: 8.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAkgSLKGTVALNGE---ALESRLLKVISaYVMQDDLLFpmlt 205
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLK--PQQGEITLDGVpvsDLEKALSSLIS-VLNQRPYLF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 vEETLMfaaefrlprtlskskksarvqaliDQLGLRnaaktvigdeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSG 285
Cdd:cd03247 88 -DTTLR------------------------NNLGRR--------------FSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 286 LDSTSAYMVVKVLQRIAQSGSIVIMsihqpSYRILGL--LDRMIFLSRGQTVYSG 338
Cdd:cd03247 129 LDPITERQLLSLIFEVLKDKTLIWI-----THHLTGIehMDKILFLENGKIIMQG 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
132-287 |
8.14e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 79.73 E-value: 8.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGsL----KGTVALNGealesrllKVIS---------AYVMQDD 198
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIA-----G-LedptSGEILIGG--------RDVTdlppkdrniAMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 199 LLFPMLTVEETLMFAAEFrlpRTLSKSKKSARVqalidqlglRNAAKTV-IGDEGHR---GVSGGERRRVSIGTDIIHDP 274
Cdd:COG3839 85 ALYPHMTVYENIAFPLKL---RKVPKAEIDRRV---------REAAELLgLEDLLDRkpkQLSGGQRQRVALGRALVREP 152
|
170
....*....|...
gi 356576859 275 ILLFLDEPTSGLD 287
Cdd:COG3839 153 KVFLLDEPLSNLD 165
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
130-340 |
8.76e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 8.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKGSLK---GTVALNGEALESRLLKVIS---AYVMQDDLLFPM 203
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLL-----RAINGTLTptaGTVLVAGDDVEALSARAASrrvASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLmfaaefRLPRTLSKSKKS-------ARVQALIDQLGLrnaakTVIGDEGHRGVSGGERRRVSIGTDIIHDPIL 276
Cdd:PRK09536 92 FDVRQVV------EMGRTPHRSRFDtwtetdrAAVERAMERTGV-----AQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356576859 277 LFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQpsyriLGL----LDRMIFLSRGQTVYSGSP 340
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHD-----LDLaaryCDELVLLADGRVRAAGPP 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
128-343 |
9.41e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 78.11 E-value: 9.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLidalaNRIAKGSLK---GTVALNGEALESRLLKVISAY---VMQD-DLL 200
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTI-----SKILTGLLKpqsGEIKIDGITISKENLKEIRKKigiIFQNpDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLTVEETLMFAAEfrlprtlSKSKKSARVQALIDQLGLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:PRK13632 96 FIGATVEDDIAFGLE-------NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQN-LSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSI-HQPSYRILGllDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISItHDMDEAILA--DKVIVFSEGKLIAQGKPKEI 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
132-343 |
1.22e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIdALANRiAKGSLKGTVALNGEAL----ESRLLKVISaYVMQDDLLFPMlTVE 207
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLL-QLLTR-AWDPQQGEILLNGQPIadysEAALRQAIS-VVSQRVHLFSA-TLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEfrlprtlskSKKSARVQALIDQLGLRNAAKTV------IGdEGHRGVSGGERRRVSIGTDIIHD-PILLfLD 280
Cdd:PRK11160 432 DNLLLAAP---------NASDEALIEVLQQVGLEKLLEDDkglnawLG-EGGRQLSGGEQRRLGIARALLHDaPLLL-LD 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQsGSIVIMSIHqpsyRILGL--LDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK11160 501 EPTEGLDAETERQILELLAEHAQ-NKTVLMITH----RLTGLeqFDRICVMDNGQIIEQGTHQEL 560
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
123-343 |
1.43e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.12 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 123 SMFTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNR----IAKGSLKGTVALNGEALESR------LLKVIsA 192
Cdd:PRK14239 12 SVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRmndlNPEVTITGSIVYNGHNIYSPrtdtvdLRKEI-G 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 193 YVMQDDLLFPMlTVEETLMFAaeFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDEGhRGVSGGERRRVSIGTDIIH 272
Cdd:PRK14239 90 MVFQQPNPFPM-SIYENVVYG--LRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSA-LGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356576859 273 DPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIM--SIHQPSyRIlglLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVtrSMQQAS-RI---SDRTGFFLDGDLIEYNDTKQM 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
129-313 |
1.82e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.05 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKviSAYVMQDDLLFPMLTVEE 208
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH--GSITLDGKPVEGPGAE--RGVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 TLMFAAEFRlprTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDS 288
Cdd:PRK11248 90 NVAFGLQLA---GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ-----LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180
....*....|....*....|....*.
gi 356576859 289 -TSAYMVVKVLQRIAQSGSIVIMSIH 313
Cdd:PRK11248 162 fTREQMQTLLLKLWQETGKQVLLITH 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
128-287 |
2.48e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKGSLK---GTVALNGEAlesRLlkvisAYVMQDDLLFPML 204
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLL-----KILAGELEpdsGEVSIPKGL---RI-----GYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLM-------------FAAEFRLPRTLSKSKKSARVQALIDQLGLRNA---AKTVI------GDEGHRGV---SGG 259
Cdd:COG0488 77 TVLDTVLdgdaelraleaelEELEAKLAEPDEDLERLAELQEEFEALGGWEAearAEEILsglgfpEEDLDRPVselSGG 156
|
170 180
....*....|....*....|....*...
gi 356576859 260 ERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
124-353 |
2.93e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.36 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 124 MFTRT---KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKgslKGTVALNGEALES----RLLKVIS--AYV 194
Cdd:PRK15134 291 ILKRTvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS---QGEIWFDGQPLHNlnrrQLLPVRHriQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 195 MQD--DLLFPMLTVEETLMFAAEFRLPrTLSKSKKSARVQALIDQLGLRNAAKtvigdegHR---GVSGGERRRVSIGTD 269
Cdd:PRK15134 368 FQDpnSSLNPRLNVLQIIEEGLRVHQP-TLSAAQREQQVIAVMEEVGLDPETR-------HRypaEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 270 IIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQLplyfse 349
Cdd:PRK15134 440 LILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV------ 513
|
....
gi 356576859 350 FGHP 353
Cdd:PRK15134 514 FAAP 517
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
128-287 |
3.15e-15 |
|
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: 75.37 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALA--NRIAKGSL--KGTVALNGEALESRLlkvisAYVMQDDLLFPM 203
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAglEEPTSGRIyiGGRDVTDLPPKDRDI-----AMVFQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLMFaaefrlPRTLSKSKKSArvqalIDQlGLRNAAKTV-IGDEGHR---GVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:cd03301 87 MTVYDNIAF------GLKLRKVPKDE-----IDE-RVREVAELLqIEHLLDRkpkQLSGGQRQRVALGRAIVREPKVFLM 154
|
....*...
gi 356576859 280 DEPTSGLD 287
Cdd:cd03301 155 DEPLSNLD 162
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
132-343 |
6.78e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.02 E-value: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALES--------RLLKVIS-AYVMQDDLLFp 202
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHF-NALLKPS-SGTITIAGYHITPetgnknlkKLRKKVSlVFQFPEAQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 mltvEETLMFAAEFRlPRTLSKSKKSARVQAL--IDQLGLrnaaKTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:PRK13641 100 ----ENTVLKDVEFG-PKNFGFSEDEAKEKALkwLKKVGL----SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMD-DVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
128-342 |
6.93e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.05 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnRIAKgSLKGTVALNGEALESRLLKVISAYV--MQDDLLFPM-L 204
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA-RLLT-PQSGTVFLGDKPISMLSSRQLARRLalLPQHHLTPEgI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAaefRLPRTLSKSKKSARVQALIDQlglrNAAKTVIGDEGHRGV---SGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:PRK11231 92 TVRELVAYG---RSPWLSLWGRLSAEDNARVNQ----AMEQTRINHLADRRLtdlSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIH---QPS-YrilglLDRMIFLSRGQTVYSGSPSQ 342
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQASrY-----CDHLVVLANGHVMAQGTPEE 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
132-314 |
9.90e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 74.28 E-value: 9.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALanRIAKGSLKGTVALNGEAL---------ESRLLKVISAYVMQDDLLFP 202
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVL--NLLEMPRSGTLNIAGNHFdfsktpsdkAIRELRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAaefrlP-RTLSKSKKSARVQA--LIDQLGLRNAAktvigDEGHRGVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:PRK11124 96 HLTVQQNLIEA-----PcRVLGLSKDQALARAekLLERLRLKPYA-----DRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190
....*....|....*....|....*....|....*
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQ 314
Cdd:PRK11124 166 DEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
123-358 |
1.07e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 75.89 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 123 SMFTRTKTL---LNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSL---KGTVALNGE---ALESRLLKVISAy 193
Cdd:COG4586 26 GLFRREYREveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT-----GILvptSGEVRVLGYvpfKRRKEFARRIGV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 194 VM-QDDLLFPMLTVEETL-MFAAEFRLPRTLSKskksARVQALIDQLGLRNAAKTVIgdeghRGVSGGERRRVSIGTDII 271
Cdd:COG4586 100 VFgQRSQLWWDLPAIDSFrLLKAIYRIPDAEYK----KRLDELVELLDLGELLDTPV-----RQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 272 HDPILLFLDEPTSGLDSTSAYMVVKVLQRI-AQSGSIVIMSIHqpsY--RILGLLDRMIFLSRGQTVYSGSPSQLPLYFS 348
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSH---DmdDIEALCDRVIVIDHGRIIYDGSLEELKERFG 247
|
250
....*....|....*..
gi 356576859 349 -------EFGHPIPETD 358
Cdd:COG4586 248 pyktivlELAEPVPPLE 264
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
132-343 |
1.11e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.15 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANriAKGSLKGTVALNGEALE----SRLLKVISAYVMQDDLLFPMLTVE 207
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRATSGRIVFDGKDITdwqtAKIMREAVAIVPEGRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAeFRLPRTLSKsKKSARVQALIDQLGLRNAAKTVIgdeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:PRK11614 99 ENLAMGG-FFAERDQFQ-ERIKWVYELFPRLHERRIQRAGT-------MSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 288 STSAYMVVKVLQRIAQSGsIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQG-MTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
124-340 |
1.47e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 74.48 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 124 MFTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKG------SLKGTVALNGEALES----RLLKVISAY 193
Cdd:PRK13547 9 VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgaRVTGDVTLNGEPLAAidapRLARLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 194 VMQDDLLFPmLTVEETLMFAaefRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGdeghRGV---SGGERRRVSIGT-- 268
Cdd:PRK13547 89 PQAAQPAFA-FSAREIVLLG---RYPHARRAGALTHRDGEIAWQALALAGATALVG----RDVttlSGGELARVQFARvl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 269 -------DIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSI-HQPSYRILgLLDRMIFLSRGQTVYSGSP 340
Cdd:PRK13547 161 aqlwpphDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAAR-HADRIAMLADGAIVAHGAP 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
132-371 |
3.07e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.90 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALnGEalesrllKVISAYVMQDDL------------ 199
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHL-NGLLQPT-SGTVTI-GE-------RVITAGKKNKKLkplrkkvgivfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 -----LFPMlTVEETLMFAaefrlPRTLSKSKKSARVQA--LIDQLGLRNAaktvIGDEGHRGVSGGERRRVSIGTDIIH 272
Cdd:PRK13634 93 fpehqLFEE-TVEKDICFG-----PMNFGVSEEDAKQKAreMIELVGLPEE----LLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 273 DPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSI-VIMSIHQ----PSYRilgllDRMIFLSRGQTVYSGSPSQL---P 344
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLtTVLVTHSmedaARYA-----DQIVVMHKGTVFLQGTPREIfadP 237
|
250 260
....*....|....*....|....*..
gi 356576859 345 LYFSEFGHPIPETdnrTEFALDLIREL 371
Cdd:PRK13634 238 DELEAIGLDLPET---VKFKRALEEKF 261
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
132-340 |
3.17e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.97 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDAL-------------------ANRIAKGSLKGTVALNGEALESRLLKVISA 192
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLnalllpdtgtiewifkdekNKKKTKEKEKVLEKLVIQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 193 YVMQDDLLFPML-------TVEETLMFAaefrlPRTLSKSKKSARVQAL--IDQLGLrnaaktvigDEGHR-----GVSG 258
Cdd:PRK13651 103 IRRRVGVVFQFAeyqlfeqTIEKDIIFG-----PVSMGVSKEEAKKRAAkyIELVGL---------DESYLqrspfELSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 259 GERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSG 338
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD-NVLEWTKRTIFFKDGKIIKDG 247
|
..
gi 356576859 339 SP 340
Cdd:PRK13651 248 DT 249
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
129-350 |
3.76e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.04 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIA-KGSLKgtvaLNGEAL----ESRLLKVIsAYVMQDDLLFPM 203
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyQGSLK----INGIELreldPESWRKHL-SWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 lTVEETLMFAAEFRLPRTLSKSKKSARVQALIDQL--GLrnaaKTVIGDEGhRGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:PRK11174 438 -TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLpqGL----DTPIGDQA-AGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQsGSIVIMSIHQPSYriLGLLDRMIFLSRGQTVYSGSPSQL---PLYFSEF 350
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASR-RQTTLMVTHQLED--LAQWDQIWVMQDGQIVQQGDYAELsqaGGLFATL 580
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
100-333 |
3.92e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 100 LSSIFPRRSNRLGAV---AEAPTVGESMFTRTKTLlNDISGEARDGEIMAVLGASGSGKSTLIDALANrIAKGSLKGTVA 176
Cdd:TIGR02633 242 ITSLYPHEPHEIGDVileARNLTCWDVINPHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKFEGNVF 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 177 LNGEALESR-LLKVIS---AYVMQD---DLLFPMLTVEETLMFAA--EFRLPRTLSKSKKSARVQALIDQLGLRNAAKTV 247
Cdd:TIGR02633 320 INGKPVDIRnPAQAIRagiAMVPEDrkrHGIVPILGVGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 248 -IGdeghrGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSG-SIVIMSIHQPsyRILGLLDR 325
Cdd:TIGR02633 400 pIG-----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELA--EVLGLSDR 472
|
....*...
gi 356576859 326 MIFLSRGQ 333
Cdd:TIGR02633 473 VLVIGEGK 480
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
132-343 |
4.33e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.61 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRI--AKGSLK-GTVALNGEALESRLL----KVISAYVMQDDLLFpml 204
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqpTEGKVTvGDIVVSSTSKQKEIKpvrkKVGVVFQFPESQLF--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 tvEETLMFAAEFRlPRTLSKSKKSARVQAL--IDQLGLRNAaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:PRK13643 99 --EETVLKDVAFG-PQNFGIPKEKAEKIAAekLEMVGLADE----FWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 283 TSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
132-378 |
4.92e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.96 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEAL----ESRLLKV---ISaYVMQDDLLFPML 204
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI-NLLERPT-SGSVLVDGVDLtalsERELRAArrkIG-MIFQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAaeFRLPRTlSKSKKSARVQALIDQLGLrnaaktvigdEGHRGV-----SGGERRRVSIGTDIIHDPILLFL 279
Cdd:COG1135 98 TVAENVALP--LEIAGV-PKAEIRKRVAELLELVGL----------SDKADAypsqlSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQS-G-SIVI----MSIhqpsyrILGLLDRMIFLSRGQTVYSGSPSQLplyfseFGHP 353
Cdd:COG1135 165 DEATSALDPETTRSILDLLKDINRElGlTIVLitheMDV------VRRICDRVAVLENGRIVEQGPVLDV------FANP 232
|
250 260 270
....*....|....*....|....*....|...
gi 356576859 354 --------IPETDNRTEFALDLIRELEGSPGGT 378
Cdd:COG1135 233 qseltrrfLPTVLNDELPEELLARLREAAGGGR 265
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
129-341 |
7.72e-14 |
|
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: 71.02 E-value: 7.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEalesrllkvisayvmqdDLLFpmLTVEE 208
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKGE-----------------DITD--LPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 ------TLMFAAEFRLPrtlskskksarvqalidqlGLRNAaktvigdEGHRGV----SGGERRRVSIGTDIIHDPILLF 278
Cdd:cd03217 74 rarlgiFLAFQYPPEIP-------------------GVKNA-------DFLRYVnegfSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPsyRILGLL--DRMIFLSRGQTVYSGSPS 341
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQ--RLLDYIkpDRVHVLYDGRIVKSGDKE 190
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
130-315 |
1.22e-13 |
|
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: 70.08 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKG---SLKGTVALNGEAL-ESR-LLKVISAYVMQDDLLFPML 204
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLL-----RILAGllrPDSGEVRWNGTPLaEQRdEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAAEFRLPRTLSkskksarVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRT-------IEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|.
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSIVIMSIHQP 315
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
129-305 |
1.56e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANriAKGSLKGTVALNGEALESRLLKVISAY------VMQDDL--L 200
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVG--LESPSQGNVSWRGEPLAKLNRAQRKAFrrdiqmVFQDSIsaV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLTVEETLmfAAEFRLPRTLSKSKKSARVQALIDQLGLRNAaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:PRK10419 103 NPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDDS----VLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180
....*....|....*....|....*...
gi 356576859 281 EPTSGLD---STSAYMVVKVLQRiaQSG 305
Cdd:PRK10419 177 EAVSNLDlvlQAGVIRLLKKLQQ--QFG 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
132-289 |
1.68e-13 |
|
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: 73.57 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGslkGTVALNGEALESRLLKVISAY------VMQDDL--LFPM 203
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE---GEIRFDGQDLDGLSRRALRPLrrrmqvVFQDPFgsLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLmfaAE-FRL-PRTLSKSKKSARVQALIDQLGLrnaaktvigDEGHRG-----VSGGERRRVSIGTDIIHDPIL 276
Cdd:COG4172 379 MTVGQII---AEgLRVhGPGLSAAERRARVAEALEEVGL---------DPAARHrypheFSGGQRQRIAIARALILEPKL 446
|
170
....*....|...
gi 356576859 277 LFLDEPTSGLDST 289
Cdd:COG4172 447 LVLDEPTSALDVS 459
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
130-313 |
2.05e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIDALAN--RIAKGSlkgtVALNGEALESRLLKVISAYVMQD---DLLFPML 204
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfvRLASGK----ISILGQPTRQALQKNLVAYVPQSeevDWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 tVEETLMFA-----AEFRLPrtlsKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:PRK15056 97 -VEDVVMMGryghmGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190
....*....|....*....|....*....|....
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIH 313
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
129-466 |
2.78e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.91 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDAL----------------------ANRIAKGSLKGT-VALNGEALES- 184
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyeptsgriiyhvalcekCGYVERPSKVGEpCPVCGGTLEPe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 185 -------------RLLKVISAYVMQDDLLFPMLTVEETLMFAaefrLPRTLSKSKKSA-RVQALIDQLGLRNAAKTVIgd 250
Cdd:TIGR03269 93 evdfwnlsdklrrRIRKRIAIMLQRTFALYGDDTVLDNVLEA----LEEIGYEGKEAVgRAVDLIEMVQLSHRITHIA-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 251 eghRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSI-VIMSIHQPSYrILGLLDRMIFL 329
Cdd:TIGR03269 167 ---RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIsMVLTSHWPEV-IEDLSDKAIWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 330 SRGQTVYSGSPSQLPLYFSEfGHPIPETDNRTEFALDLIRelegspggtksLVEFNKSWQSMtkhhqekeeERNGLSLKE 409
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAVFME-GVSEVEKECEVEVGEPIIK-----------VRNVSKRYISV---------DRGVVKAVD 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 410 AISASISRGKL-----VSGASNTN---------PNPSSMVPTFANQFWVEMatlSKRSFLNSRRMPELIGI 466
Cdd:TIGR03269 302 NVSLEVKEGEIfgivgTSGAGKTTlskiiagvlEPTSGEVNVRVGDEWVDM---TKPGPDGRGRAKRYIGI 369
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
126-289 |
3.22e-13 |
|
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: 72.79 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 126 TRTKTLLNDISGEARDGEIMAVLGASGSGKS----TLIDALANRIAKGSlkGTVALNGEAL----ESRLLKV----IsAY 193
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPS--GSILFDGQDLlglsERELRRIrgnrI-AM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 194 VMQDDL--LFPMLTVE----ETLmfaaefRLPRTLSKSKKSARVQALIDQLGLRNAAKtVIGDEGHRgVSGGERRRVSIG 267
Cdd:COG4172 97 IFQEPMtsLNPLHTIGkqiaEVL------RLHRGLSGAAARARALELLERVGIPDPER-RLDAYPHQ-LSGGQRQRVMIA 168
|
170 180
....*....|....*....|..
gi 356576859 268 TDIIHDPILLFLDEPTSGLDST 289
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVT 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
132-333 |
3.64e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 69.39 E-value: 3.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDAL-AN-RIAKGSL-----KGTVALnGEALESRLLKV----ISaYVMQddll 200
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIyGNyLPDSGSIlvrhdGGWVDL-AQASPREILALrrrtIG-YVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 F----PMLTveeTLMFAAEFRLPRTLSKSKKSARVQALIDQLGL-----RNAAKTVigdeghrgvSGGERRRVSIGTDII 271
Cdd:COG4778 101 FlrviPRVS---ALDVVAEPLLERGVDREEARARARELLARLNLperlwDLPPATF---------SGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 272 HDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRiLGLLDRMIFLSRGQ 333
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR-EAVADRVVDVTPFS 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
128-353 |
3.85e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKStlIDALAN-RIAKGS----LKGTVALNGEAL----ESRLLKVIS---AYVM 195
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKS--VTALSIlRLLPSPpvvyPSGDIRFHGESLlhasEQTLRGVRGnkiAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 196 QDDL--LFPMLTVEETLmfAAEFRLPRTLSKskKSARVQAL--IDQLGLRNAAKTvIGDEGHRgVSGGERRRVSIGTDII 271
Cdd:PRK15134 99 QEPMvsLNPLHTLEKQL--YEVLSLHRGMRR--EAARGEILncLDRVGIRQAAKR-LTDYPHQ-LSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 272 HDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQLplyFSEFG 351
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL---FSAPT 249
|
..
gi 356576859 352 HP 353
Cdd:PRK15134 250 HP 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
129-343 |
4.22e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVIS---AYVMQDDLLFPMLT 205
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSE--GEILLDAQPLESWSSKAFArkvAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEEtlmFAAEFRLP--RTLSK--SKKSARVQALIDQLGLRNAAktvigdegHRGV---SGGERRRVSIGTDIIHDPILLF 278
Cdd:PRK10575 102 VRE---LVAIGRYPwhGALGRfgAADREKVEEAISLVGLKPLA--------HRLVdslSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQ----PSYrilglLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDinmaARY-----CDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
132-343 |
6.22e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.92 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIdALANRIAKGSLkGTVALNGE-----ALESrLLKVIsAYVMQDDLLFPMlTV 206
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDPQS-GRILIDGTdirtvTRAS-LRRNI-AVVFQDAGLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAAEFRLPRTLSKSKKSARVQALIdqlgLRNAAK--TVIGDEGhRGVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:PRK13657 426 EDNIRVGRPDATDEEMRAAAERAQAHDFI----ERKPDGydTVVGERG-RQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSIVIMSiHQPSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13657 501 ALDVETEAKVKAALDELMKGRTTFIIA-HRLS--TVRNADRILVFDNGRVVESGSFDEL 556
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
127-333 |
7.29e-13 |
|
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: 67.46 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANriAKGSLKGTVALNGEAL------ESRLLKVisAYVMQD--- 197
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFG--LRPPASGEITLDGKPVtrrsprDAIRAGI--AYVPEDrkr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 198 DLLFPMLTVEETLMfaaefrLPRTLskskksarvqalidqlglrnaaktvigdeghrgvSGGERRRVSIGTDIIHDPILL 277
Cdd:cd03215 87 EGLVLDLSVAENIA------LSSLL----------------------------------SGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 278 FLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSihqpSY---RILGLLDRMIFLSRGQ 333
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLI----SSeldELLGLCDRILVMYEGR 181
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
142-333 |
7.33e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.65 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 142 GEIMAVLGASGSGKSTLIDALANrIAKGSlKGTVALNGEAL-----ESR--LLKVISAYVMQDDLLFPMLTVEETLMFAA 214
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAG-LDDGS-SGEVSLVGQPLhqmdeEARakLRAKHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 215 efrLPRTLSKSKKSARVQALIDQLGLrnaaktvigdeGHR------GVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDS 288
Cdd:PRK10584 114 ---LLRGESSRQSRNGAKALLEQLGL-----------GKRldhlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 356576859 289 TSAYMVVKVLQRIAQS-GSIVIMSIHQPsyRILGLLDRMIFLSRGQ 333
Cdd:PRK10584 180 QTGDKIADLLFSLNREhGTTLILVTHDL--QLAARCDRRLRLVNGQ 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
76-322 |
7.36e-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: 68.65 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 76 PRSLPFVLSFSNLTYSiksrrkmslssiFPRRSNRLgavaeaptvgesmftrtktLLNDISGEARDGEIMAVLGASGSGK 155
Cdd:cd03248 5 PDHLKGIVKFQNVTFA------------YPTRPDTL-------------------VLQDVSFTLHPGEVTALVGPSGSGK 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 156 STLIDALANRIAkgSLKGTVALNGEAL---ESRLLKVISAYVMQDDLLFPMlTVEETLMFAaefrLPRTLSKSKKSARVQ 232
Cdd:cd03248 54 STVVALLENFYQ--PQGGQVLLDGKPIsqyEHKYLHSKVSLVGQEPVLFAR-SLQDNIAYG----LQSCSFECVKEAAQK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 233 ALIDQL--GLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIM 310
Cdd:cd03248 127 AHAHSFisELASGYDTEVGEKGSQ-LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVI 205
|
250
....*....|....*.
gi 356576859 311 SIH----QPSYRILGL 322
Cdd:cd03248 206 AHRlstvERADQILVL 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
144-339 |
7.40e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.67 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 144 IMAVLGASGSGKSTLIDALANRIAKGslKGTVALNGEAL-----------ESRllKVisAYVMQDDLLFPMLTVEETLMF 212
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQ--KGRIVLNGRVLfdaekgiclppEKR--RI--GYVFQDARLFPHYKVRGNLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 213 ------AAEF--------------RLPRTLSkskksarvqalidqlglrnaaktvigdeghrgvsGGERRRVSIGTDIIH 272
Cdd:PRK11144 100 gmaksmVAQFdkivallgieplldRYPGSLS----------------------------------GGEKQRVAIGRALLT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 273 DPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGS 339
Cdd:PRK11144 146 APELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
131-326 |
8.69e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.69 E-value: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 131 LLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALeSRLLKVISA--------YVMQDDLLFP 202
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTS--GDVIFNGQPM-SKLSSAAKAelrnqklgFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMfaaefrLPRTLSKSKKS---ARVQALIDQLGLRNAAKtvigdegHRG--VSGGERRRVSIGTDIIHDPILL 277
Cdd:PRK11629 101 DFTALENVA------MPLLIGKKKPAeinSRALEMLAAVGLEHRAN-------HRPseLSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 356576859 278 FLDEPTSGLDSTSAYMVVKVLQRI-AQSGSIVIMSIHQpsyriLGLLDRM 326
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHD-----LQLAKRM 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
100-333 |
9.39e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 9.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 100 LSSIFPRRSNRLGAV---AEAPTVGESMFTRTKtLLNDISGEARDGEIMAVLGASGSGKSTLIDALANrIAKGSLKGTVA 176
Cdd:PRK13549 244 LTALYPREPHTIGEVileVRNLTAWDPVNPHIK-RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPGRWEGEIF 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 177 LNGEALESR-LLKVIS---AYVMQD---DLLFPMLTVEETLMFAA--EFRLPRTLSKSKKSARVQALIDQLGLRNAAKTV 247
Cdd:PRK13549 322 IDGKPVKIRnPQQAIAqgiAMVPEDrkrDGIVPVMGVGKNITLAAldRFTGGSRIDDAAELKTILESIQRLKVKTASPEL 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 248 -IGdeghrGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSG-SIVIMSIHQPsyRILGLLDR 325
Cdd:PRK13549 402 aIA-----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGvAIIVISSELP--EVLGLSDR 474
|
....*...
gi 356576859 326 MIFLSRGQ 333
Cdd:PRK13549 475 VLVMHEGK 482
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
134-338 |
1.03e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 134 DISGEARDGEIMAVLGASGSGKSTLIDALANRIA-----------KGSLKGTVALnGEALESRLLKVISAYVMQD--DLL 200
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLApdagevhyrmrDGQLRDLYAL-SEAERRRLLRTEWGFVHQHprDGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLT----VEETLMFAAEfrlpRTLSKSKKSA-----RVQalIDQLGLrnaaktvigDEGHRGVSGGERRRVSIGTDII 271
Cdd:PRK11701 103 RMQVSaggnIGERLMAVGA----RHYGDIRATAgdwleRVE--IDAARI---------DDLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 272 HDPILLFLDEPTSGLD-STSAYMVVKVLQRIAQSGSIVIMSIHQpsyriLG----LLDRMIFLSRGQTVYSG 338
Cdd:PRK11701 168 THPRLVFMDEPTGGLDvSVQARLLDLLRGLVRELGLAVVIVTHD-----LAvarlLAHRLLVMKQGRVVESG 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
132-343 |
1.11e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.11 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALE-SR--LLKVISAYVM----QDDLLFPML 204
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNL-NGILKPS-SGRILFDGKPIDySRkgLMKLRESVGMvfqdPDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAAEFRLPrtlsKSKKSARVQALIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:PRK13636 100 VYQDVSFGAVNLKLP----EDEVRKRVDNALKRTGIEH-----LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 285 GLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQ----PSYrilglLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKElGLTIIIATHDidivPLY-----CDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
134-353 |
1.18e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 134 DISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVIS-----------------AYVMQ 196
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAG--GLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgadmAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 197 DDL--LFPMLTVEETLmfAAEFRLPRTLSKSKKSARVQALIDQLGLRNAaKTVIGDEGHRgVSGGERRRVSIGTDIIHDP 274
Cdd:PRK10261 112 EPMtsLNPVFTVGEQI--AESIRLHQGASREEAMVEAKRMLDQVRIPEA-QTILSRYPHQ-LSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 275 ILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQLplyFSEFGHP 353
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI---FHAPQHP 263
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
128-343 |
1.48e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.60 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKGSLK---GTVALNGEALESR----LLKVISAYVMQDDLL 200
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTV-----RLIDGLLEaesGQIIIDGDLLTEEnvwdIRHKIGMVFQNPDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLTVEETLMFAAEFR-LPRTLSKSkksaRVQALIDQLGLRNAAKTvigdEGHRgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:PRK13650 94 FVGATVEDDVAFGLENKgIPHEEMKE----RVNEALELVGMQDFKER----EPAR-LSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRIlGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
124-343 |
1.67e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.15 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 124 MFTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRI-----AKGSLKGTVALNGE---ALESRLLKVISAYVM 195
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLieiydSKIKVDGKVLYFGKdifQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 196 QDDLLFPMLTVEETLMFAAEFRLPRTLSKSKKSarVQALIDQLGLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPI 275
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKVGLWKEVYDRLNSPASQ-LSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356576859 276 LLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSiHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQ-QVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
140-353 |
1.69e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.16 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 140 RDGEIMAVLGASGSGKSTLIDALANrIAKGSLKGTV---ALNGEAL------ESRllKVIS---AYVMQDDL--LFPMLT 205
Cdd:COG4170 31 NEGEIRGLVGESGSGKSLIAKAICG-ITKDNWHVTAdrfRWNGIDLlklsprERR--KIIGreiAMIFQEPSscLDPSAK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFAaefrLPRTLSKSK-------KSARVQALIDQLGLRNaaktvigdegHRGV--------SGGERRRVSIGTDI 270
Cdd:COG4170 108 IGDQLIEA----IPSWTFKGKwwqrfkwRKKRAIELLHRVGIKD----------HKDImnsyphelTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 271 IHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQLplyFSEF 350
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQI---LKSP 250
|
...
gi 356576859 351 GHP 353
Cdd:COG4170 251 HHP 253
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
132-343 |
2.07e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.20 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKST---LIDALANRiakgsLKGTVALNGEALESR----LLKVISAYVMQDDLLFPML 204
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFEE-----FEGKVKIDGELLTAEnvwnLRRKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAAEFR-LPRT-LSKSKKSARVQALIDQLGLRNAAKtvigdeghrgVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:PRK13642 98 TVEDDVAFGMENQgIPREeMIKRVDEALLAVNMLDFKTREPAR----------LSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 283 TSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQpSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKYQLTVLSITH-DLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
125-343 |
2.20e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.29 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 125 FTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALESRLLKVISAYV-----MQDDL 199
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHF-NGILKPT-SGSVLIRGEPITKENIREVRKFVglvfqNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 LFPMlTVEETLMFAAefrLPRTLSKSKKSARVQALIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:PRK13652 91 IFSP-TVEQDIAFGP---INLGLDEETVAHRVSSALHMLGLEE-----LRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
130-362 |
2.53e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.60 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAK-GSLKGTVALNGEAL----ESRLLKVIS---AYVMQDDL-- 199
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAnGRIGGSATFNGREIlnlpEKELNKLRAeqiSMIFQDPMts 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 LFPMLTVEETLMfaAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTvIGDEGHRgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:PRK09473 110 LNPYMRVGEQLM--EVLMLHKGMSKAEAFEESVRMLDAVKMPEARKR-MKMYPHE-FSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQLplyFSEFGHP----- 353
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGV-VAGICDKVLVMYAGRTMEYGNARDV---FYQPSHPysigl 261
|
250
....*....|..
gi 356576859 354 ---IPETDNRTE 362
Cdd:PRK09473 262 lnaVPRLDAEGE 273
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
125-300 |
2.86e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.96 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 125 FTRTKtLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKG---SLKGTVALNGE---ALESRLLKVisAYVMQDD 198
Cdd:PRK10851 12 FGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLL-----RIIAGlehQTSGHIRFHGTdvsRLHARDRKV--GFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 199 LLFPMLTVEETLMFAAEFrLPRTLSKSKK--SARVQALIDQLGLRNAAktvigDEGHRGVSGGERRRVSIGTDIIHDPIL 276
Cdd:PRK10851 84 ALFRHMTVFDNIAFGLTV-LPRRERPNAAaiKAKVTQLLEMVQLAHLA-----DRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180
....*....|....*....|....
gi 356576859 277 LFLDEPTSGLDStsayMVVKVLQR 300
Cdd:PRK10851 158 LLLDEPFGALDA----QVRKELRR 177
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
113-339 |
2.90e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.58 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 113 AVAEAPTVGESMF--TRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkgtvalnGEALESRLLkvi 190
Cdd:PTZ00243 655 RSAKTPKMKTDDFfeLEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISE--------GRVWAERSI--- 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 191 sAYVMQDDLLFPMlTVEETLMFAAEFRLPRtLSKSKKSARVQALIDQLGlrNAAKTVIGDEGhRGVSGGERRRVSIGTDI 270
Cdd:PTZ00243 724 -AYVPQQAWIMNA-TVRGNILFFDEEDAAR-LADAVRVSQLEADLAQLG--GGLETEIGEKG-VNLSGGQKARVSLARAV 797
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 271 IHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQpsYRILGLLDRMIFLSRGQTVYSGS 339
Cdd:PTZ00243 798 YANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDGRVEFSGS 864
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
136-340 |
3.25e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 136 SGEARDGEIMAVLGASGSGKSTLIDALANRIA--KGSLKGTVAlngealesrllkvIS---AYVMQDdllFPMlTVEETL 210
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKpdEGEVDEDLK-------------ISykpQYISPD---YDG-TVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 211 MFAAEFRLPRTLSKSKksarvqaLIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTS 290
Cdd:COG1245 423 RSANTDDFGSSYYKTE-------IIKPLGLEK-----LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 356576859 291 AYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIflsrgqtVYSGSP 340
Cdd:COG1245 491 RLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM-------VFEGEP 533
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
126-341 |
3.29e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 67.05 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 126 TRTKTL----LNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLKGTVALNGEALESRLLKviSAYVMQDdllF 201
Cdd:cd03237 5 TMKKTLgeftLEVEGGSISESEVIGILGPNGIGKTTFIKMLA-----GVLKPDEGDIEIELDTVSYK--PQYIKAD---Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMlTVEETLMfaaefrlPRTLSKSKKSARVQALIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:cd03237 75 EG-TVRDLLS-------SITKDFYTHPYFKTEIAKPLQIEQ-----ILDREVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIflsrgqtVYSGSPS 341
Cdd:cd03237 142 PSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI-------VFEGEPS 194
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
129-333 |
4.47e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGS---LKGTVALNGEALESRLLkvisayvMQDDLLFPMLT 205
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAgelLAGTAPLAEAREDTRLM-------FQDARLLPWKK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFAaefrlprtLSKSKKSARVQALiDQLGLRNAAKtvigdEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSG 285
Cdd:PRK11247 98 VIDNVGLG--------LKGQWRDAALQAL-AAVGLADRAN-----EWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 356576859 286 LDSTSAYMVVKVLQRI-AQSGSIVIMSIHQPSYRIlGLLDRMIFLSRGQ 333
Cdd:PRK11247 164 LDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAV-AMADRVLLIEEGK 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
132-343 |
6.70e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 6.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALAN--RIAKGS--LKGTVALNGEALESrLLKVISAYVMQDDLLFPMLTVE 207
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGllRPQKGKvlVSGIDTGDFSKLQG-IRKLVGIVFQNPETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAE-FRLPRTlskskksaRVQALIDqlglRNAAKTVIGDEGHRG---VSGGERRRVSIGTDIIHDPILLFLDEPT 283
Cdd:PRK13644 97 EDLAFGPEnLCLPPI--------EIRKRVD----RALAEIGLEKYRHRSpktLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 284 SGLDSTSAYMVVKVLQRIAQSGSIVIMSIHqpSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
129-315 |
6.81e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.21 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKG---SLKGTVALNGEALEsrllKVISAYvmQDDLLF---- 201
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLL-----RILAGlarPDAGEVLWQGEPIR----RQRDEY--HQDLLYlghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 ----PMLTVEETLMFAAefRLPRTLSKSkksARVQALiDQLGLRN----AAKTVigdeghrgvSGGERRRVSIGTDIIHD 273
Cdd:PRK13538 83 pgikTELTALENLRFYQ--RLHGPGDDE---ALWEAL-AQVGLAGfedvPVRQL---------SAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 356576859 274 PILLFLDEPTSGLDSTSaymvVKVLQRI----AQSGSIVIMSIHQP 315
Cdd:PRK13538 148 APLWILDEPFTAIDKQG----VARLEALlaqhAEQGGMVILTTHQD 189
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
132-337 |
8.38e-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: 63.99 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRllkvisayvmqddllfpmltveetlm 211
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDS--GEILVDGKEVSFA-------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 212 faaefrlprtlskSKKSARVQ--ALIDQLglrnaaktvigdeghrgvSGGERRRVSIGTDIIHDPILLFLDEPTSGLDST 289
Cdd:cd03216 68 -------------SPRDARRAgiAMVYQL------------------SVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 356576859 290 SAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYS 337
Cdd:cd03216 117 EVERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDGRVVGT 163
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
131-338 |
9.50e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 65.70 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 131 LLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRI----AKGSLKGTVALNGE---ALESRLLKVISAYVMQDDLLFPM 203
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLielyPEARVSGEVYLDGQdifKMDVIELRRRVQMVFQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLmfAAEFRLPRtLSKSKKS--ARVQALIDQLGLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:PRK14247 97 LSIFENV--ALGLKLNR-LVKSKKElqERVRWALEKAQLWDEVKDRLDAPAGK-LSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSiHQPSyRILGLLDRMIFLSRGQTVYSG 338
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVT-HFPQ-QAARISDYVAFLYKGQIVEWG 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
138-343 |
1.05e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.37 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 138 EARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGE--ALESRLLKVISAyVMQDDLLFPMLTVEETLMFAAE 215
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPAS--GSLTLNGQdhTTTPPSRRPVSM-LFQENNLFSHLTVAQNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 216 FRLprTLSKSKKsARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDII-HDPILLfLDEPTSGLD-STSAYM 293
Cdd:PRK10771 98 PGL--KLNAAQR-EKLHAIARQMGIEDLLARLPGQ-----LSGGQRQRVALARCLVrEQPILL-LDEPFSALDpALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 356576859 294 VVKVLQRIAQSGSIVIMSIHQ--PSYRIlglLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSleDAARI---APRSLVVADGRIAWDGPTDEL 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
142-315 |
1.39e-11 |
|
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: 64.44 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 142 GEIMAVLGASGSGKSTLIDALANRIAKgsLKGTVALNGEALESRLLKVISA--YVMQDDLLFPMLTVEETLMFAAEFrlp 219
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPP--LAGRVLLNGGPLDFQRDSIARGllYLGHAPGIKTTLSVLENLRFWHAD--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 220 rtlskSKKSARVQALiDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSaymVVKVLQ 299
Cdd:cd03231 101 -----HSDEQVEEAL-ARVGLNG-----FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG---VARFAE 166
|
170
....*....|....*....
gi 356576859 300 RIA---QSGSIVIMSIHQP 315
Cdd:cd03231 167 AMAghcARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
132-343 |
1.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.80 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDaLANRIAKgSLKGTVALNGEALESRLLKVISAYVMQDDL----LFPML--- 204
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQ-LTNGLII-SETGQTIVGDYAIPANLKKIKEVKRLRKEIglvfQFPEYqlf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 --TVEETLMFAaefrlPRTLSKSKKSA--RVQALIDQLGL-RNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:PRK13645 105 qeTIEKDIAFG-----PVNLGENKQEAykKVPELLKLVQLpEDYVKRSPFE-----LSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQS-GSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
96-335 |
1.43e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 96 RKM---SLSSIFPRRSNRLGAV---AEAPTVGESmftrtktlLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKG 169
Cdd:COG1129 234 RLMvgrELEDLFPKRAAAPGEVvleVEGLSVGGV--------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 170 SlkGTVALNGEALesRLLKVISA------YVMQDDL---LFPMLTVEE--TLMFAAEFRLPRTLSKSKKSARVQALIDQL 238
Cdd:COG1129 306 S--GEIRLDGKPV--RIRSPRDAiragiaYVPEDRKgegLVLDLSIREniTLASLDRLSRGGLLDRRRERALAEEYIKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 239 GLR-NAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSG-SIVIMSihqpS 316
Cdd:COG1129 382 RIKtPSPEQPVGN-----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGkAVIVIS----S 452
|
250 260
....*....|....*....|.
gi 356576859 317 Y--RILGLLDRMIFLSRGQTV 335
Cdd:COG1129 453 ElpELLGLSDRILVMREGRIV 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
142-344 |
1.52e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 142 GEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALeSRLLKV----ISAY-VMQDDLLFPMLTVEETLMfaaeF 216
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDS--GTLEIGGNPC-ARLTPAkahqLGIYlVPQEPLLFPNLSVKENIL----F 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 217 RLPRT-LSKSKKSARVQALIDQLGLRNAAKTV-IGDeghrgvsggeRRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMV 294
Cdd:PRK15439 110 GLPKRqASMQKMKQLLAALGCQLDLDSSAGSLeVAD----------RQIVEILRGLMRDSRILILDEPTASLTPAETERL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 356576859 295 VKVLQRIAQSG-SIVIMSIHQPSYRILGllDRMIFLSRGQTVYSGSPSQLP 344
Cdd:PRK15439 180 FSRIRELLAQGvGIVFISHKLPEIRQLA--DRISVMRDGTIALSGKTADLS 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
128-340 |
1.65e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.51 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKG---SLKGTVALNGEAL-----ESRLLKVisayVMQDDL 199
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVL-----RLIAGfetPDSGRIMLDGQDIthvpaENRHVNT----VFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 LFPMLTVEETLMFAaeFRLPRTlSKSKKSARV-QAL----IDQLGLRNAAKtvigdeghrgVSGGERRRVSIGTDIIHDP 274
Cdd:PRK09452 97 LFPHMTVFENVAFG--LRMQKT-PAAEITPRVmEALrmvqLEEFAQRKPHQ----------LSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356576859 275 ILLFLDEPTSGLDstsaY-------MVVKVLQRiaQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSP 340
Cdd:PRK09452 164 KVLLLDESLSALD----YklrkqmqNELKALQR--KLGITFVFVTHDQE-EALTMSDRIVVMRDGRIEQDGTP 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
126-310 |
1.84e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 126 TRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALES----RLLKVISaYVMQDDLLF 201
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS--GTLLFEGEDISTlkpeIYRQQVS-YCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMlTVEETLMFAAEFRlprtlSKSKKSARVQALIDQLGLRNAaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:PRK10247 94 GD-TVYDNLIFPWQIR-----NQQPDPAIFLDDLERFALPDT----ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180
....*....|....*....|....*....
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIM 310
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVL 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
99-333 |
1.90e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 99 SLSSIFPRRSNRLGavaEAPTVGESMFTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALN 178
Cdd:PRK10982 234 SLTQRFPDKENKPG---EVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSA--GTITLH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 179 GEALESR-LLKVIS---AYVMQDDL---LFPMLTVEETLMFA------AEFRLprtLSKSKKSARVQALIDQLGLRNAA- 244
Cdd:PRK10982 309 GKKINNHnANEAINhgfALVTEERRstgIYAYLDIGFNSLISnirnykNKVGL---LDNSRMKSDTQWVIDSMRVKTPGh 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 245 KTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGS-IVIMSIHQPsyRILGLL 323
Cdd:PRK10982 386 RTQIGS-----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKgIIIISSEMP--ELLGIT 458
|
250
....*....|
gi 356576859 324 DRMIFLSRGQ 333
Cdd:PRK10982 459 DRILVMSNGL 468
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
132-340 |
2.47e-11 |
|
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: 64.05 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALAnRIAKGSlKGTVALNG--------EALESRLlkvisAYVMQDDLLFPM 203
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALF-RLVELS-SGSILIDGvdiskiglHDLRSRI-----SIIPQDPVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 lTVEETLMF---AAEFRLPRTLSKSKKSARVQALIDQLGlrnaakTVIgDEGHRGVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:cd03244 93 -TIRSNLDPfgeYSDEELWQALERVGLKEFVESLPGGLD------TVV-EEGGENLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRiAQSGSIVIMSIHqpsyRILGLL--DRMIFLSRGQTVYSGSP 340
Cdd:cd03244 165 EATASVDPETDALIQKTIRE-AFKDCTVLTIAH----RLDTIIdsDRILVLDKGRVVEFDSP 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
132-333 |
2.93e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRL----LKVISAYVMQD---DLLFPML 204
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTS--GYVTLDGHEVVTRSpqdgLANGIVYISEDrkrDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAaKTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:PRK10762 346 SVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNI-KTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSG-SIVIMSIHQPsyRILGLLDRMIFLSRGQ 333
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGlSIILVSSEMP--EVLGMSDRILVMHEGR 472
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
131-346 |
3.15e-11 |
|
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: 66.69 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 131 LLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALES---RLLKVISAYVMQDDLLFPMLTVE 207
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS--GEILLNGFSLKDidrHTLRQFINYLPQEPYIFSGSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEFRLPRTLSKSKKSARVQALIDQLGLrnAAKTVIGDEGHrGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:TIGR01193 567 NLLLGAKENVSQDEIWAACEIAEIKDDIENMPL--GYQTELSEEGS-SISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 288 STSAYMVVKVLQRIAQSGSIVI---MSIHQPSyrilgllDRMIFLSRGQTVYSGSPSQLPLY 346
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDKTIIFVahrLSVAKQS-------DKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
125-343 |
3.35e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.40 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 125 FTR-TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL----ESRLLKVISAYVM--QD 197
Cdd:PRK11831 15 FTRgNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDH--GEILFDGENIpamsRSRLYTVRKRMSMlfQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 198 DLLFPMLTVEETLMFA--AEFRLPRTLSKSKKSARVQALidqlGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPI 275
Cdd:PRK11831 93 GALFTDMNVFDNVAYPlrEHTQLPAPLLHSTVMMKLEAV----GLRGAAKLMPSE-----LSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356576859 276 LLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
132-342 |
3.57e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEAL------ESRLLKVisAYVMQDDLLFP 202
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILY-----GLYQpdsGEILIDGKPVrirsprDAIALGI--GMVHQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:COG3845 94 NLTVAENIVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVED-----LSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356576859 283 TSGL-----DStsaymVVKVLQRIAQSG-SIVIMS--IHQpsyrILGLLDRMIFLSRGQTVYSGSPSQ 342
Cdd:COG3845 169 TAVLtpqeaDE-----LFEILRRLAAEGkSIIFIThkLRE----VMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
129-355 |
3.69e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.44 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKST---LIDAL----ANRIAKGSLKGtVALNGEALESRLLKVisAYVMQD-DLL 200
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLllpdDNPNSKITVDG-ITLTAKTVWDIREKV--GIVFQNpDNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLTVEETLMFAAEfrlPRTLSKSKKSARVQALIDQLGLRNAAktvigDEGHRGVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:PRK13640 97 FVGATVGDDVAFGLE---NRAVPRPEMIKIVRDVLADVGMLDYI-----DSEPANLSGGQKQRVAIAGILAVEPKIIILD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIhqpSYRI--LGLLDRMIFLSRGQTVYSGSPSQL---PLYFSEFGHPIP 355
Cdd:PRK13640 169 ESTSMLDPAGKEQILKLIRKLKKKNNLTVISI---THDIdeANMADQVLVLDDGKLLAQGSPVEIfskVEMLKEIGLDIP 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
133-333 |
3.77e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 133 NDISGEARDGEIMAVLGASGSGKSTLIDAL--ANRIAKGSlkgtVALNGEALESR----LLKVISAYVMQ---DDLLFPM 203
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLfgVDKRAGGE----IRLNGKDISPRspldAVKKGMAYITEsrrDNGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 204 LTVEETLMFAAEFRLPR------TLSKSKKSARVQALIDQLGLRNAAKtvigDEGHRGVSGGERRRVSIGTDIIHDPILL 277
Cdd:PRK09700 356 FSIAQNMAISRSLKDGGykgamgLFHEVDEQRTAENQRELLALKCHSV----NQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 278 FLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIM-SIHQPsyRILGLLDRMIFLSRGQ 333
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMvSSELP--EIITVCDRIAVFCEGR 486
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
132-343 |
5.51e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.05 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIdALANRIAKGSlKGTVALNG---------EALESRLLKVisAYVMQDDLLFP 202
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMV-RLLNRLIEPT-RGQVLIDGvdiakisdaELREVRRKKI--AMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAAEfrLPRTLSKSKKSARVQALiDQLGLRNAAKTViGDEghrgVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:PRK10070 120 HMTVLDNTAFGME--LAGINAEERREKALDAL-RQVGLENYAHSY-PDE----LSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 283 TSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
132-343 |
7.54e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.51 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL---ESRLLKVISAYVMQDDLLFPMlTVEE 208
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG--GQVLLDGVPLvqyDHHYLHRQVALVGQEPVLFSG-SVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 TLMFAAEFRLPRTLSKSKKSARVQALIdqLGLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDS 288
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAKAANAHDFI--MEFPNGYDTEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 289 TSAYMvvkvLQRIAQSGSIVIMSI-HQPSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:TIGR00958 651 ECEQL----LQESRSRASRTVLLIaHRLS--TVERADQILVLKKGSVVEMGTHKQL 700
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
119-287 |
7.85e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.22 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 119 TVGESMFTRTKTL--LNDISGEARDGEIMAVLGASGSGKSTLIDALAnRIAKGSlKGTVALNGEAL------ESRLLKVI 190
Cdd:PRK11308 16 PVKRGLFKPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIETPT-GGELYYQGQDLlkadpeAQKLLRQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 191 SAYVMQDDL--LFPMLTVEETLmfAAEFRLPRTLSKSKKSARVQALIDQLGLRNAaktvigdegHRG-----VSGGERRR 263
Cdd:PRK11308 94 IQIVFQNPYgsLNPRKKVGQIL--EEPLLINTSLSAAERREKALAMMAKVGLRPE---------HYDryphmFSGGQRQR 162
|
170 180
....*....|....*....|....
gi 356576859 264 VSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALD 186
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
129-287 |
8.00e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAkgSLKGTVALnGEalesrllKVISAYVMQD-DLLFPMLTVE 207
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELE--PDSGTVKL-GE-------TVKIGYFDQHqEELDPDKTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLmfaaefrlpRTLSKSKKSARVQALIDQLGLRnaaktviGDEGHRGV---SGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:COG0488 398 DEL---------RDGAPGGTEQEVRGYLGRFLFS-------GDDAFKPVgvlSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
...
gi 356576859 285 GLD 287
Cdd:COG0488 462 HLD 464
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
128-343 |
8.37e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlKGTVALNGEAlesrllkvisAYVMQDDLLFPMlTVE 207
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVVIRGSV----------AYVPQVSWIFNA-TVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEFRlPRTLSKSKKSARVQALIDQLGLRNaaKTVIGDEGhRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:PLN03232 697 ENILFGSDFE-SERYWRAIDVTALQHDLDLLPGRD--LTEIGERG-VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 288 STSAYMVVKVLQRIAQSGSIVIMSIHQPSYriLGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PLN03232 773 AHVAHQVFDSCMKDELKGKTRVLVTNQLHF--LPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
140-313 |
8.53e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 65.81 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 140 RDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVAlnGEALESRLLKVIS--AYVMQDDLLFPMLTVEETLMFAAEFR 217
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVA--GKSILTNISDVHQnmGYCPQFDAIDDLLTGREHLYLYARLR 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 218 -LPrtlskSKKSARVQAL-IDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVV 295
Cdd:TIGR01257 2041 gVP-----AEEIEKVANWsIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170
....*....|....*...
gi 356576859 296 KVLQRIAQSGSIVIMSIH 313
Cdd:TIGR01257 2111 NTIVSIIREGRAVVLTSH 2128
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
144-343 |
9.27e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.10 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 144 IMAVLGASGSGKSTLIDALANRIAKGslKGTVALNGEALESR-----LLKVISAYVMQD-DLLFPMLTVEETLMFA---- 213
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQ--KGAVLWQGKPLDYSkrgllALRQQVATVFQDpEQQIFYTDIDSDIAFSlrnl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 214 --AEFRLPRTLSKSkksarvQALIDQLGLRNAAKTVIgdeghrgvSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSA 291
Cdd:PRK13638 107 gvPEAEITRRVDEA------LTLVDAQHFRHQPIQCL--------SHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 356576859 292 YMVVKVLQRIAQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
129-309 |
1.08e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.96 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKGSLKgtvALNGEALESRLLKVisAYVMQDDLLFPMLTVEE 208
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGVDK---DFNGEARPQPGIKV--GYLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 TLM---------------FAAEFRLPRTLSKS--KKSARVQALIDQLGLRNAAKTV----------IGDEGHRGVSGGER 261
Cdd:TIGR03719 88 NVEegvaeikdaldrfneISAKYAEPDADFDKlaAEQAELQEIIDAADAWDLDSQLeiamdalrcpPWDADVTKLSGGER 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 356576859 262 RRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAqsGSIVI 309
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GTVVA 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
132-343 |
1.42e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALES-------RLLKVISAYVMQddllFPML 204
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNI-NALLKPT-TGTVTVDDITITHktkdkyiRPVRKRIGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 -----TVEETLMFAAE-FRLPrtLSKSKksARVQALIDQLGL-RNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILL 277
Cdd:PRK13646 97 qlfedTVEREIIFGPKnFKMN--LDEVK--NYAHRLLMDLGFsRD-----VMSQSPFQMSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 278 FLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
129-343 |
1.77e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.42 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALA---NRIAKGSLKGTVALNGEAL----ESRLLKVISAYVMQDDLLF 201
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmnDKVSGYRYSGDVLLGGRSIfnyrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLmfaAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:PRK14271 114 PMSIMDNVL---AGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSiHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRLTVIIVT-HNLA-QAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
96-315 |
1.83e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 96 RKMSLSSIF---PRRSNRLGAVAEAPTVGESmfTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLK 172
Cdd:COG2401 9 VLMRVTKVYssvLDLSERVAIVLEAFGVELR--VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 173 GTVALngealesrllkvisayvmqDDLLFPmltveetlmfaaefrlprtlskskksaRVQALIDQLGLR---NAAKTVIG 249
Cdd:COG2401 87 GCVDV-------------------PDNQFG---------------------------REASLIDAIGRKgdfKDAVELLN 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 250 DEG----------HRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSI-HQP 315
Cdd:COG2401 121 AVGlsdavlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVAtHHY 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
136-361 |
2.61e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 136 SGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLKGTvalNGEALESrlLKVisAYVMQ---DDllFPMlTVEETLMF 212
Cdd:PRK13409 359 GGEIYEGEVIGIVGPNGIGKTTFAKLLA-----GVLKPD---EGEVDPE--LKI--SYKPQyikPD--YDG-TVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 213 AAEfRLPRTLSKSKksarvqaLIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAY 292
Cdd:PRK13409 424 ITD-DLGSSYYKSE-------IIKPLQLER-----LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 293 MVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIflsrgqtVYSGSPsqlplyfSEFGHPIPETDNRT 361
Cdd:PRK13409 491 AVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM-------VFEGEP-------GKHGHASGPMDMRE 545
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
132-343 |
3.72e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 61.29 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALESRLLKVISA---YVMQD--DLLFPMlTV 206
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHL-NGIYLPQ-RGRVKVMGREVNAENEKWVRSkvgLVFQDpdDQVFSS-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAaefrlPRT--LSKSKKSARVQALIDQLGLRNAAktvigDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:PRK13647 98 WDDVAFG-----PVNmgLDKDEVERRVEEALKAVRMWDFR-----DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQGKTVIVATHDVDL-AAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
126-373 |
5.49e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.74 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 126 TRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIdALANRIAKGSlKGTVALNGEAL------ESRLLKVISAYVMQDdl 199
Cdd:PRK11153 15 GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLI-RCINLLERPT-SGRVLVDGQDLtalsekELRKARRQIGMIFQH-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 lFPML---TVEETLMFAAEfrLPRTlSKSKKSARVQALIDQLGLrnaaktviGDEGHR---GVSGGERRRVSIGTDIIHD 273
Cdd:PRK11153 91 -FNLLssrTVFDNVALPLE--LAGT-PKAEIKARVTELLELVGL--------SDKADRypaQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 274 PILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSI-HQPSYrILGLLDRMIFLSRGQTVYSGSPSQLplyfseFGH 352
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLItHEMDV-VKRICDRVAVIDAGRLVEQGTVSEV------FSH 231
|
250 260
....*....|....*....|.
gi 356576859 353 PipetdnRTEFALDLIRELEG 373
Cdd:PRK11153 232 P------KHPLTREFIQSTLH 246
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
132-338 |
5.88e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.49 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANriAKGSLKGTVALNGEALeSRLLKVISA-----YVMQDDLLFPMLTV 206
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSG--IHEPTKGTITINNINY-NKLDHKLAAqlgigIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAaefRLP-------RTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:PRK09700 98 LENLYIG---RHLtkkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN-----LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSG 338
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLA-EIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
125-301 |
6.10e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 61.26 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 125 FTRTKTL--LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEAL----ESRLLKVISAYVM--Q 196
Cdd:PRK15079 28 WQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATD--GEVAWLGKDLlgmkDDEWRAVRSDIQMifQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 197 DDL--LFPMLTVEETLMFAAEFRLPRtLSKSKKSARVQALIDQLGLRnaaKTVIGDEGHRgVSGGERRRVSIGTDIIHDP 274
Cdd:PRK15079 106 DPLasLNPRMTIGEIIAEPLRTYHPK-LSRQEVKDRVKAMMLKVGLL---PNLINRYPHE-FSGGQCQRIGIARALILEP 180
|
170 180
....*....|....*....|....*..
gi 356576859 275 ILLFLDEPTSGLDSTSAYMVVKVLQRI 301
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQL 207
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
133-288 |
6.95e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.58 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 133 NDISGEARDGEIMAVLGASGSGKSTLIDALA--NRIAKGSLK-GTVALNGEALESRLLKVisayVMQDDLLFPMLTVEET 209
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAglEDITSGDLFiGEKRMNDVPPAERGVGM----VFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 210 LMFAAEfrlprtLSKSKKS---ARVQ--ALIDQLG--LRNAAKTVigdeghrgvSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:PRK11000 96 MSFGLK------LAGAKKEeinQRVNqvAEVLQLAhlLDRKPKAL---------SGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
....*.
gi 356576859 283 TSGLDS 288
Cdd:PRK11000 161 LSNLDA 166
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
140-322 |
7.60e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.50 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 140 RDGEIMAVLGASGSGKSTLIDALANrIAKGSlKGTVALNGEALeSRL-------LKVISAYVMQDDLLFPMLTVEETLMf 212
Cdd:PRK10908 26 RPGEMAFLTGHSGAGKSTLLKLICG-IERPS-AGKIWFSGHDI-TRLknrevpfLRRQIGMIFQDHHLLMDRTVYDNVA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 213 aaefrLPRTLSKSKKS---ARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDST 289
Cdd:PRK10908 102 -----IPLIIAGASGDdirRRVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 356576859 290 SAYMVVKVLQRIAQSGSIVIMSIH------QPSYRILGL 322
Cdd:PRK10908 172 LSEGILRLFEEFNRVGVTVLMATHdiglisRRSYRMLTL 210
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
132-290 |
8.60e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.96 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTlIDALANRIAKGSlKGTVALNGEALESRLLKVIS---AYVMQDDLLFPMlTVEE 208
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKST-IANLLTRFYDID-EGEILLDGHDLRDYTLASLRnqvALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 TLMFAAEFRLPR-TLSKSKKSARVQALIDQLglRNAAKTVIGDEGhRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:PRK11176 436 NIAYARTEQYSReQIEEAARMAYAMDFINKM--DNGLDTVIGENG-VLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
...
gi 356576859 288 STS 290
Cdd:PRK11176 513 TES 515
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
79-343 |
9.06e-10 |
|
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: 62.66 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 79 LPFVLS-FSNLTYSIKSRRK-MSLSSIFP----RRSNRLGAvAEAPTVGESMFTRTKTL---LNDISGEARDGEIMAVLG 149
Cdd:TIGR00957 593 LPMVISsIVQASVSLKRLRIfLSHEELEPdsieRRTIKPGE-GNSITVHNATFTWARDLpptLNGITFSIPEGALVAVVG 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 150 ASGSGKSTLIDALANRIAKgsLKGTVALNGEAlesrllkvisAYV-----MQDDllfpmlTVEETLMFAAEFRLPRTLSK 224
Cdd:TIGR00957 672 QVGCGKSSLLSALLAEMDK--VEGHVHMKGSV----------AYVpqqawIQND------SLRENILFGKALNEKYYQQV 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 225 SKKSArvqALIDQLGLRNAAKTVIGDEGhRGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSA-YMVVKVLQRIAQ 303
Cdd:TIGR00957 734 LEACA---LLPDLEILPSGDRTEIGEKG-VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkHIFEHVIGPEGV 809
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 356576859 304 -SGSIVIMSIHQPSYriLGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:TIGR00957 810 lKNKTRILVTHGISY--LPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
130-314 |
1.10e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.38 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEALESRLLKVIS----AYVMQDDLLFPMLT 205
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTEragiVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFAAEFRLP-RTLSKSKKSARVQALIDQLGLRNAAKT-VIGDEGhrgvsGGERRRVSIGTDIIHDPILLFLDEPT 283
Cdd:TIGR02633 95 VAENIFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTrPVGDYG-----GGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190
....*....|....*....|....*....|.
gi 356576859 284 SGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQ 314
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
135-376 |
1.15e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.53 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 135 ISGEARDGEIMAVLGASGSGKSTLIDALANRIakgSLKGTVALNGEALESRLLKVIS------------AYVMQDDL--L 200
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI---DYPGRVMAEKLEFNGQDLQRISekerrnlvgaevAMIFQDPMtsL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FPMLTVEETLMFAaeFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVigDEGHRGVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:PRK11022 103 NPCYTVGFQIMEA--IKVHQGGNKKTRRQRAIDLLNQVGIPDPASRL--DVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQLplyFSEFGHPIPETDNR 360
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI---FRAPRHPYTQALLR 255
|
250
....*....|....*...
gi 356576859 361 T--EFALDLIReLEGSPG 376
Cdd:PRK11022 256 AlpEFAQDKAR-LASLPG 272
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
131-304 |
1.24e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 131 LLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKG--SLKGTVALNGEALESRLLKVIS-AYVMQD--DLLFPMLT 205
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrQTAGRVLLDGKPVAPCALRGRKiATIMQNprSAFNPLHT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 ----VEETLmfaaefrlpRTLSKSKKSARVQALIDQLGLRNAAKtvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:PRK10418 98 mhthARETC---------LALGKPADDATLTAALEAVGLENAAR--VLKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180
....*....|....*....|...
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQS 304
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQK 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
132-343 |
2.43e-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: 60.59 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALN---------GEALESRLLKVIsAYVMQDDLLFP 202
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvdmtkpGPDGRGRAKRYI-GILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAAEFRLPRTLskskksARVQALI--DQLGLRNAAKTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:TIGR03269 379 HRTVLDNLTEAIGLELPDEL------ARMKAVItlKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 281 EPTSGLDSTSAYMVVKVL--QRIAQSGSIVIMSiHQPSYrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSIlkAREEMEQTFIIVS-HDMDF-VLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
128-339 |
4.14e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEAL-----ESRL-LKVISAYvmQDDLLF 201
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGESIldlepEERAhLGIFLAF--QYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAAEFRLP-RTLSKSKKSARVQALIDQLGLRNAAKTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:CHL00131 97 PGVSNADFLRLAYNSKRKfQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFSGGEKKRNEILQMALLDSELAILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSG-SIVIMSIHQpsyrilGLLDRMI-----FLSRGQTVYSGS 339
Cdd:CHL00131 177 ETDSGLDIDALKIIAEGINKLMTSEnSIILITHYQ------RLLDYIKpdyvhVMQNGKIIKTGD 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
132-313 |
4.31e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGE---------ALESRLlkvisAYVMQDDLLFP 202
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA--GSILIDGQemrfasttaALAAGV-----AIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAaefRLPRT---LSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFL 279
Cdd:PRK11288 93 EMTVAENLYLG---QLPHKggiVNRRLLNYEAREQLEHLGVDIDPDTPLKY-----LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190
....*....|....*....|....*....|....
gi 356576859 280 DEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIH 313
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
129-352 |
4.43e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.82 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkgtvalnGEALESRLLKVisAYVMQD---DLLFPmLT 205
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE--------GVIKRNGKLRI--GYVPQKlylDTTLP-LT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFAAEFRLPRTLSKSKksaRVQA--LIDQlglrnaaktvigdeGHRGVSGGERRRVSIGTDIIHDPILLFLDEPT 283
Cdd:PRK09544 86 VNRFLRLRPGTKKEDILPALK---RVQAghLIDA--------------PMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 284 SGLD---STSAYMVVKVLQRiaQSGSIVIMSIHQpSYRILGLLDRMIFLSRgQTVYSGSP---SQLPLYFSEFGH 352
Cdd:PRK09544 149 QGVDvngQVALYDLIDQLRR--ELDCAVLMVSHD-LHLVMAKTDEVLCLNH-HICCSGTPevvSLHPEFISMFGP 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
132-309 |
7.75e-09 |
|
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: 59.06 E-value: 7.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLI-------DALAnriakgslkGTVALNGEAL-----ESrLLKVIsAYVMQDDL 199
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLArllfrfyDVTS---------GRILIDGQDIrdvtqAS-LRAAI-GIVPQDTV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 200 LF------------PMLTVEEtLMFAAefrlprtlskskKSARVQALIDQL--GLrnaaKTVIGDeghRGV--SGGERRR 263
Cdd:COG5265 443 LFndtiayniaygrPDASEEE-VEAAA------------RAAQIHDFIESLpdGY----DTRVGE---RGLklSGGEKQR 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 356576859 264 VSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQS-GSIVI 309
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGrTTLVI 549
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
185-319 |
8.44e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 185 RLLKVISAYVMQDDLLFPMlTVEETLMFAAEFRLPRTLSKSKKSARVQALIDQLglRNAAKTVIGDEGhRGVSGGERRRV 264
Cdd:PTZ00265 1292 KDLRNLFSIVSQEPMLFNM-SIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNVGPYG-KSLSGGQKQRI 1367
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 265 SIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIhqpSYRI 319
Cdd:PTZ00265 1368 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI---AHRI 1419
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
132-287 |
8.46e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALA--NRIAKGslkgTVALNGE---ALESRLLKVisAYVMQDDLLFPMLTV 206
Cdd:PRK11650 20 IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAglERITSG----EIWIGGRvvnELEPADRDI--AMVFQNYALYPHMSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 207 EETLMFAAEFRlprTLSKSKKSARVQAlidqlglrnAAKTV-IG---DEGHRGVSGGERRRVSIGTDIIHDPILLFLDEP 282
Cdd:PRK11650 94 RENMAYGLKIR---GMPKAEIEERVAE---------AARILeLEpllDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
....*
gi 356576859 283 TSGLD 287
Cdd:PRK11650 162 LSNLD 166
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
132-286 |
9.62e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEALESRLLK-------VIsayVMQDDLLFPML 204
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQASNIRdteragiAI---IHQELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDEGhrgvsGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:PRK13549 98 SVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLG-----LGQQQLVEIAKALNKQARLLILDEPTA 172
|
..
gi 356576859 285 GL 286
Cdd:PRK13549 173 SL 174
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
133-287 |
1.02e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 133 NDISGEARDGEIMAVLGASGSGKST-------LIDALAnriakgslkGTVALNGEALESRLL----KVisAYVMQDDLLF 201
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPASE---------GEAWLFGQPVDAGDIatrrRV--GYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAAE-FRLPRTlsksKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:NF033858 352 GELTVRQNLELHARlFHLPAA----EIAARVAEMLERFDLADVADALPDS-----LPLGIRQRLSLAVAVIHKPELLILD 422
|
....*..
gi 356576859 281 EPTSGLD 287
Cdd:NF033858 423 EPTSGVD 429
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
129-343 |
1.04e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.58 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGslKGTVALNGEALES---RLLKVISAYVMQDdllfPMLT 205
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT--EGEIRLDGRPLSSlshSVLRQGVAMVQQD----PVVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEEtlmFAAEFRLPRTLSKSKKSARVQALidQL-----GLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLD 280
Cdd:PRK10790 428 ADT---FLANVTLGRDISEEQVWQALETV--QLaelarSLPDGLYTPLGEQGNN-LSVGQKQLLALARVLVQTPQILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356576859 281 EPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSiHQPSYRILGllDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK10790 502 EATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLSTIVEA--DTILVLHRGQAVEQGTHQQL 561
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
144-338 |
1.07e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.77 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 144 IMAVLGASGSGKSTLIDAL-----ANRIAKgsLKGTVALNGEALESRLLKVIS-----AYVMQDDLLFPMLTVEETLMFA 213
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFnrlleLNEEAR--VEGEVRLFGRNIYSPDVDPIEvrrevGMVFQYPNPFPHLTIYDNVAIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 214 AEFRlprTLSKSKKS--ARVQALIDQLGLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSA 291
Cdd:PRK14267 110 VKLN---GLVKSKKEldERVEWALKKAALWDEVKDRLNDYPSN-LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 356576859 292 YMVVKVLQRIAQSGSIVIMSiHQPSyRILGLLDRMIFLSRGQTVYSG 338
Cdd:PRK14267 186 AKIEELLFELKKEYTIVLVT-HSPA-QAARVSDYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
132-343 |
1.10e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.06 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNGEALES----RLLKVIS---AYVMQddllFPML 204
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLL-NGLHVPT-QGSVRVDDTLITStsknKDIKQIRkkvGLVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TV-EETLMFAAEFRlPRTLSKSKKSARVQALiDQLGLRNAAKTVIgDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPT 283
Cdd:PRK13649 97 QLfEETVLKDVAFG-PQNFGVSQEEAEALAR-EKLALVGISESLF-EKNPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 284 SGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSyRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
123-316 |
1.50e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 123 SMFTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKgsLKGTVALNGEA-------LESRL----LKVIS 191
Cdd:PRK14258 14 SFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNE--LESEVRVEGRVeffnqniYERRVnlnrLRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 192 AYVMQDDLLFPMlTVEETLMFAAefRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIgdegHRG---VSGGERRRVSIGT 268
Cdd:PRK14258 91 SMVHPKPNLFPM-SVYDNVAYGV--KIVGWRPKLEIDDIVESALKDADLWDEIKHKI----HKSaldLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 356576859 269 DIIHDPILLFLDEPTSGLDSTSAYMVVKVLQ--RIAQSGSIVIMS--IHQPS 316
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVShnLHQVS 215
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
120-317 |
4.87e-08 |
|
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: 54.26 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 120 VGESMFTRTKTL--LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKgsLKGTVALNGEALESRLLKVIS------ 191
Cdd:cd03290 3 VTNGYFSWGSGLatLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT--LEGKVHWSNKNESEPSFEATRsrnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 192 -AYVMQDDLLFPMlTVEETLMFAAEFrlprtlskskKSARVQALIDQLGLRNAAKTV-IGDE---GHRGV--SGGERRRV 264
Cdd:cd03290 81 vAYAAQKPWLLNA-TVEENITFGSPF----------NKQRYKAVTDACSLQPDIDLLpFGDQteiGERGInlSGGQRQRI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 265 SIGTDIIHDPILLFLDEPTSGLDS--TSAYMVVKVLQRIAQSGSIVIMSIHQPSY 317
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIhlSDHLMQEGILKFLQDDKRTLVLVTHKLQY 204
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
129-290 |
5.12e-08 |
|
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: 52.45 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTValngealesrllkvisayvmqddllfpmltvee 208
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDE--GIV--------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 tlmfaaefrlprtlsKSKKSARVqALIDQLglrnaaktvigdeghrgvSGGERRRVSIGTDIIHDPILLFLDEPTSGLDS 288
Cdd:cd03221 58 ---------------TWGSTVKI-GYFEQL------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
..
gi 356576859 289 TS 290
Cdd:cd03221 104 ES 105
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
129-290 |
5.42e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 5.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKGSLKgtvALNGEALESRLLKVisAYVMQDDLLFPMLTVEE 208
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLL-----RIMAGVDK---EFEGEARPAPGIKV--GYLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 TLM---------------FAAEFRLPRTLSKS--KKSARVQALIDQLGLRN----------AAKTVIGDEGHRGVSGGER 261
Cdd:PRK11819 90 NVEegvaevkaaldrfneIYAAYAEPDADFDAlaAEQGELQEIIDAADAWDldsqleiamdALRCPPWDAKVTKLSGGER 169
|
170 180
....*....|....*....|....*....
gi 356576859 262 RRVSIGTDIIHDPILLFLDEPTSGLDSTS 290
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
216-343 |
8.83e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.74 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 216 FRLPRTLSKSKKSARVQA--LIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYM 293
Cdd:NF000106 108 YMIGR*LDLSRKDARARAdeLLERFSLTEAAGRAAAK-----YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNE 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 356576859 294 VVKVLQRIAQSGSIVIMSIhQPSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:NF000106 183 VWDEVRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
132-340 |
9.05e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.99 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTlIDALANRIAKGSlKGTVALNGEALESRLLKVISAY---VMQD-DLLFPMLTVE 207
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKST-IAKLMIGIEKVK-SGEIFYNNQAITDDNFEKLRKHigiVFQNpDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 ETLMFAAEFRLprtLSKSKKSARVQALIDQLGLRNAAKtvigDEGHrGVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:PRK13648 103 YDVAFGLENHA---VPYDEMHRRVSEALKQVDMLERAD----YEPN-ALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 356576859 288 STSAYMVVKVLQRIAQSGSIVIMSI-HQPSYRILGllDRMIFLSRGqTVY-SGSP 340
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISItHDLSEAMEA--DHVIVMNKG-TVYkEGTP 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
129-343 |
9.41e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALESRLLKVIS---AYVMQDDLLFPMLT 205
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH--GHVWLDGEHIQHYASKEVArriGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEEtlmFAAEFRLPR----TLSKSKKSARVQALIDQLGLrnaakTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:PRK10253 98 VQE---LVARGRYPHqplfTRWRKEDEEAVTKAMQATGI-----THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
132-288 |
1.16e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlKGTVALNGEAlesrllkvisAYVMQDDLLFPMlTVEETLM 211
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS-DASVVIRGTV----------AYVPQVSWIFNA-TVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 212 FAAEFRLPRTlsksKKSARVQALIDQLGLRNAAK-TVIGDeghRGV--SGGERRRVSIGTDIIHDPILLFLDEPTSGLDS 288
Cdd:PLN03130 701 FGSPFDPERY----ERAIDVTALQHDLDLLPGGDlTEIGE---RGVniSGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
133-343 |
1.24e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 133 NDISGEARDGEIMAVLGASGSGKSTLIDALAnriakGSLK---GTVALNGEALESRLLKVISAYVM----QDDLLFPMLT 205
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLT-----GFYKptgGTILLRGQHIEGLPGHQIARMGVvrtfQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 206 VEETLMFAAEFRLPRTL------------SKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHD 273
Cdd:PRK11300 97 VIENLLVAQHQQLKTGLfsgllktpafrrAESEALDRAATWLERVGLLEHANRQAGN-----LAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 274 PILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
129-316 |
1.29e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.81 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnriakgSL----KGTVALNGEAlesrllkvisayvmqdDLLF--- 201
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA------GLwpygSGRIARPAGA----------------RVLFlpq 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 ----PMLTVEETLMFAAEfrlPRTLSkskkSARVQALIDQLGLRNAAKTVigDEG---HRGVSGGERRRVSIGTDIIHDP 274
Cdd:COG4178 434 rpylPLGTLREALLYPAT---AEAFS----DAELREALEAVGLGHLAERL--DEEadwDQVLSLGEQQRLAFARLLLHKP 504
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 356576859 275 ILLFLDEPTSGLDSTSAYMVVKVLQRiAQSGSIVImSI-HQPS 316
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLRE-ELPGTTVI-SVgHRST 545
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
129-370 |
2.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.17 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALaNRIAKGSlKGTVALNG--EALESRLLKVISA--YVMQ--DDLLFP 202
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHM-NALLIPS-EGKVYVDGldTSDEENLWDIRNKagMVFQnpDNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLtVEETLMFAaefrlPRTLSKSKKSARVQalidqlgLRNAAKTVIGDEGHRG----VSGGERRRVSIGTDIIHDPILLF 278
Cdd:PRK13633 101 TI-VEEDVAFG-----PENLGIPPEEIRER-------VDESLKKVGMYEYRRHaphlLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRI-AQSGSIVIMSIHQPSYRILGllDRMIFLSRGQTVYSGSPSQLplyFSE------FG 351
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEA--DRIIVMDSGKVVMEGTPKEI---FKEvemmkkIG 242
|
250
....*....|....*....
gi 356576859 352 HPIPETdnrTEFALDLIRE 370
Cdd:PRK13633 243 LDVPQV---TELAYELKKE 258
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
134-341 |
3.40e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 134 DISGEARDGEIMAVLGASGSGKSTLIDALAN-RIAKGslkGTVALNGEALES-----RLLKVIsAYVMQDDL---LF--- 201
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGlRPARG---GRIMLNGKEINAlstaqRLARGL-VYLPEDRQssgLYlda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAaefRLPRTLSKSKKSARVQALIDQLGLRNAAktviGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:PRK15439 357 PLAWNVCALTHN---RRGFWIKPARENAVLERYRRALNIKFNH----AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMsIHQPSYRILGLLDRMIFLSRGQtvYSGSPS 341
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVLF-ISSDLEEIEQMADRVLVMHQGE--ISGALT 486
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
132-287 |
4.19e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLIdAL---ANRIAKGSLKgtvALNGEALESRLLKVIS---AYvMQDDL---LFP 202
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLL-SLiagARKIQQGRVE---VLGGDMADARHRRAVCpriAY-MPQGLgknLYP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MLTVEETLMFAAefRLpRTLSKSKKSARVQALIDQLGL-----RNAAKtvigdeghrgVSGGERRRVSIGTDIIHDPILL 277
Cdd:NF033858 92 TLSVFENLDFFG--RL-FGQDAAERRRRIDELLRATGLapfadRPAGK----------LSGGMKQKLGLCCALIHDPDLL 158
|
170
....*....|
gi 356576859 278 FLDEPTSGLD 287
Cdd:NF033858 159 ILDEPTTGVD 168
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
128-305 |
5.49e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTL-LNDIsgEARDGEIMAVLGASGSGKSTLIDALANRIA--KG----SLKGTVALNGEALEsrllKVISAyVMQD--- 197
Cdd:PRK10938 16 TKTLqLPSL--TLNAGDSWAFVGANGSGKSALARALAGELPllSGerqsQFSHITRLSFEQLQ----KLVSD-EWQRnnt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 198 DLLFPmlTVEETLMFAAEFrlprTLSKSKKSARVQALIDQLGLrnaakTVIGDEGHRGVSGGERRRVSIGTDIIHDPILL 277
Cdd:PRK10938 89 DMLSP--GEDDTGRTTAEI----IQDEVKDPARCEQLAQQFGI-----TALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180
....*....|....*....|....*...
gi 356576859 278 FLDEPTSGLDSTSAYMVVKVLQRIAQSG 305
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQSG 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
140-341 |
6.05e-07 |
|
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: 51.60 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 140 RDGEIMAVLGASGSGKSTLIDALAnriakGSLKGTVALNGEALESRllKVISAY---VMQDdlLFPMLtVEETLMFAAEF 216
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILA-----GKLKPNLGKFDDPPDWD--EILDEFrgsELQN--YFTKL-LEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 217 ----RLPRT--------LSKSKKSARVQALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:cd03236 94 qyvdLIPKAvkgkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQ-----LSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSIVIMSIHQpsyriLGLLDrmiFLSRGQTVYSGSPS 341
Cdd:cd03236 169 YLDIKQRLNAARLIRELAEDDNYVLVVEHD-----LAVLD---YLSDYIHCLYGEPG 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
83-338 |
6.83e-07 |
|
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: 50.99 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 83 LSFSNLT--YSIKSRRKMSLssifpRRSNRLGAVAEAptvgesmftRTKTLLNDISGEARDGEIMAVLGASGSGKSTLID 160
Cdd:cd03220 1 IELENVSksYPTYKGGSSSL-----KKLGILGRKGEV---------GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 161 ALANRIAKGSlkGTVALNGealesrllKVISayvmqddLLF------PMLTVEETLMFAAEFrlpRTLSKSKKSARVQAL 234
Cdd:cd03220 67 LLAGIYPPDS--GTVTVRG--------RVSS-------LLGlgggfnPELTGRENIYLNGRL---LGLSRKEIDEKIDEI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 235 IDQLGLrnaaktviGDEGHRGV---SGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMS 311
Cdd:cd03220 127 IEFSEL--------GDFIDLPVktySSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILV 198
|
250 260
....*....|....*....|....*..
gi 356576859 312 IHQPSYrILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03220 199 SHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
132-338 |
7.11e-07 |
|
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: 50.01 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTLidalanriakgslkgtvalngealesrllkvisayvmqddllfpmltVEETLM 211
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL-----------------------------------------------VNEGLY 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 212 FAAEFRLPRTLSKSKKSARVqaLIDQLglRNAAKTVIG----DEGHRGVSGGERRRVSIGTDIIHDP--ILLFLDEPTSG 285
Cdd:cd03238 44 ASGKARLISFLPKFSRNKLI--FIDQL--QFLIDVGLGyltlGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 356576859 286 LDSTSAYMVVKVLQRIAQSGSIVIMSIHQPsyRILGLLDRMIFLSRGQTVYSG 338
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFGPGSGKSGG 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
240-316 |
7.21e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 7.21e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356576859 240 LRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRI-AQSGSIVIMSIHQPS 316
Cdd:PTZ00265 565 LPDKYETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLS 641
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
127-343 |
8.55e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 127 RTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAN--RIAKGSlkgtVALNGEAL------ESRLLKVisAYVMQDD 198
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGlrPPASGS----IRLDGEDItglsprERRRLGV--AYIPEDR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 199 L---LFPMLTVEETLMF----AAEFRLPRTLSKSKKSARVQALIDQLGLRNA-AKTVIgdeghRGVSGGERRRVSIGTDI 270
Cdd:COG3845 343 LgrgLVPDMSVAENLILgryrRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPgPDTPA-----RSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 271 IHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSihqpSY---RILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI----SEdldEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
82-340 |
1.54e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.08 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 82 VLSFSNLT--YSIKSRRKMSLSSIFPRRSNRlgavaeaptvgesmFTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLI 159
Cdd:COG1134 4 MIEVENVSksYRLYHEPSRSLKELLLRRRRT--------------RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 160 DALAnriakGSLK---GTVALNGEalesrllkvISAyvmqddLL-----F-PMLTVEETLMFAAefrlpRTLSKSKKSar 230
Cdd:COG1134 70 KLIA-----GILEptsGRVEVNGR---------VSA------LLelgagFhPELTGRENIYLNG-----RLLGLSRKE-- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 231 VQALIDQLglrnAAKTVIGDEGHRGV---SGGERRR----VSIGTDiiHDpILLfLDEptsgldstsAYMVV------KV 297
Cdd:COG1134 123 IDEKFDEI----VEFAELGDFIDQPVktySSGMRARlafaVATAVD--PD-ILL-VDE---------VLAVGdaafqkKC 185
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 356576859 298 LQRIAQ---SGSIVIMSIHQPSYrILGLLDRMIFLSRGQTVYSGSP 340
Cdd:COG1134 186 LARIRElreSGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDGDP 230
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
128-343 |
2.08e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.25 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTLLNDISGEARDGEIMAVLGASGSGKSTLIdALANR---IAKGSLK----GTVALNGEALESRLlkvisAYVMQDDLL 200
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLL-SLIQRhfdVSEGDIRfhdiPLTKLQLDSWRSRL-----AVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FpmltvEETLmfAAEFRLPR---TLSKSKKSARVQALIDQ-LGLRNAAKTVIGDeghRGV--SGGERRRVSIGTDIIHDP 274
Cdd:PRK10789 401 F-----SDTV--ANNIALGRpdaTQQEIEHVARLASVHDDiLRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 275 ILLFLDEPTSGLDSTSAYMVVKVLQRIAQsGSIVIMSIHQPSyrILGLLDRMIFLSRGQTVYSGSPSQL 343
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLS--ALTEASEILVMQHGHIAQRGNHDQL 536
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
128-291 |
2.30e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 128 TKTL-----LNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEALESRLLK-------VIsayVM 195
Cdd:NF040905 8 TKTFpgvkaLDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILFDGEVCRFKDIRdsealgiVI---IH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 196 QDDLLFPMLTVEETLMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDeghRGVsgGERRRVSIGTDIIHDPI 275
Cdd:NF040905 85 QELALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELLAKVGLDESPDTLVTD---IGV--GKQQLVEIAKALSKDVK 159
|
170
....*....|....*..
gi 356576859 276 LLFLDEPTSGL-DSTSA 291
Cdd:NF040905 160 LLILDEPTAALnEEDSA 176
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
104-338 |
5.71e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 104 FPRRSNRLGAVaeaptvgesmfTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAkgSLKGTVALNGEALE 183
Cdd:PRK10261 323 FPLRSGLLNRV-----------TREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE--SQGGEIIFNGQRID 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 184 S------RLLKVISAYVMQDDL--LFPMLTVEETLMfaAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGDEghrg 255
Cdd:PRK10261 390 TlspgklQALRRDIQFIFQDPYasLDPRQTVGDSIM--EPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE---- 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 256 VSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTV 335
Cdd:PRK10261 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
...
gi 356576859 336 YSG 338
Cdd:PRK10261 544 EIG 546
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
129-287 |
9.87e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAkgSLKGTVALngealeSRLLKVisAYVMQDDLLFpmLTVEE 208
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELA--PVSGEIGL------AKGIKL--GYFAQHQLEF--LRADE 392
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356576859 209 TLMfaaefrlpRTLSKSKKSARVQALIDQLGLRNAAKTVIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLD 287
Cdd:PRK10636 393 SPL--------QHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRR-FSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
140-324 |
1.32e-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: 48.63 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 140 RDGEIMAVLGASGSGKSTLIDALANRI--------AKGS-------LKGTVALNG-EALESRLLKVI--SAYVmqdDLLf 201
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELkpnlgdydEEPSwdevlkrFRGTELQDYfKKLANGEIKVAhkPQYV---DLI- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PML---TVEETLMFAAEfrlprtlsksKKSARvqALIDQLGLRNAAKTVIGDeghrgVSGGERRRVSIGTDIIHDPILLF 278
Cdd:COG1245 173 PKVfkgTVRELLEKVDE----------RGKLD--ELAEKLGLENILDRDISE-----LSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQpsyriLGLLD 324
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHD-----LAILD 276
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
313-446 |
1.71e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 47.98 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 313 HQPSYRILGLLDRMIFLSR-GQTVYSGSPSQLPLYFSEFGHPIPETDNRTEFALDLireLEGspggtksLVEFNKSWQSM 391
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDI---LEG-------IVKPSTSSGVD 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 392 TKHHQEKEEERNGLS-----LKEAISASISRGklVSGASNTNPNPSSMVPTFANQFWVEM 446
Cdd:pfam19055 71 YKQLPVRWMLHNGYPvppdmLQNADGIAASSG--ENSSNGTNPGVGSEEQSFAGELWQDV 128
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
257-316 |
1.84e-05 |
|
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: 45.61 E-value: 1.84e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 257 SGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAymvVKVLQRIAQSGSIVIMSIHQPS 316
Cdd:cd03223 93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE---DRLYQLLKELGITVISVGHRPS 149
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
131-333 |
1.88e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 131 LLNDISGEARDGEIMAVLGASGSGKSTLIDAL--ANRIAkgslKGTVALNGEALESRLLK-VISAYVM------QDDLLF 201
Cdd:PRK11288 268 LREPISFSVRAGEIVGLFGLVGAGRSELMKLLygATRRT----AGQVYLDGKPIDIRSPRdAIRAGIMlcpedrKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAAE--FRLPRTLSKSKKSAR-VQALIDQLglrnAAKTVIGDEGHRGVSGGERRRVSIGTDIIHDPILLF 278
Cdd:PRK11288 344 PVHSVADNINISARrhHLRAGCLINNRWEAEnADRFIRSL----NIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQSG-SIVIMSIHQPsyRILGLLDRMIFLSRGQ 333
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVIYELAAQGvAVLFVSSDLP--EVLGVADRIVVMREGR 473
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
259-343 |
2.67e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 259 GERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPSYRILGLLDRMIFLSRGQTVYSG 338
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
....*
gi 356576859 339 SPSQL 343
Cdd:PRK15093 242 PSKEL 246
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
140-309 |
2.75e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 140 RDGEIMAVLGASGSGKSTLIDALANRI--------AKGS-------LKGTVALNG-EALESRLLKVI--SAYVmqdDLLf 201
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGELipnlgdyeEEPSwdevlkrFRGTELQNYfKKLYNGEIKVVhkPQYV---DLI- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PML---TVEETLMfaaefrlprtlsKSKKSARVQALIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLF 278
Cdd:PRK13409 173 PKVfkgKVRELLK------------KVDERGKLDEVVERLGLEN-----ILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|.
gi 356576859 279 LDEPTSGLDSTSAYMVVKVLQRIAQSGSIVI 309
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAEGKYVLV 266
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
129-329 |
3.97e-05 |
|
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: 47.21 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALAnRIAkgSLKGTVALNGEALESRLLKvisayvmQDDLLFPMLTvEE 208
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLL--STEGEIQIDGVSWNSVTLQ-------TWRKAFGVIP-QK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 209 TLMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKT-------VIGDEGHRgVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:TIGR01271 1301 VFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQfpdkldfVLVDGGYV-LSNGHKQLMCLARSILSKAKILLLDE 1379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 356576859 282 PTSGLDSTSAYMVVKVLQRiAQSGSIVIMSIHqpsyRILGLLDRMIFL 329
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEH----RVEALLECQQFL 1422
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
130-288 |
9.22e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.48 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIdalanRIAKGSLK---GTVALNGE-----ALESRLLKVisayVMQDDLLF 201
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVL-----RLVAGLEKpteGQIFIDGEdvthrSIQQRDICM----VFQSYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 202 PMLTVEETLMFAAEFRlprTLSKSKKSARVQ---ALIDQLGLrnaaktviGDEGHRGVSGGERRRVSIGTDIIHDPILLF 278
Cdd:PRK11432 91 PHMSLGENVGYGLKML---GVPKEERKQRVKealELVDLAGF--------EDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170
....*....|
gi 356576859 279 LDEPTSGLDS 288
Cdd:PRK11432 160 FDEPLSNLDA 169
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
130-329 |
1.01e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.85 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 130 TLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIakgSLKGTVALNGEALESRLLKvisayvmQDDLLFPMLTvEET 209
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL---NTEGDIQIDGVSWNSVPLQ-------KWRKAFGVIP-QKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 210 LMFAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIGD------EGHRGVSGGERRRVSIGTDIIHDPILLFLDEPT 283
Cdd:cd03289 87 FIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQldfvlvDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 356576859 284 SGLDSTSAYMVVKVLQRiAQSGSIVIMSIHqpsyRILGLLDRMIFL 329
Cdd:cd03289 167 AHLDPITYQVIRKTLKQ-AFADCTVILSEH----RIEAMLECQRFL 207
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
141-335 |
1.19e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 141 DGEIMAVLGASGSGKSTLIDALAN-------------------------RIAKGSLKGTVAlNGEALESRLLK---VISA 192
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarlqqdppRNVEGTVYDFVA-EGIEEQAEYLKryhDISH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 193 YVMQD---DLLFPMLTVEETLMFAAEFRLprtlskskkSARVQALIDQLGLRnaaktviGDEGHRGVSGGERRRVSIGTD 269
Cdd:PRK11147 107 LVETDpseKNLNELAKLQEQLDHHNLWQL---------ENRINEVLAQLGLD-------PDAALSSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356576859 270 IIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIaqSGSIVIMSiHQPSYrILGLLDRMIFLSRGQTV 335
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QGSIIFIS-HDRSF-IRNMATRIVDLDRGKLV 232
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
129-338 |
1.54e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSLKGTVALNGEAL-----ESRLLK-VISAYvmqddlLFP 202
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLlelspEDRAGEgIFMAF------QYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 203 MltveETLMFAAEFRLPRTLSKSKKSaRVQALID----------QLGLRNAAKTVIGDEGHRGVSGGERRRVSIGTDIIH 272
Cdd:PRK09580 88 V----EIPGVSNQFFLQTALNAVRSY-RGQEPLDrfdfqdlmeeKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 273 DPILLFLDEPTSGLDSTSAYMV---VKVLQRiaQSGSIVIMSIHQpsyRILGLL--DRMIFLSRGQTVYSG 338
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVadgVNSLRD--GKRSFIIVTHYQ---RILDYIkpDYVHVLYQGRIVKSG 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
257-335 |
2.58e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 257 SGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIM-SIHQPsyRILGLLDRMIFLSRGQTV 335
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIViSSELP--ELLGMCDRIYVMNEGRIT 483
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
134-339 |
3.49e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 134 DISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALE-------SRLLKVIsayvMQD--DLLFPML 204
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTS--GELLIDDHPLHfgdysyrSQRIRMI----FQDpsTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAaeFRLPRTLSKSKKSARVQALIDQLGLRNaaktvigDEGH---RGVSGGERRRVSIGTDIIHDPILLFLDE 281
Cdd:PRK15112 105 RISQILDFP--LRLNTDLEPEQREKQIIETLRQVGLLP-------DHASyypHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356576859 282 PTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPsyriLGLL----DRMIFLSRGQTVYSGS 339
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGISYIYVTQH----LGMMkhisDQVLVMHQGEVVERGS 233
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
132-181 |
7.04e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 7.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 356576859 132 LNDISGEARDGEIMAVLGASGSGKSTlidaLANRIAKGSL--KGTVALNGEA 181
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKST----LSNLIAGVTMpnKGTVDIKGSA 87
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
142-328 |
7.57e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.43 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 142 GEIMAVLGASGSGKSTLIDALANRIAKGSlKGTVALNGEALESRLLkvisayvmqddllfpmltveetlmfaaeFRLPRT 221
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPG-GGVIYIDGEDILEEVL----------------------------DQLLLI 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 222 LSKSKKSARVQALIDQLGLRNAAKtvigdeghrgvsggerrrvsigtdiiHDPILLFLDEPTSGLDSTSAYMVVK----- 296
Cdd:smart00382 53 IVGGKKASGSGELRLRLALALARK--------------------------LKPDVLILDEITSLLDAEQEALLLLleelr 106
|
170 180 190
....*....|....*....|....*....|..
gi 356576859 297 VLQRIAQSGSIVIMSIHQPSYRILGLLDRMIF 328
Cdd:smart00382 107 LLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
137-341 |
8.44e-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: 41.02 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 137 GEARDGEIMAVLGASGSGKSTLIDALAnriakGSLKGTvalngealesrllkvisayvmQDDLLFPMLTVeetlmfaaef 216
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILA-----GQLIPN---------------------GDNDEWDGITP---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 217 rlprtlskSKKSARVQalidqlglrnaaktvigdeghrgVSGGERRRVSIGTDIIHDPILLFLDEPTSGLDSTSAYMVVK 296
Cdd:cd03222 64 --------VYKPQYID-----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 356576859 297 VLQRIAQSGSIVIMSIHQPSYRILGLLDRMIflsrgqtVYSGSPS 341
Cdd:cd03222 113 AIRRLSEEGKKTALVVEHDLAVLDYLSDRIH-------VFEGEPG 150
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
139-253 |
1.28e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 41.31 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 139 ARDGE-IMAVLGASGSGKSTLIDALANRIAKgslkgtvalngealesrllKVISAYVmqddlLFPMLTVEETL-MFAAEF 216
Cdd:COG3267 39 LAQGGgFVVLTGEVGTGKTTLLRRLLERLPD-------------------DVKVAYI-----PNPQLSPAELLrAIADEL 94
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 356576859 217 RLPrtLSKSKKSARVQALIDQLGLRNAAKT---VIGDEGH 253
Cdd:COG3267 95 GLE--PKGASKADLLRQLQEFLLELAAAGRrvvLIIDEAQ 132
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
133-315 |
1.67e-03 |
|
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: 39.65 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 133 NDISGEarDGEIMAVLGASGSGKSTLIDALAnriakgslkgtVALNGEALESRLLKV-----ISAYVmqddllfpmltve 207
Cdd:cd03227 14 NDVTFG--EGSLTIITGPNGSGKSTILDAIG-----------LALGGAQSATRRRSGvkagcIVAAV------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 208 etlmfAAEFRLprtlskskksarvqaLIDQLglrnaaktvigdeghrgvSGGERRRVSIGTDIIH----DPILLFLDEPT 283
Cdd:cd03227 68 -----SAELIF---------------TRLQL------------------SGGEKELSALALILALaslkPRPLYILDEID 109
|
170 180 190
....*....|....*....|....*....|..
gi 356576859 284 SGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQP 315
Cdd:cd03227 110 RGLDPRDGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
142-164 |
1.99e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 1.99e-03
|
| PRK06547 |
PRK06547 |
hypothetical protein; Provisional |
130-165 |
2.35e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235825 Cd Length: 172 Bit Score: 39.73 E-value: 2.35e-03
10 20 30
....*....|....*....|....*....|....*...
gi 356576859 130 TLLNDISGEARDGEIMAVL--GASGSGKSTLIDALANR 165
Cdd:PRK06547 1 MLVALIAARLCGGGMITVLidGRSGSGKTTLAGALAAR 38
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
142-179 |
2.75e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 2.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 356576859 142 GEIMAVLGASGSGKSTLIDALA--NRIAKGSLKGTVALNG 179
Cdd:COG4637 21 GPLTVLIGANGSGKSNLLDALRflSDAARGGLQDALARRG 60
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-163 |
3.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 3.12e-03
10 20
....*....|....*....|...
gi 356576859 141 DGEIMAVLGASGSGKSTLIDALA 163
Cdd:COG4913 23 DGRGTLLTGDNGSGKSTLLDAIQ 45
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
256-342 |
3.54e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 256 VSGGERRRVSI----GTDIIHdpILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPsyRILGLLDRMIFLSR 331
Cdd:PRK00635 477 LSGGEQERTALakhlGAELIG--ITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDE--QMISLADRIIDIGP 552
|
90
....*....|....*..
gi 356576859 332 ------GQTVYSGSPSQ 342
Cdd:PRK00635 553 gagifgGEVLFNGSPRE 569
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
125-316 |
6.73e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 125 FTRTKTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIAKGSlkGTVALNGEALeSRLLKVISAYVMQDDLLFPML 204
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSS--GNIYYKNCNI-NNIAKPYCTYIGHNLGLKLEM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 205 TVEETLMFAAEFRlprtlsksKKSARVQALIDQLGLRNaaktvIGDEGHRGVSGGERRRVSIGTDIIHDPILLFLDEPTS 284
Cdd:PRK13541 86 TVFENLKFWSEIY--------NSAETLYAAIHYFKLHD-----LLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180 190
....*....|....*....|....*....|..
gi 356576859 285 GLDSTSAYMVVKVLQRIAQSGSIVIMSIHQPS 316
Cdd:PRK13541 153 NLSKENRDLLNNLIVMKANSGGIVLLSSHLES 184
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
129-343 |
8.10e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 38.74 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 129 KTLLNDISGEARDGEIMAVLGASGSGKSTLIDALANRIakGSLKGTVALNG--------EALESRLlkvisAYVMQDDLL 200
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV--DIFDGKIVIDGidisklplHTLRSRL-----SIILQDPIL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356576859 201 FpmltveetlmfAAEFRLPRTLSKSKKSARVQALIDQLGLRNAAKTVIG------DEGHRGVSGGERRRVSIGTDIIHDP 274
Cdd:cd03288 107 F-----------SGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGgldavvTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356576859 275 ILLFLDEPTSGLDSTSAYMVVKVLQRIAQSGSIVIMsihqpSYRILGLL--DRMIFLSRGQTVYSGSPSQL 343
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTI-----AHRVSTILdaDLVLVLSRGILVECDTPENL 241
|
|
| |
