|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
59-698 |
5.72e-168 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 495.34 E-value: 5.72e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 59 NRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGY--KTSSIEGSVTMNGAERNLSAFRKLSAYIMQDNQLHG 136
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRspKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 NLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMT------RNLSGGQKKRLSIALELVSNPPIMFFDE 210
Cdd:TIGR00955 113 TLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 211 PTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQLYTLADGQCVYQGSTKQLVPFLSTLNLECPSYHNPA 290
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 291 SYVIEVSCGEHGDhtrklvdaiDNGKRDVRssadyaglkarndlvkvqnlKAILDKNDASSVSGrkyednltlnngllng 370
Cdd:TIGR00955 273 DFYVQVLAVIPGS---------ENESRERI--------------------EKICDSFAVSDIGR---------------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 371 mvnDIVKEGNVSSAlvttnERGDAMIDVEKSVNCttallteeitspeRYPTSQFHQFWVVLKRTLLFSYRDWTLMYLRLF 450
Cdd:TIGR00955 308 ---DMLVNTNLWSG-----KAGGLVKDSENMEGI-------------GYNASWWTQFYALLKRSWLSVLRDPLLLKVRLI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 451 AHLLVGFLIGALYYDIGNDGAKVLSNLGFLFFNMLFLMYTSMTITILSFPLEMPVLLKENFNRWYSLKSYYLAISVADLP 530
Cdd:TIGR00955 367 QTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELP 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 531 FQAIFCVIYVSIVYYFTSQPWELFRFSMFLSACLLISFVAQSVGLVVGAAM-NVQNGVFLAPVMSVPFLLFSGFFVSFDA 609
Cdd:TIGR00955 447 LFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFsSTSMALTVGPPFVIPFLLFGGFFINSDS 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 610 IPVYLRWITYLSYIRYGFEGTALATYGyGREKLRCFQT----YCHFKSPItTLEELDMVNANFTLDIVALIVIFVVLRIS 685
Cdd:TIGR00955 527 IPVYFKWLSYLSWFRYGNEGLLINQWS-DVDNIECTSAnttgPCPSSGEV-ILETLSFRNADLYLDLIGLVILIFFFRLL 604
|
650
....*....|...
gi 24580555 686 AYLFLRWKLKTVR 698
Cdd:TIGR00955 605 AYFALRIRIRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
43-267 |
5.13e-85 |
|
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: 265.95 E-value: 5.13e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 43 AVDLAFHNLTYRVKEGNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTS-SIEGSVTMNGAERNLSAF 121
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 122 RKLSAYIMQDNQLHGNLTVQEAMTVATNLklskkfskpekhsmiddilltlslsehrytmtRNLSGGQKKRLSIALELVS 201
Cdd:cd03213 81 RKIIGYVPQDDILHPTLTVRETLMFAAKL--------------------------------RGLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 202 NPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQLYTLADGQCVYQG 267
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
44-691 |
1.06e-69 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 240.17 E-value: 1.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 44 VDLAFHNLTYRVKEGNRSN-----------------------AKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG- 99
Cdd:PLN03211 38 ITLKFMDVCYRVKFENMKNkgsnikrilghkpkisdetrqiqERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 100 YKTSSIEGSVTMNGAERNLSAFRKlSAYIMQDNQLHGNLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRY 179
Cdd:PLN03211 118 IQGNNFTGTILANNRKPTKQILKR-TGFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCEN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 180 TMT-----RNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQ 254
Cdd:PLN03211 197 TIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 255 LYTLADGQCVYQGSTKQLVPFLSTLNLECPSYHNPASYVIEVScgehgDHTRKLVDAIDNGKRDVRSSAdyagLKARNDL 334
Cdd:PLN03211 277 VLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLA-----NGVCQTDGVSEREKPNVKQSL----VASYNTL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 335 VKVQnlkaildkndassvsgrkyednltlnngllngmvndiVKEGNVSSALVTTNERGDAMIDVEKSVNCTTALLteeit 414
Cdd:PLN03211 348 LAPK-------------------------------------VKAAIEMSHFPQANARFVGSASTKEHRSSDRISI----- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 415 sperypTSQFHQFWVVLKRtLLFSYRDWTLMYLRLFAHLLVGFLIGALYYDigNDGAKVLSNLGFLFFNMLFLMYTSMTI 494
Cdd:PLN03211 386 ------STWFNQFSILLQR-SLKERKHESFNTLRVFQVIAAALLAGLMWWH--SDFRDVQDRLGLLFFISIFWGVFPSFN 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 495 TILSFPLEMPVLLKENFNRWYSLKSYYLAISVADLPFQAIFCVIYVSIVYYFTSQPWELFRFSMFLSACLLISFVAQSVG 574
Cdd:PLN03211 457 SVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLG 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 575 LVVGAA-MNVQNGVFLAPVMSVPFLLFSGFFVsfDAIPVYLRWITYLSYIRYGFEGTALATYGYGREKLRCFQtyCHFKS 653
Cdd:PLN03211 537 LALGAAiMDAKKASTIVTVTMLAFVLTGGFYV--HKLPSCMAWIKYISTTFYSYRLLINVQYGEGKRISSLLG--CSLPH 612
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 24580555 654 PITT-----LEELDMVNANFTLDIVALIVIFVVLRISAYLFLR 691
Cdd:PLN03211 613 GSDRasckfVEEDVAGQISPATSVSVLIFMFVGYRLLAYLALR 655
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
59-267 |
2.99e-63 |
|
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: 209.82 E-value: 2.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 59 NRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG--YKTSSIEGSVTMNGAERNLSAFRKLSAYIMQDNQLHG 136
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrvEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 NLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLT-LSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGL 215
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24580555 216 DSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQLYTLADGQCVYQG 267
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
46-267 |
1.19e-61 |
|
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: 204.40 E-value: 1.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNRSnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSS-IEGSVTMNGAERNLSaFRKL 124
Cdd:cd03232 4 LTWKNLNYTVPVKGGK--RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLDKN-FQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 125 SAYIMQDNQLHGNLTVQEAMTVATNLklskkfskpekhsmiddilltlslsehrytmtRNLSGGQKKRLSIALELVSNPP 204
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRFSALL--------------------------------RGLSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 205 IMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQLYTLA-DGQCVYQG 267
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKrGGKTVYFG 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
48-633 |
1.24e-59 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 218.05 E-value: 1.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FH--NLTYRVKEgnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSI--EGSVTMNGAERNlSAFRK 123
Cdd:TIGR00956 760 FHwrNLTYEVKI--KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSFQR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQdNQLH-GNLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMT----RNLSGGQKKRLSIALE 198
Cdd:TIGR00956 837 SIGYVQQ-QDLHlPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVE 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 199 LVSNPP-IMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQLYTLADG-QCVY-----QGSTKQ 271
Cdd:TIGR00956 916 LVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYfgdlgENSHTI 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 272 LVPFLSTLNLECPSYHNPASYVIEVSCGEHGDHTrklvdaidngKRDV----RSSADYAGLKArndlvKVQNLKAILDKn 347
Cdd:TIGR00956 996 INYFEKHGAPKCPEDANPAEWMLEVIGAAPGAHA----------NQDYhevwRNSSEYQAVKN-----ELDRLEAELSK- 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 348 dassvSGRKYednltlnngllngmvndivkegnvssalvttnergdamidveksvncttallteEITSPERYPTSQFHQF 427
Cdd:TIGR00956 1060 -----AEDDN------------------------------------------------------DPDALSKYAASLWYQF 1080
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 428 WVVLKRTLLFSYRDWTLMYLRLFAHLLVGFLIGALYYDIGNdGAKVLSNLGFLFFNMLFLMYTSMTITILSF-PLEMPVL 506
Cdd:TIGR00956 1081 KLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGT-SLQGLQNQMFAVFMATVLFNPLIQQYLPPFvAQRDLYE 1159
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 507 LKENFNRWYSLKSYYLAISVADLPFQAI-----FCVIYVSIVYYFTSQPWELF--RFSMFLSACLLISFVAQSVG-LVVG 578
Cdd:TIGR00956 1160 VRERPSRTFSWLAFIAAQITVEIPYNLVagtifFFIWYYPVGFYWNASKTGQVheRGVLFWLLSTMFFLYFSTLGqMVIS 1239
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 579 AAMNVQNGVFLAPVMSVPFLLFSGFFVSFDAIP---VYLRWITYLSYIRYGFEGTALA 633
Cdd:TIGR00956 1240 FNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPgfwIFMYRCSPFTYLVQALLSTGLA 1297
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-626 |
2.36e-49 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 187.36 E-value: 2.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 30 AQPKTLQHLPKRPaVDLAFHNLTYRV-------KEGNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKT 102
Cdd:PLN03140 853 VAPKRGMVLPFTP-LAMSFDDVNYFVdmpaemkEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKT 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 103 SS-IEGSVTMNGAERNLSAFRKLSAYIMQdNQLHG-NLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYT 180
Cdd:PLN03140 932 GGyIEGDIRISGFPKKQETFARISGYCEQ-NDIHSpQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDA 1010
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 181 MT-----RNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQL 255
Cdd:PLN03140 1011 IVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDEL 1090
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 256 YTLA-DGQCVYQG----STKQLVPFLSTLN--LECPSYHNPASYVIEVScgehgdhtrklvdaidNGKRDVRSSADYAgl 328
Cdd:PLN03140 1091 LLMKrGGQVIYSGplgrNSHKIIEYFEAIPgvPKIKEKYNPATWMLEVS----------------SLAAEVKLGIDFA-- 1152
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 329 karndlvkvqnlkaildkndassvsgrkyednltlnngllngmvndivkEGNVSSALVTTNErgdamidveksvncttAL 408
Cdd:PLN03140 1153 -------------------------------------------------EHYKSSSLYQRNK----------------AL 1167
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 409 LTEEITSP----ERYPTSQFHQ-FWVVLKRTLlfsYRDWTLMY-------LRLFAHLLVGFLIGALYYDIGN--DGAKVL 474
Cdd:PLN03140 1168 VKELSTPPpgasDLYFATQYSQsTWGQFKSCL---WKQWWTYWrspdynlVRFFFTLAAALMVGTIFWKVGTkrSNANDL 1244
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 475 SN-LGFLFFNMLFLMYTSMTITILSFPLEMPVLLKENFNRWYSLKSYYLAISVADLPFQAIFCVIYVSIVYYFTSQPWEL 553
Cdd:PLN03140 1245 TMvIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTA 1324
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 554 FRFSMFlsacLLISFVA----QSVGLV-VGAAMNVQNGVFLAPVMSVPFLLFSGFFVSFDAIP---VYLRWITYLSYIRY 625
Cdd:PLN03140 1325 AKFFWF----YFISFFSflyfTYYGMMtVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPkwwVWYYWICPVAWTVY 1400
|
.
gi 24580555 626 G 626
Cdd:PLN03140 1401 G 1401
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
430-629 |
7.55e-49 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 170.15 E-value: 7.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 430 VLKRTLLFSYRDWTLMYLRLFAHLLVGFLIGALYYDIGNDGAkVLSNLGFLFFNMLFLMYTSMTITILSFPLEMPVLLKE 509
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 510 NFNRWYSLKSYYLAISVADLPFQAIFCVIYVSIVYYFTSQPWELFRFSMFLSACLLISFVAQSVGLVVGA-AMNVQNGVF 588
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISAlAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24580555 589 LAPVMSVPFLLFSGFFVSFDAIPVYLRWITYLSYIRYGFEG 629
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEA 200
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
59-628 |
1.59e-47 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 181.85 E-value: 1.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 59 NRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTS----SIEGSVTMNGAERN--LSAFRKLSAYIMQdN 132
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS-NTDgfhiGVEGVITYDGITPEeiKKHYRGDVVYNAE-T 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 133 QLH-GNLTVQEAMTVATNLKLS----KKFSKPE-KHSMIDDILLTLSLSEHRYT-----MTRNLSGGQKKRLSIALELVS 201
Cdd:TIGR00956 147 DVHfPHLTVGETLDFAARCKTPqnrpDGVSREEyAKHIADVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 202 NPPIMFFDEPTSGLDSSTCFQCIHLLKMLAA-GGRTVICTIHQPSARLFEMFDQLYTLADGQCVYQGSTKQLVPFLSTLN 280
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMG 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 281 LECPSYHNPASYVIEV-SCGEH---GDHTRKLVDAIDNGKRDVRSSADYAGLKARNDlvkvqnlkaILDKNDASSVSGRK 356
Cdd:TIGR00956 307 FKCPDRQTTADFLTSLtSPAERqikPGYEKKVPRTPQEFETYWRNSPEYAQLMKEID---------EYLDRCSESDTKEA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 357 YednltlnngllngmvndivKEGNVSsalvttnergdamidvEKSVNCttallteEITSPerYPTSQFHQFWVVLKRTLL 436
Cdd:TIGR00956 378 Y-------------------RESHVA----------------KQSKRT-------RPSSP--YTVSFSMQVKYCLARNFL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 437 FSYRDWTLMYLRLFAHLLVGFLIGALYYDIGNDGAKVLSNLGFLFFNMLFLMYTSMtITILSFPLEMPVLLKenfNRWYS 516
Cdd:TIGR00956 414 RMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNAFSSL-LEIASMYEARPIVEK---HRKYA 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 517 L---KSYYLAISVADLPFQAIFCVIYVSIVYYFTSQPWELFRFSMFLSACLLISFVAQSVGLVVGAAM-NVQNGVFLAPV 592
Cdd:TIGR00956 490 LyhpSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTkTLSEAMTPAAI 569
|
570 580 590
....*....|....*....|....*....|....*.
gi 24580555 593 MSVPFLLFSGFFVSFDAIPVYLRWITYLSYIRYGFE 628
Cdd:TIGR00956 570 LLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFE 605
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
46-272 |
1.65e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 162.16 E-value: 1.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG--AERNLSAFRK 123
Cdd:COG1131 1 IEVRGLTKRYGD------KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT-SGEVRVLGedVARDPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQDNQLHGNLTVQEamtvatNLKLSKKF---SKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELV 200
Cdd:COG1131 74 RIGYVPQEPALYPDLTVRE------NLRFFARLyglPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 201 SNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLE-EAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
46-264 |
1.26e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 156.74 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA------ERNLS 119
Cdd:COG1136 5 LELRNLTKSYGTGE--GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPT-SGEVLIDGQdisslsERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 120 AFRKLS-AYIMQDNQLHGNLTVQEamTVATNLKLSKKfSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALE 198
Cdd:COG1136 82 RLRRRHiGFVFQFFNLLPELTALE--NVALPLLLAGV-SRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24580555 199 LVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAA-GGRTVICTIHqpSARLFEMFDQLYTLADGQCV 264
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTH--DPELAARADRVIRLRDGRIV 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
48-262 |
1.58e-41 |
|
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: 150.31 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVKEGNRSnaktILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFRKL 124
Cdd:cd03225 2 LKNLSFSYPDGARP----ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT-SGEVLVDGkdlTKLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 125 SAYIMQ--DNQLHgNLTV-QEAMTVATNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVS 201
Cdd:cd03225 77 VGLVFQnpDDQFF-GPTVeEEVAFGLENLGLPEE----EIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 202 NPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQ 262
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
46-272 |
2.48e-41 |
|
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: 150.18 E-value: 2.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFR 122
Cdd:COG1122 1 IELENLSFSYPGG-----TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT-SGEVLVDGkdiTKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 KLSAYIMQ--DNQLHGNlTVQEamTVA---TNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIAL 197
Cdd:COG1122 75 RKVGLVFQnpDDQLFAP-TVEE--DVAfgpENLGLPRE----EIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 198 ELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSArLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
46-262 |
4.14e-41 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 149.18 E-value: 4.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG------AERNLS 119
Cdd:cd03255 1 IELKNLSKTYGGG--GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT-SGEVRVDGtdisklSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 120 AFRKLS-AYIMQDNQLHGNLTVQEamTVATNLKLSKKFsKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALE 198
Cdd:cd03255 78 AFRRRHiGFVFQSFNLLPDLTALE--NVELPLLLAGVP-KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 199 LVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQPsaRLFEMFDQLYTLADGQ 262
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP--ELAEYADRIIELRDGK 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
49-272 |
1.77e-39 |
|
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: 145.77 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 49 HNLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG--AERNLSAFRKLSA 126
Cdd:COG4555 5 ENLSKKYGK------VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD-SGSILIDGedVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 127 YIMQDNQLHGNLTVQEamtvatNLKLSKKF---SKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNP 203
Cdd:COG4555 78 VLPDERGLYDRLTVRE------NIRYFAELyglFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24580555 204 PIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
50-267 |
9.11e-39 |
|
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: 9.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEGnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGY--KTSSIEGSVTMNG--AERNLSAFRKLS 125
Cdd:cd03233 8 NISFTTGKG--RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSVEGDIHYNGipYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQDNQLHGNLTVQEAMTVATNLKLSKkfskpekhsmiddilltlslsehrytMTRNLSGGQKKRLSIALELVSNPPI 205
Cdd:cd03233 86 IYVSEEDVHFPTLTVRETLDFALRCKGNE--------------------------FVRGISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 206 MFFDEPTSGLDSSTCFQCIHLLKMLA-AGGRTVICTIHQPSARLFEMFDQLYTLADGQCVYQG 267
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
46-272 |
2.61e-37 |
|
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: 139.63 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRvkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERN------LS 119
Cdd:cd03256 1 IEVENLSKT-----YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-SGSVLIDGTDINklkgkaLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 120 AFRKLSAYIMQDNQLHGNLTVQEAMTVA-----TNLK-LSKKFSKPEKHSMIDdILLTLSLSEHRYTMTRNLSGGQKKRL 193
Cdd:cd03256 75 QLRRQIGMIFQQFNLIERLSVLENVLSGrlgrrSTWRsLFGLFPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 194 SIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQPS-ARLFemFDQLYTLADGQCVYQGSTKQ 271
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIVFDGPPAE 231
|
.
gi 24580555 272 L 272
Cdd:cd03256 232 L 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
46-282 |
2.71e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.45 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVkegnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGaeRNLSAFRKL 124
Cdd:COG1121 7 IELENLTVSY------GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGlLPPTS--GTVRLFG--KPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 125 SAYIMQDNQLHGN--LTVQE--AMTVATNLKLSKKFSKPEKhSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELV 200
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRDvvLMGRYGRRGLFRRPSRADR-EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 201 SNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSArLFEMFDQLYTLADGQcVYQGSTKQlvpFLSTLN 280
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGL-VAHGPPEE---VLTPEN 230
|
..
gi 24580555 281 LE 282
Cdd:COG1121 231 LS 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
46-273 |
1.44e-36 |
|
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: 137.87 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGaeRNLSAF---- 121
Cdd:COG1120 2 LEAENLSVGYGG------RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDG--RDLASLsrre 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 122 --RKLsAYIMQDNQLHGNLTVQEamTVAT----NLKLSKKFSKpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSI 195
Cdd:COG1120 73 laRRI-AYVPQEPPAPFGLTVRE--LVALgrypHLGLFGRPSA-EDREAVEEALERTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 196 ALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQPS--ARLfemFDQLYTLADGQCVYQGSTKQL 272
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlaARY---ADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 24580555 273 V 273
Cdd:COG1120 226 L 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
49-242 |
2.65e-36 |
|
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: 135.46 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 49 HNLTYRVKEGNRsnaktILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAFRKLSAYI 128
Cdd:cd03226 3 ENISFSYKKGTE-----ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES-SGSILLNGKPIKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 129 MQD--NQLHGNltvqeamTVATNLKLSKKfSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIM 206
Cdd:cd03226 77 MQDvdYQLFTD-------SVREELLLGLK-ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 24580555 207 FFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIH 242
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
46-260 |
4.70e-36 |
|
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: 134.91 E-value: 4.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVkeGNRsnakTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA--ERNLSAFRK 123
Cdd:COG4133 3 LEAENLSCRR--GER----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS-AGEVLWNGEpiRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQDNQLHGNLTVQEamtvatNLKLSKKFSKPEKHSM-IDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSN 202
Cdd:COG4133 76 RLAYLGHADGLKPELTVRE------NLRFWAALYGLRADREaIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 203 PPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPsarLFEMFDQLYTLAD 260
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLGD 204
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
64-272 |
2.36e-35 |
|
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: 133.78 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA------ERNLSAFRKLSAYIMQDNQLHGN 137
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD-SGEVLIDGEdisglsEAELYRLRRRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 138 LTVQEamTVAtnLKLSKKFSKPEkhSMIDDI-LLTLS---LSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTS 213
Cdd:cd03261 92 LTVFE--NVA--FPLREHTRLSE--EEIREIvLEKLEavgLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 214 GLD--SSTCF-QCIHLLKmlAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:cd03261 166 GLDpiASGVIdDLIRSLK--KELGLTSIMVTHDLD-TAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
60-272 |
4.97e-35 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 132.24 E-value: 4.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 60 RSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG--YKTSsieGSVTMNGAE--RNLSAFRKLSAYIMQDNQLH 135
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGelRPTS---GTAYINGYSirTDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 136 GNLTVQEAMTVATNLK-LSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSG 214
Cdd:cd03263 88 DELTVREHLRFYARLKgLPKS----EIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 215 LDS---STCFQCIHLLKmlaaGGRTVICTIHqpSARLFEMF-DQLYTLADGQCVYQGSTKQL 272
Cdd:cd03263 164 LDPasrRAIWDLILEVR----KGRSIILTTH--SMDEAEALcDRIAIMSDGKLRCIGSPQEL 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
46-272 |
7.64e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.87 E-value: 7.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRvkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE------RNLS 119
Cdd:COG3638 3 LELRNLSKR-----YPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT-SGEILVDGQDvtalrgRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 120 AFRKLSAYIMQDNQLHGNLTVQEAmtVAT-------NLK-LSKKFSKPEKHsMIDDILLTLSLSEHRYTMTRNLSGGQKK 191
Cdd:COG3638 77 RLRRRIGMIFQQFNLVPRLSVLTN--VLAgrlgrtsTWRsLLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 192 RLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAA-GGRTVICTIHQPS-ARLFemFDQLYTLADGQCVYQGST 269
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDlARRY--ADRIIGLRDGRVVFDGPP 231
|
...
gi 24580555 270 KQL 272
Cdd:COG3638 232 AEL 234
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
46-272 |
1.35e-34 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 132.04 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNL--TYrvkegnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE------RN 117
Cdd:TIGR02315 2 LEVENLskVY-------PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-SGSILLEGTDitklrgKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 118 LSAFRKLSAYIMQDNQLHGNLTVQEAMTVA------TNLKLSKKFSKPEKHSMIDdILLTLSLSEHRYTMTRNLSGGQKK 191
Cdd:TIGR02315 74 LRKLRRRIGMIFQHYNLIERLTVLENVLHGrlgykpTWRSLLGRFSEEDKERALS-ALERVGLADKAYQRADQLSGGQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 192 RLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQPS-ARLFEmfDQLYTLADGQCVYQGST 269
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDlAKKYA--DRIVGLKAGEIVFDGAP 230
|
...
gi 24580555 270 KQL 272
Cdd:TIGR02315 231 SEL 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
67-213 |
1.40e-34 |
|
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: 128.53 E-value: 1.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNGAE---RNLSAFRKLSAYIMQDNQLHGNLTVQEa 143
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVRE- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24580555 144 mtvatNLKLSKKFSKPEKHSM---IDDILLTLSLSEHRYT----MTRNLSGGQKKRLSIALELVSNPPIMFFDEPTS 213
Cdd:pfam00005 79 -----NLRLGLLLKGLSKREKdarAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-273 |
2.90e-34 |
|
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: 137.97 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 16 GTAGAGQLKA---QIVPAQPKTLQHLPKRPAVDLAFHNLTYRvkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKST 92
Cdd:COG4988 304 GIAAAEKIFAlldAPEPAAPAGTAPLPAAGPPSIELEDVSFS-----YPGGRPALDGLSLTIPPGERVALVGPSGAGKST 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 93 LLNILSGYKTSSiEGSVTMNGAER---NLSAFRKLSAYIMQDNQL-HGnltvqeamTVATNLKLSK-KFSKPE-----KH 162
Cdd:COG4988 379 LLNLLLGFLPPY-SGSILINGVDLsdlDPASWRRQIAWVPQNPYLfAG--------TIRENLRLGRpDASDEEleaalEA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 163 SMIDDILLTLS------LSEHRytmtRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRT 236
Cdd:COG4988 450 AGLDEFVAALPdgldtpLGEGG----RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRT 524
|
250 260 270
....*....|....*....|....*....|....*..
gi 24580555 237 VICTIHQPSARlfEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:COG4988 525 VILITHRLALL--AQADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
64-262 |
7.23e-34 |
|
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: 127.51 E-value: 7.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE--RNLSAFRKLSAYIMQDNQLHGNLTVQ 141
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-SGEIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EamtvatNLKLSKkfskpekhsmiddilltlslsehrytmtrnlsgGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCF 221
Cdd:cd03230 92 E------NLKLSG---------------------------------GMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24580555 222 QCIHLLKMLAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQ 262
Cdd:cd03230 133 EFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGR 172
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
48-262 |
1.04e-33 |
|
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: 126.59 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFRKL 124
Cdd:cd00267 2 IENLSFRYGG------RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-SGEILIDGkdiAKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 125 SAYIMQdnqlhgnltvqeamtvatnlklskkfskpekhsmiddilltlslsehrytmtrnLSGGQKKRLSIALELVSNPP 204
Cdd:cd00267 75 IGYVPQ------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 205 IMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSArLFEMFDQLYTLADGQ 262
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
46-262 |
1.57e-32 |
|
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: 123.65 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKegnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNG---AERNLSAF 121
Cdd:cd03228 1 IEFKNVSFSYP----GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlYDPTS--GEILIDGvdlRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 122 RKLSAYIMQDNQLHgnltvqeAMTVATNLklskkfskpekhsmiddilltlslsehrytmtrnLSGGQKKRLSIALELVS 201
Cdd:cd03228 75 RKNIAYVPQDPFLF-------SGTIRENI----------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 202 NPPIMFFDEPTSGLDSSTCFQCIHLLKMLaAGGRTVICTIHQPSarLFEMFDQLYTLADGQ 262
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLS--TIRDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
29-273 |
5.94e-32 |
|
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: 132.27 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 29 PAQPKTLQHLPKRPAvDLAFHNLTYRVkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieG 107
Cdd:COG2274 458 REEGRSKLSLPRLKG-DIELENVSFRY----PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlYEPTS--G 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 108 SVTMNG---AERNLSAFRKLSAYIMQDNQL-HGnltvqeamTVATNLKLSKKFSKPE------KHSMIDDILLTLS---- 173
Cdd:COG2274 531 RILIDGidlRQIDPASLRRQIGVVLQDVFLfSG--------TIRENITLGDPDATDEeiieaaRLAGLHDFIEALPmgyd 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 174 --LSEhrytMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVICTIHQPSarLFEM 251
Cdd:COG2274 603 tvVGE----GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS--TIRL 675
|
250 260
....*....|....*....|..
gi 24580555 252 FDQLYTLADGQCVYQGSTKQLV 273
Cdd:COG2274 676 ADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
46-267 |
4.96e-31 |
|
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: 121.07 E-value: 4.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNRSNakTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNG------AERNL 118
Cdd:cd03257 2 LEVKNLSVSFPTGGGSV--KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGlLKPTS--GSIIFDGkdllklSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 119 SAFRKLSAYIMQD--NQLHGNLTVQEAmtVATNLKLSKKFSKPEKHSMI-DDILLTLSLSEHRYTM-TRNLSGGQKKRLS 194
Cdd:cd03257 78 KIRRKEIQMVFQDpmSSLNPRMTIGEQ--IAEPLRIHGKLSKKEARKEAvLLLLVGVGLPEEVLNRyPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 195 IALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQPSArLFEMFDQLYTLADGQCVYQG 267
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
62-272 |
7.15e-31 |
|
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: 121.24 E-value: 7.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGA------ERNLSAFRKLSAYIMQDNQL 134
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGlLRPDS--GEILVDGQditglsEKELYELRRRIGMLFQGGAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 135 HGNLTVQEamTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSG 214
Cdd:COG1127 94 FDSLTVFE--NVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 215 LD--SSTCF-QCIHLLKmlAAGGRTVICTIHQ-PSArlFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:COG1127 172 LDpiTSAVIdELIRELR--DELGLTSVVVTHDlDSA--FAIADRVAVLADGKIIAEGTPEEL 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
46-262 |
1.09e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.54 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVkegnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAER---NLSAFR 122
Cdd:COG4619 1 LELEGLSFRV------GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-SGEIYLDGKPLsamPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 KLSAYIMQDNQLHGNlTVQEAMTVATNLKlSKKFSKPEKHSMIDDILLTLSLSEHRytmTRNLSGGQKKRLSIALELVSN 202
Cdd:COG4619 74 RQVAYVPQEPALWGG-TVRDNLPFPFQLR-ERKFDRERALELLERLGLPPDILDKP---VERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 203 PPIMFFDEPTSGLDSSTcFQCIH--LLKMLAAGGRTVICTIHQPsARLFEMFDQLYTLADGQ 262
Cdd:COG4619 149 PDVLLLDEPTSALDPEN-TRRVEelLREYLAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
25-273 |
1.49e-30 |
|
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: 126.80 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 25 AQIVPAQPKTLQH---LPKRPAVDLAFHNLTYRVKEGNRsnakTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-Y 100
Cdd:COG4987 310 NELLDAPPAVTEPaepAPAPGGPSLELEDVSFRYPGAGR----PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRfL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 101 KTSSieGSVTMNG---AERNLSAFRKLSAYIMQDNQLHgnltvqeAMTVATNLKLSKKFSKPEK----------HSMIDD 167
Cdd:COG4987 386 DPQS--GSITLGGvdlRDLDEDDLRRRIAVVPQRPHLF-------DTTLRENLRLARPDATDEElwaalervglGDWLAA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 168 I---LLTLsLSEHrytmTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVICTIHQP 244
Cdd:COG4987 457 LpdgLDTW-LGEG----GRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRL 530
|
250 260
....*....|....*....|....*....
gi 24580555 245 SArlFEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:COG4987 531 AG--LERMDRILVLEDGRIVEQGTHEELL 557
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
46-312 |
1.65e-30 |
|
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: 126.17 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKeGNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE------RNL 118
Cdd:COG1123 261 LEVRNLSKRYP-VRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGlLRPTS--GSILFDGKDltklsrRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 119 SAFRKLSAYIMQD--NQLHGNLTVQEAmtVATNLKLSKKFSKPEKHSMIDDILLTLSLSE---HRYTmtRNLSGGQKKRL 193
Cdd:COG1123 338 RELRRRVQMVFQDpySSLNPRMTVGDI--IAEPLRLHGLLSRAERRERVAELLERVGLPPdlaDRYP--HELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 194 SIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAA-GGRTVictihqpsarLF---------EMFDQLYTLADGQC 263
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTY----------LFishdlavvrYIADRVAVMYDGRI 483
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 24580555 264 VYQGSTKQLvpflstlnlecpsYHNPASyvievscgehgDHTRKLVDAI 312
Cdd:COG1123 484 VEDGPTEEV-------------FANPQH-----------PYTRALLAAV 508
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
58-273 |
2.01e-30 |
|
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: 119.91 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 58 GNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE---RNLSAFRKLSAYIMQD--N 132
Cdd:COG1124 12 GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW-SGEVTFDGRPvtrRRRKAFRRRVQMVFQDpyA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 133 QLHGNLTVQEAmtVATNLKLSKKfskPEKHSMIDDILLTLSLSE---HRYTmtRNLSGGQKKRLSIALELVSNPPIMFFD 209
Cdd:COG1124 91 SLHPRHTVDRI--LAEPLRIHGL---PDREERIAELLEQVGLPPsflDRYP--HQLSGGQRQRVAIARALILEPELLLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 210 EPTSGLDSSTCFQCIHLLKML-AAGGRTVICTIHQPSARLFeMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:COG1124 164 EPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAH-LCDRVAVMQNGRIVEELTVADLL 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
65-297 |
2.45e-30 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 128.43 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 65 TILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSS--IEGSVTMNGAERNLSAFRKLSAYIMQdNQLH-GNLTVQ 141
Cdd:PLN03140 179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkVSGEITYNGYRLNEFVPRKTSAYISQ-NDVHvGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EAMT-------VATNLKLSKKFSKPEKHSMI------------------------DDILLTLSLSEHRYT-----MTRNL 185
Cdd:PLN03140 258 ETLDfsarcqgVGTRYDLLSELARREKDAGIfpeaevdlfmkatamegvksslitDYTLKILGLDICKDTivgdeMIRGI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 186 SGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQ---CIHLLKMLAAGgrTVICTIHQPSARLFEMFDQLYTLADGQ 262
Cdd:PLN03140 338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQivkCLQQIVHLTEA--TVLMSLLQPAPETFDLFDDIILLSEGQ 415
|
250 260 270
....*....|....*....|....*....|....*
gi 24580555 263 CVYQGSTKQLVPFLSTLNLECPSYHNPASYVIEVS 297
Cdd:PLN03140 416 IVYQGPRDHILEFFESCGFKCPERKGTADFLQEVT 450
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
48-267 |
4.04e-30 |
|
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: 118.02 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVkegnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGaeRNLSAFRKLSAY 127
Cdd:cd03235 2 VEDLTVSY------GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT-SGSIRVFG--KPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 128 IMQdnqlHGN------LTVQE--AMTVATNLKLSKKFSKPEKHSmIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALEL 199
Cdd:cd03235 73 VPQ----RRSidrdfpISVRDvvLMGLYGHKGLFRRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 200 VSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSArLFEMFDQLYTLaDGQCVYQG 267
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
66-272 |
6.39e-30 |
|
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: 117.92 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLS---AYIMQDNQLHGNLTVQ 141
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR-SGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EamtvatNLKLSKKFSKPEKHSMIDDILLTL--SLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST 219
Cdd:cd03224 94 E------NLLLGAYARRRAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24580555 220 CFQCIHLLKMLAAGGRTVIcTIHQPSARLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:cd03224 168 VEEIFEAIRELRDEGVTIL-LVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
46-267 |
9.51e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 116.91 E-value: 9.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEgnrsnaKTILKGVSGRLRSGeLTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE--RNLSAFRK 123
Cdd:cd03264 1 LQLENLTKRYGK------KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGQDvlKQPQKLRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQDNQLHGNLTVQEAMTVATNLKlskKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNP 203
Cdd:cd03264 73 RIGYLPQEFGVYPNFTVREFLDYIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 204 PIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQG 267
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
49-267 |
1.13e-29 |
|
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: 115.61 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 49 HNLTYRVkegnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFRKLS 125
Cdd:cd03214 3 ENLSVGY------GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGkdlASLSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQdnqlhgnltvqeAMTvATNLklskkfskpekhsmiddilltLSLSEHRYTMtrnLSGGQKKRLSIALELVSNPPI 205
Cdd:cd03214 76 AYVPQ------------ALE-LLGL---------------------AHLADRPFNE---LSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 206 MFFDEPTSGLDSSTCFQCIHLLKMLAA-GGRTVICTIHQPS-ARLFemFDQLYTLADGQCVYQG 267
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNlAARY--ADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
62-267 |
1.86e-29 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 116.08 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLSAYIMQDNQLHGNLTV 140
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-SGEILIDGRDvTGVPPERRNIGMVFQDYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 QEamTVATNLKLsKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTC 220
Cdd:cd03259 90 AE--NIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24580555 221 FQCIHLLK-MLAAGGRTVICTIHQPS-ArlFEMFDQLYTLADGQCVYQG 267
Cdd:cd03259 167 EELREELKeLQRELGITTIYVTHDQEeA--LALADRIAVMNEGRIVQVG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
58-272 |
5.01e-29 |
|
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: 115.76 E-value: 5.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 58 GNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG------AERNLSAFRKLSAYIMQD 131
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT-SGSVLVDGtdltllSGKELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 132 NQLHGNLTVQEamTVATNLKLSKKfSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:cd03258 91 FNLLSSRTVFE--NVALPLEIAGV-PKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 212 TSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQPSArLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:cd03258 168 TSALDPETTQSILALLRDINRElGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
46-262 |
6.51e-29 |
|
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: 113.44 E-value: 6.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA-----ERNLSA 120
Cdd:cd03229 1 LELKNVSKRYGQ------KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-SGSILIDGEdltdlEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQDNQLHGNLTVQEamtvatNLKLSkkfskpekhsmiddilltlslsehrytmtrnLSGGQKKRLSIALELV 200
Cdd:cd03229 74 LRRRIGMVFQDFALFPHLTVLE------NIALG-------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 201 SNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQPsARLFEMFDQLYTLADGQ 262
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
67-238 |
9.02e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 114.84 E-value: 9.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE-RNLSAFRKLSAYI---MQDNQLHGNLTVQ 141
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGfLRPTS--GSVLFDGEDiTGLPPHEIARLGIgrtFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EAMTVATNLKLSKKF-------SKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSG 214
Cdd:cd03219 94 ENVMVAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180
....*....|....*....|....
gi 24580555 215 LDSSTCFQCIHLLKMLAAGGRTVI 238
Cdd:cd03219 174 LNPEETEELAELIRELRERGITVL 197
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
77-267 |
1.88e-28 |
|
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: 113.36 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 77 GELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLS--AFRKLSAyIMQDNQLHGNLTVQE--AMTVATNLKL 152
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQ-SGRVLINGVDVTAAppADRPVSM-LFQENNLFAHLTVEQnvGLGLSPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 153 SkkfskPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHL-LKMLA 231
Cdd:cd03298 102 T-----AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLvLDLHA 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 24580555 232 AGGRTVICTIHQPSARLfEMFDQLYTLADGQCVYQG 267
Cdd:cd03298 177 ETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
46-314 |
1.97e-28 |
|
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: 120.01 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGnrsnAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGY--KTSSIEGSVTMNG---AERNLSA 120
Cdd:COG1123 5 LEVRDLSVRYPGG----DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGrdlLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQD--NQLHGnLTVQEAMT-VATNLKLSKKfskpEKHSMIDDILLTLSLSE--HRYTMTrnLSGGQKKRLSI 195
Cdd:COG1123 81 RGRRIGMVFQDpmTQLNP-VTVGDQIAeALENLGLSRA----EARARVLELLEAVGLERrlDRYPHQ--LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 196 ALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAA-GGRTVICTIHQPsARLFEMFDQLYTLADGQCVYQGSTKQL-- 272
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEIla 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24580555 273 -------VPFLSTLNLECPSYHNPASYVIEVS--CGEHGDHTRKLVDAIDN 314
Cdd:COG1123 233 apqalaaVPRLGAARGRAAPAAAAAEPLLEVRnlSKRYPVRGKGGVRAVDD 283
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
49-271 |
6.64e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.29 E-value: 6.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 49 HNLTYRVkeGNRsnakTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGaeRNLSAF--RKLSA 126
Cdd:COG4559 5 ENLSVRL--GGR----TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS-SGEVRLNG--RPLAAWspWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 127 Y--IM-QDNQLHGNLTVQE--AMTVATNLklskkFSKPEKHSMIDDIL-LT--LSLSEHRYtmtRNLSGGQKKRLSIA-- 196
Cdd:COG4559 76 RraVLpQHSSLAFPFTVEEvvALGRAPHG-----SSAAQDRQIVREALaLVglAHLAGRSY---QTLSGGEQQRVQLArv 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 197 ----LELVSNPP-IMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSarLFEMF-DQLYTLADGQCVYQGSTK 270
Cdd:COG4559 148 laqlWEPVDGGPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN--LAAQYaDRILLLHQGRLVAQGTPE 225
|
.
gi 24580555 271 Q 271
Cdd:COG4559 226 E 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
66-242 |
7.60e-28 |
|
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: 110.98 E-value: 7.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE-----RNLSAFRKLSAYIMQ--DNQLHGN 137
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGlLRPQS--GAVLIDGEPldysrKGLLERRQRVGLVFQdpDDQLFAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 138 LTVQEAMTVATNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:TIGR01166 85 DVDQDVAFGPLNLGLSEA----EVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*
gi 24580555 218 STCFQCIHLLKMLAAGGRTVICTIH 242
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
77-272 |
1.11e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 111.77 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 77 GELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE--RNLSAFRKLSAyIMQDNQLHGNLTVQE--AMTVATNLKL 152
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPPD-SGRILWNGQDltALPPAERPVSM-LFQENNLFPHLTVAQniGLGLRPGLKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 153 SkkfskPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAA 232
Cdd:COG3840 103 T-----AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24580555 233 G-GRTVICTIHQPS--ARLfemFDQLYTLADGQCVYQGSTKQL 272
Cdd:COG3840 178 ErGLTVLMVTHDPEdaARI---ADRVLLVADGRIAADGPTAAL 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
48-242 |
1.62e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.91 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVKEGnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGaeRNLSA--FRKL 124
Cdd:COG2884 4 FENVSKRYPGG-----REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeERPTS--GQVLVNG--QDLSRlkRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 125 SAY------IMQDNQLHGNLTVQE----AMTVAtnlklskKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLS 194
Cdd:COG2884 75 PYLrrrigvVFQDFRLLPDRTVYEnvalPLRVT-------GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24580555 195 IALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIH 242
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
50-262 |
2.29e-27 |
|
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: 108.84 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEGNRsnakTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERN---LSAFRKLSA 126
Cdd:cd03246 5 NVSFRYPGAEP----PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADISqwdPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 127 YIMQDNQLhgnltvqeamtvatnlklskkFSKpekhSMIDDIlltlslsehrytmtrnLSGGQKKRLSIALELVSNPPIM 206
Cdd:cd03246 80 YLPQDDEL---------------------FSG----SIAENI----------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 207 FFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSarLFEMFDQLYTLADGQ 262
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGR 172
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
46-238 |
3.04e-27 |
|
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: 110.25 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVkeGNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAFRKls 125
Cdd:cd03293 1 LEVRNVSKTY--GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT-SGEVLVDGEPVTGPGPDR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQDNQLHGNLTVQEamTVATNLKLsKKFSKPEKHSMIDDILLTLSLS--EHRYtmTRNLSGGQKKRLSIALELVSNP 203
Cdd:cd03293 76 GYVFQQDALLPWLTVLD--NVALGLEL-QGVPKAEARERAEELLELVGLSgfENAY--PHQLSGGMRQRVALARALAVDP 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 24580555 204 PIMFFDEPTSGLDSSTCFQcIH--LLKMLAAGGRTVI 238
Cdd:cd03293 151 DVLLLDEPFSALDALTREQ-LQeeLLDIWRETGKTVL 186
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
62-244 |
3.13e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 109.58 E-value: 3.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAFRKLSAYIMQDNQLHGNLTVQ 141
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPA-AGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EamtvatNLKLSKKFsKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCF 221
Cdd:PRK13539 92 E------NLEFWAAF-LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|...
gi 24580555 222 QCIHLLKMLAAGGRTVICTIHQP 244
Cdd:PRK13539 165 LFAELIRAHLAQGGIVIAATHIP 187
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
64-273 |
5.49e-27 |
|
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: 110.01 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNIL-SGYKTSSieGSVTMNG---AERNLSAFRKLSAYIMQDNQLHGNlt 139
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfRFYDVSS--GSILIDGqdiREVTLDSLRRAIGVVPQDTVLFND-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 vqeamTVATNLKLSKKFSKPE------KHSMIDDILLTLS------LSEhRYTMtrnLSGGQKKRLSIALELVSNPPIMF 207
Cdd:cd03253 90 -----TIGYNIRYGRPDATDEevieaaKAAQIHDKIMRFPdgydtiVGE-RGLK---LSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 208 FDEPTSGLDSST---CFQCIhllkMLAAGGRTVICTIHqpsaRLFEMF--DQLYTLADGQCVYQGSTKQLV 273
Cdd:cd03253 161 LDEATSALDTHTereIQAAL----RDVSKGRTTIVIAH----RLSTIVnaDKIIVLKDGRIVERGTHEELL 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
63-272 |
1.01e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 109.31 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 63 AKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG-----AERNLSAFRKLSAYIMQDNQLHGN 137
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPD-SGTITVDGedltdSKKDINKLRRKVGMVFQQFNLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 138 LTVQEAMTVAtnLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD- 216
Cdd:COG1126 92 LTVLENVTLA--PIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDp 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24580555 217 -------SstcfqcihLLKMLAAGGRTVICTIHqpsarlfEM-F-----DQLYTLADGQCVYQGSTKQL 272
Cdd:COG1126 170 elvgevlD--------VMRDLAKEGMTMVVVTH-------EMgFarevaDRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
64-243 |
1.12e-26 |
|
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: 108.39 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-----RNLSAFRKLSAYIMQDNQLHGNL 138
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD-SGTIIIDGLKltddkKNINELRQKVGMVFQQFNLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 139 TVQEAMTVA--TNLKLSKKfsKPEKHSMidDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:cd03262 92 TVLENITLApiKVKGMSKA--EAEERAL--ELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180
....*....|....*....|....*..
gi 24580555 217 SSTCFQCIHLLKMLAAGGRTVICTIHQ 243
Cdd:cd03262 168 PELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
46-238 |
3.97e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 107.87 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNL--TYRVKEGNRsnakTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFR 122
Cdd:COG1116 8 LELRGVskRFPTGGGGV----TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT-SGEVLVDGKPvTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 klsAYIMQDNQLHGNLTVQEamTVATNLKLsKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSN 202
Cdd:COG1116 83 ---GVVFQEPALLPWLTVLD--NVALGLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 24580555 203 PPIMFFDEPTSGLDSSTCFQcIH--LLKMLAAGGRTVI 238
Cdd:COG1116 157 PEVLLMDEPFGALDALTRER-LQdeLLRLWQETGKTVL 193
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
64-267 |
4.75e-26 |
|
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: 106.15 E-value: 4.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE--RNLSAFRKLSAyIMQDNQLHGNLTVQ 141
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD-SGEITFDGKSyqKNIEALRRIGA-LIEAPGFYPNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EAMTVATNLKLSKKfskpekhSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCF 221
Cdd:cd03268 91 ENLRLLARLLGIRK-------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 24580555 222 QCIHLLKMLAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQG 267
Cdd:cd03268 164 ELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
65-238 |
7.17e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 107.05 E-value: 7.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 65 TILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGaeRNLSAfrkLSAYIM---------QDNQL 134
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGfYRPTS--GRILFDG--RDITG---LPPHRIarlgiartfQNPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 135 HGNLTVQEAMTVATNLKLSKKF------------SKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSN 202
Cdd:COG0411 91 FPELTVLENVLVAAHARLGRGLlaallrlprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 24580555 203 PPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVI 238
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIRRLRDErGITIL 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
45-273 |
1.24e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.80 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 45 DLAFHNLTYRVKEGnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNG---AERNLSA 120
Cdd:COG1132 339 EIEFENVSFSYPGD-----RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfYDPTS--GRILIDGvdiRDLTLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQDNQL-HGnltvqeamTVATNLKLSKK-FSKPE-----KHSMIDDILLTLslsEHRY-TMT----RNLSGG 188
Cdd:COG1132 412 LRRQIGVVPQDTFLfSG--------TIRENIRYGRPdATDEEveeaaKAAQAHEFIEAL---PDGYdTVVgergVNLSGG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 189 QKKRLSIALELVSNPPIMFFDEPTSGLDSSTcfqCIHLLKMLAA--GGRTVIcTI-HQPSArlFEMFDQLYTLADGQCVY 265
Cdd:COG1132 481 QRQRIAIARALLKDPPILILDEATSALDTET---EALIQEALERlmKGRTTI-VIaHRLST--IRNADRILVLDDGRIVE 554
|
....*...
gi 24580555 266 QGSTKQLV 273
Cdd:COG1132 555 QGTHEELL 562
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
77-269 |
1.77e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 104.94 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 77 GELTAIMGPSGAGKSTLLNILSGYKTSsIEGSVTMNGAERNLSA-FRKLSAYIMQDNQLHGNLTVQEamTVATNLKLSKK 155
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEP-ASGSIKVNDQSHTGLApYQRPVSMLFQENNLFAHLTVRQ--NIGLGLHPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 156 FSKPEKHSMIDdILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAA-GG 234
Cdd:TIGR01277 101 LNAEQQEKVVD-AAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSeRQ 179
|
170 180 190
....*....|....*....|....*....|....*
gi 24580555 235 RTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGST 269
Cdd:TIGR01277 180 RTLLMVTHHLS-DARAIASQIAVVSQGKIKVVSDC 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
50-284 |
3.14e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.93 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEGNRSnaktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE-----RNLSAFRK 123
Cdd:PRK13639 6 DLKYSYPDGTEA-----LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTS--GEVLIKGEPikydkKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQ--DNQLHGNLTVQEAMTVATNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVS 201
Cdd:PRK13639 79 TVGIVFQnpDDQLFAPTVEEDVAFGPLNLGLSKE----EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 202 NPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQpsARLFEMF-DQLYTLADGQCVYQGSTKQLVPFLSTL- 279
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEGTPKEVFSDIETIr 232
|
....*..
gi 24580555 280 --NLECP 284
Cdd:PRK13639 233 kaNLRLP 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
76-267 |
1.19e-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: 102.37 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 76 SGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA-------ERNLSAFRKLSAYIMQDNQLHGNLTVQEAMTVAT 148
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPD-GGTIVLNGTvlfdsrkKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 149 nlklsKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLL- 227
Cdd:cd03297 101 -----KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELk 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24580555 228 KMLAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQG 267
Cdd:cd03297 176 QIKKNLNIPVIFVTHDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
39-262 |
2.03e-24 |
|
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: 102.13 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 39 PKRPAVDLafHNLTYRVKEGnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA---- 114
Cdd:COG4181 4 SSAPIIEL--RGLTKTVGTG--AGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPT-SGTVRLAGQdlfa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 115 --ERNLSAFR-KLSAYIMQDNQLHGNLTVQEamTVATNLKLSkkfSKPEKHSMIDDILLTLSLSeHRYT-MTRNLSGGQK 190
Cdd:COG4181 79 ldEDARARLRaRHVGFVFQSFQLLPTLTALE--NVMLPLELA---GRRDARARARALLERVGLG-HRLDhYPAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 191 KRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLL-KMLAAGGRTVICTIHQPsaRLFEMFDQLYTLADGQ 262
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVTHDP--ALAARCDRVLRLRAGR 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
67-260 |
2.03e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 102.41 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE-RNLSAFRKLSAYIMQDNQLHGNLTVQEam 144
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGfIKPDS--GKILLNGKDiTNLPPEKRDISYVPQNYALFPHMTVYK-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 145 TVATNLKLsKKFSKPEKHSMIDDILLTLSLSE--HRYTMTrnLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQ 222
Cdd:cd03299 91 NIAYGLKK-RKVDKKEIERKVLEIAEMLGIDHllNRKPET--LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 24580555 223 CIHLLKML-AAGGRTVICTIHQpsarlfemFDQLYTLAD 260
Cdd:cd03299 168 LREELKKIrKEFGVTVLHVTHD--------FEEAWALAD 198
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
67-267 |
2.58e-24 |
|
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: 101.51 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE-RNLSAF--RKLSAYIMQDNQL-HG----N 137
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlYKPTS--GSVLLDGTDiRQLDPAdlRRNIGYVPQDVTLfYGtlrdN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 138 LT----------VQEAMTVATNLKLSKKfskpekHSMIDDilltLSLSEHrytmTRNLSGGQKKRLSIALELVSNPPIMF 207
Cdd:cd03245 98 ITlgapladderILRAAELAGVTDFVNK------HPNGLD----LQIGER----GRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 208 FDEPTSGLDSSTCFQCIHLLKMLaAGGRTVICTIHQPSarLFEMFDQLYTLADGQCVYQG 267
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
49-268 |
2.76e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.54 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 49 HNLTYRVkegnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNGaeRNLSAF--RKLSA 126
Cdd:PRK13548 6 RNLSVRL------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGE-LSPDSGEVRLNG--RPLADWspAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 127 Y--IM-QDNQLHGNLTVQE--AMTVATNlklskKFSKPEKHSMIDDILLTLSLSE--HRYTMTrnLSGGQKKRLSIALEL 199
Cdd:PRK13548 77 RraVLpQHSSLSFPFTVEEvvAMGRAPH-----GLSRAEDDALVAAALAQVDLAHlaGRDYPQ--LSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24580555 200 V------SNPPIMFFDEPTSGLDSSTCFQCIHLLKMLA-AGGRTVICTIHqpSARLFEMF-DQLYTLADGQCVYQGS 268
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH--DLNLAARYaDRIVLLHQGRLVADGT 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
67-250 |
4.51e-24 |
|
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: 100.95 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE------RNLSAFRKLSAYIMQDNQLHGNLTV 140
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPT-SGTIRVNGQDvsdlrgRAIPYLRRKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 QEamTVATNLKLSKKFSKpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTC 220
Cdd:cd03292 96 YE--NVAFALEVTGVPPR-EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190
....*....|....*....|....*....|
gi 24580555 221 FQCIHLLKMLAAGGRTVICTIHqpSARLFE 250
Cdd:cd03292 173 WEIMNLLKKINKAGTTVVVATH--AKELVD 200
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
62-272 |
7.89e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 100.93 E-value: 7.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG--YKTSSieGSVTMNGAER---NLSAFRKLSAYI---MQDnQ 133
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlPPTYG--NDVRLFGERRggeDVWELRKRIGLVspaLQL-R 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 134 LHGNLTVQEAmtVAT----NLKLSKKFSkPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFD 209
Cdd:COG1119 91 FPRDETVLDV--VLSgffdSIGLYREPT-DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 210 EPTSGLDSSTCFQCIHLLKMLAAGGRTVICTI-HQPSArLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVtHHVEE-IPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
46-244 |
8.64e-24 |
|
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: 99.36 E-value: 8.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRvkegnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNGAERNLSA--FRK 123
Cdd:TIGR01189 1 LAARNLACS------RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL-LRPDSGEVRWNGTPLAEQRdePHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQDNQLHGNLTVQEamtvatNLKLSKKFSKPEKHsMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNP 203
Cdd:TIGR01189 74 NILYLGHLPGLKPELSALE------NLHFWAAIHGGAQR-TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24580555 204 PIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQP 244
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
64-216 |
9.95e-24 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 100.39 E-value: 9.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLSAYIMQDNQLHGNLTVQE 142
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-SGEILLDGKDiTNLPPHKRPVNTVFQNYALFPHLTVFE 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 143 amTVATNLKLsKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:cd03300 92 --NIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
46-267 |
2.29e-23 |
|
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: 97.77 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEgnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAErnLSAFRK- 123
Cdd:cd03247 1 LSINNVSFSYPE----QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQ--GEITLDGVP--VSDLEKa 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQDNQlhgnltvqEAMTVATNLklskkfskpekhsmiddilltlslsehRYTMTRNLSGGQKKRLSIALELVSNP 203
Cdd:cd03247 73 LSSLISVLNQ--------RPYLFDTTL---------------------------RNNLGRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 204 PIMFFDEPTSGLDSSTCFQCIHLLkMLAAGGRTVICTIHQPSArlFEMFDQLYTLADGQCVYQG 267
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLI-FEVLKDKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
66-272 |
2.65e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 99.29 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLS---AYIMQDNQLHGNLTVQ 141
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR-SGSIRFDGEDiTGLPPHRIARlgiGYVPEGRRIFPSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EamtvatNLKL--SKKFSKPEKHSMIDDIlLTL--SLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:COG0410 97 E------NLLLgaYARRDRAEVRADLERV-YELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 218 STCFQCIHLLKMLAAGGRTVICtIHQPSARLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:COG0410 170 LIVEEIFEIIRRLNREGVTILL-VEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
67-242 |
3.00e-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: 98.60 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGY-KTSSIEGSVTMNGAERNLSAFRKLSAYIMQDnqlhgnLTVQEAMT 145
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLlKPTSGRATVAGHDVVREPREVRRRIGIVFQD------LSVDDELT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 146 VATNLKLSKK---FSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQ 222
Cdd:cd03265 90 GWENLYIHARlygVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180
....*....|....*....|.
gi 24580555 223 CI-HLLKMLAAGGRTVICTIH 242
Cdd:cd03265 170 VWeYIEKLKEEFGMTILLTTH 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-245 |
4.57e-23 |
|
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: 103.52 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 23 LKAQIVPAQPKTlqHLPKRPAVDLAFHNLTYRvkEGNRSNAktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKT 102
Cdd:TIGR02857 301 LDAAPRPLAGKA--PVTAAPASSLEFSGVSVA--YPGRRPA---LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 103 SSiEGSVTMNG---AERNLSAFRKLSAYIMQDNQLHgnltvqeAMTVATNLKLSKKFSKPEK----------HSMIDDIL 169
Cdd:TIGR02857 374 PT-EGSIAVNGvplADADADSWRDQIAWVPQHPFLF-------AGTIAENIRLARPDASDAEirealeraglDEFVAALP 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 170 LTLS--LSEHrytmTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLaAGGRTVICTIHQPS 245
Cdd:TIGR02857 446 QGLDtpIGEG----GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLA 518
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
46-267 |
6.77e-23 |
|
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: 97.35 E-value: 6.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNGAERNLSAFRKLs 125
Cdd:cd03269 1 LEVENVTKRFGR------VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI-ILPDSGEVLFDGKPLDIAARNRI- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQDNQLHGNLTVQEAMTVATNLK-LSKKFSKPEkhsmIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPP 204
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKgLKKEEARRR----IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 205 IMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQpSARLFEMFDQLYTLADGQCVYQG 267
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
45-273 |
1.18e-22 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 103.02 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 45 DLAFHNLTYRVKEGNRSNaktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKtsSIEGSVTMNGAERNL---SA 120
Cdd:TIGR03375 463 EIEFRNVSFAYPGQETPA----LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGlYQ--PTEGSVLLDGVDIRQidpAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQDNQL-HGnltvqeamTVATNLKLSKKFskPEKHSMIDDILLT-----LSLSEHRYTMT-----RNLSGGQ 189
Cdd:TIGR03375 537 LRRNIGYVPQDPRLfYG--------TLRDNIALGAPY--ADDEEILRAAELAgvtefVRRHPDGLDMQigergRSLSGGQ 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 190 KKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVICTIHQPSarLFEMFDQLYTLADGQCVYQGST 269
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA-GKTLVLVTHRTS--LLDLVDRIIVMDNGRIVADGPK 683
|
....
gi 24580555 270 KQLV 273
Cdd:TIGR03375 684 DQVL 687
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
60-244 |
1.23e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 60 RSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKtSSIEGSVTMNGAERnlsafrklSAYIMQ----DNQLh 135
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL-RPTSGTVRRAGGAR--------VAYVPQrsevPDSL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 136 gNLTVQEAMTVAT--NLKLSKKFSKpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTS 213
Cdd:NF040873 71 -PLTVRDLVAMGRwaRRGLWRRLTR-DDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|.
gi 24580555 214 GLDSSTCFQCIHLLKMLAAGGRTVICTIHQP 244
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
41-272 |
1.43e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.38 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 41 RPAVDLAFHNLTYRVKEGNRSnaktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNG-----A 114
Cdd:PRK13636 1 MEDYILKVEELNYNYSDGTHA-----LKGININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSS--GRILFDGkpidyS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 115 ERNLSAFRKLSAYIMQ--DNQLHGNLTVQEAMTVATNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKR 192
Cdd:PRK13636 74 RKGLMKLRESVGMVFQdpDNQLFSASVYQDVSFGAVNLKLPED----EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 193 LSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQ-PSARLFemFDQLYTLADGQCVYQGSTK 270
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDiDIVPLY--CDNVFVMKEGRVILQGNPK 227
|
..
gi 24580555 271 QL 272
Cdd:PRK13636 228 EV 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
60-273 |
1.46e-22 |
|
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: 96.84 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 60 RSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNGAE-RNLSAFRKLSA---YIMQDNQLH 135
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGL-VKPDSGKILLDGQDiTKLPMHKRARLgigYLPQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 136 GNLTVQEamtvatNLKL---SKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPT 212
Cdd:cd03218 88 RKLTVEE------NILAvleIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 213 SGLDSSTCFQCIHLLKMLAAGGRTVICTIHqpSAR-LFEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIGVLITDH--NVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
62-272 |
1.67e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.13 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSS----------IEGSVTMNGAERNLSAFRKLSAYIMQD 131
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEagtirvgditIDTARSLSQQKGLIRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 132 NQLHGNLTVQEamTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:PRK11264 94 FNLFPHRTVLE--NIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 212 TSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPS-ARlfEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:PRK11264 172 TSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSfAR--DVADRAIFMDQGRIVEQGPAKAL 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
73-273 |
2.75e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.19 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 73 RLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLS--AFRKLSAyIMQDNQLHGNLTVQE--AMTVAT 148
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGQDHTTTppSRRPVSM-LFQENNLFSHLTVAQniGLGLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 149 NLKLSkkfskPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLK 228
Cdd:PRK10771 99 GLKLN-----AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 229 MlaaggrtvICTIHQ-----------PSARLFEMFdqlYTLADGQCVYQGSTKQLV 273
Cdd:PRK10771 174 Q--------VCQERQltllmvshsleDAARIAPRS---LVVADGRIAWDGPTDELL 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
48-219 |
3.05e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 98.61 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNL--TYRVKEGNRsnakTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA------ERNLS 119
Cdd:COG1135 4 LENLskTFPTKGGPV----TALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPT-SGSVLVDGVdltalsERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 120 AFRKLSAYIMQdnqlHGNLtvQEAMTVATN----LKLSKKfSKPEKHSMIDDiLLTL-SLSEHRYTMTRNLSGGQKKRLS 194
Cdd:COG1135 79 AARRKIGMIFQ----HFNL--LSSRTVAENvalpLEIAGV-PKAEIRKRVAE-LLELvGLSDKADAYPSQLSGGQKQRVG 150
|
170 180
....*....|....*....|....*
gi 24580555 195 IALELVSNPPIMFFDEPTSGLDSST 219
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPET 175
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
45-216 |
3.16e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.61 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 45 DLAFHNLTYRVkegnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNG--------AE 115
Cdd:COG3839 3 SLELENVSKSY------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPTS--GEILIGGrdvtdlppKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 116 RNLsafrklsAYIMQDNQL--HgnltvqeaMTVATN----LKLsKKFSKPEKHSMIDDILLTLSLSE--HRYtmTRNLSG 187
Cdd:COG3839 75 RNI-------AMVFQSYALypH--------MTVYENiafpLKL-RKVPKAEIDRRVREAAELLGLEDllDRK--PKQLSG 136
|
170 180
....*....|....*....|....*....
gi 24580555 188 GQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
50-274 |
3.28e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.29 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG---YKTSSieGSVTMNGA--------ERnl 118
Cdd:COG0396 5 NLHVSVEG------KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTS--GSILLDGEdilelspdER-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 119 saFRKLSAYIMQdnqlhgN------LTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSE---HRYtMTRNLSGGQ 189
Cdd:COG0396 75 --ARAGIFLAFQ------YpveipgVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEdflDRY-VNEGFSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 190 KKRLSIALELVSNPPIMFFDEPTSGLDsstcfqcIHLLKMLAAG-------GRTVICTIHQPsaRLFEMF--DQLYTLAD 260
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLD-------IDALRIVAEGvnklrspDRGILIITHYQ--RILDYIkpDFVHVLVD 216
|
250
....*....|....
gi 24580555 261 GQCVYQGsTKQLVP 274
Cdd:COG0396 217 GRIVKSG-GKELAL 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
49-273 |
5.15e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.92 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 49 HNLTYRVkegnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE------RNLSafR 122
Cdd:COG4604 5 KNVSKRY------GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD-SGEVLVDGLDvattpsRELA--K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 KLSayIM-QDNQLHGNLTVQEamTVAtnlklskkF-----SK----PEKHSMIDDILLTLSLSE--HRYTMTrnLSGGQK 190
Cdd:COG4604 76 RLA--ILrQENHINSRLTVRE--LVA--------FgrfpySKgrltAEDREIIDEAIAYLDLEDlaDRYLDE--LSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 191 KRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIH---QPSARLfemfDQLYTLADGQCVYQ 266
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHdinFASCYA----DHIVAMKDGRVVAQ 217
|
....*..
gi 24580555 267 GSTKQLV 273
Cdd:COG4604 218 GTPEEII 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
70-304 |
6.09e-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: 97.88 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 70 VSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNG-------AERNLSAFRKLSAYIMQDNQLHGNLTVQE 142
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGL-TRPDEGEIVLNGrtlfdsrKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 143 amtvatNLKLSKKFSKPEKHSMIDDILLTLSLSEH---RYTmtRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST 219
Cdd:TIGR02142 95 ------NLRYGMKRARPSERRISFERVIELLGIGHllgRLP--GRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 220 CFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQLYTLADGQCVYQGSTKQLvpfLSTLNLECPSyHNPASYVIEVSCG 299
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV---WASPDLPWLA-REDQGSLIEGVVA 242
|
....*
gi 24580555 300 EHGDH 304
Cdd:TIGR02142 243 EHDQH 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
63-268 |
6.62e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.47 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 63 AKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAFRKLSAYIMQDNQLHgnlTVQE 142
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ-SGTVFLGDKPISMLSSRQLARRLALLPQHH---LTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 143 AMTV--------ATNLKLSKKFSkPEKHSMID---DILLTLSLSEHRYTmtrNLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:PRK11231 90 GITVrelvaygrSPWLSLWGRLS-AEDNARVNqamEQTRINHLADRRLT---DLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 212 TSGLDSSTCFQCIHLLKMLAAGGRTVICTIH---QPSarlfEMFDQLYTLADGQCVYQGS 268
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQGT 221
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
67-242 |
6.62e-22 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 96.69 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERnLSAFRKLSAYIMQDNQlhgNLTVQEAMTV 146
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPT-SGTARVAGYDV-VREPRKVRRSIGIVPQ---YASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 147 ATNLKLSKKF---SKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQC 223
Cdd:TIGR01188 84 RENLEMMGRLyglPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170
....*....|....*....
gi 24580555 224 IHLLKMLAAGGRTVICTIH 242
Cdd:TIGR01188 164 WDYIRALKEEGVTILLTTH 182
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
66-273 |
8.69e-22 |
|
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: 94.91 E-value: 8.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNGA---ERNLSAFRKLSAYIMQDNQLHgnltvqe 142
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERF-YDPTSGEILLDGVdirDLNLRWLRSQIGLVSQEPVLF------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 143 AMTVATNLKLSKKFSKPE------KHSMIDDILLTLslsEHRY-TM----TRNLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:cd03249 90 DGTIAENIRYGKPDATDEeveeaaKKANIHDFIMSL---PDGYdTLvgerGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 212 TSGLDSSTCFQCIHLLKmLAAGGRTVICTIHQPSArlFEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:cd03249 167 TSALDAESEKLVQEALD-RAMKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
65-216 |
1.13e-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: 97.09 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 65 TILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG--------AERNLsafrklsAYIMQDNQLHG 136
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD-SGRILLDGrdvtglppEKRNV-------GMVFQDYALFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 NLTVQEamTVATNLKLsKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:COG3842 91 HLTVAE--NVAFGLRM-RGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-273 |
1.15e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.51 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 26 QIVPAQPKTL---QHLPKRPAVDLAFHNLTYRVKEGNRSnaktILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKT 102
Cdd:PRK11160 316 EITEQKPEVTfptTSTAAADQVSLTLNNVSFTYPDQPQP----VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 103 SSiEGSVTMNGaeRNLSAFRklsayimqDNQLHGNLTV--QE----AMTVATNLKLSKKFSKPEKHSmidDILLTLSLSE 176
Cdd:PRK11160 392 PQ-QGEILLNG--QPIADYS--------EAALRQAISVvsQRvhlfSATLRDNLLLAAPNASDEALI---EVLQQVGLEK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 177 HRYTMT----------RNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVICTIHqpsa 246
Cdd:PRK11160 458 LLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH---- 532
|
250 260
....*....|....*....|....*....
gi 24580555 247 RLFEM--FDQLYTLADGQCVYQGSTKQLV 273
Cdd:PRK11160 533 RLTGLeqFDRICVMDNGQIIEQGTHQELL 561
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
45-272 |
1.44e-21 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 99.65 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 45 DLAFHNLTYRVkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSIeGSVTMNG---AERNLSAF 121
Cdd:TIGR03797 451 AIEVDRVTFRY----RPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPES-GSVFYDGqdlAGLDVQAV 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 122 RKLSAYIMQDNQL-----------HGNLTVQEAMTVATNLKLSKKFSK-PEK-HSMIDDilltlslsehrytMTRNLSGG 188
Cdd:TIGR03797 526 RRQLGVVLQNGRLmsgsifeniagGAPLTLDEAWEAARMAGLAEDIRAmPMGmHTVISE-------------GGGTLSGG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 189 QKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVIC----TIHQPsarlfemfDQLYTLADGQCV 264
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKV-TRIVIAhrlsTIRNA--------DRIYVLDAGRVV 663
|
....*...
gi 24580555 265 YQGSTKQL 272
Cdd:TIGR03797 664 QQGTYDEL 671
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
62-272 |
2.17e-21 |
|
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: 93.40 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG----YKTSSIEGSVTMNGAER-----NLSAFRKLSAYIMQD- 131
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlIPGAPDEGEVLLDGKDIydldvDVLELRRRVGMVFQKp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 132 NQLHGnlTVQEamTVATNLKLSKKFSKPEKHSMIDDILLTLSLSE--HRYTMTRNLSGGQKKRLSIALELVSNPPIMFFD 209
Cdd:cd03260 91 NPFPG--SIYD--NVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANEPEVLLLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 210 EPTSGLDS-STcfQCIHLLKMLAAGGRTVICTIH--QPSARLfemFDQLYTLADGQCVYQGSTKQL 272
Cdd:cd03260 167 EPTSALDPiST--AKIEELIAELKKEYTIVIVTHnmQQAARV---ADRTAFLLNGRLVEFGPTEQI 227
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
67-238 |
2.23e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 94.03 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNGAE-RNLSAF--------RKLsayimqdnQlhgN 137
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITG-KTRPDSGSVLFGGTDlTGLDEHeiarlgigRKF--------Q---K 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 138 LTVQEAMTVATNLKLSKKFSK-----------PEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIM 206
Cdd:COG4674 94 PTVFEELTVFENLELALKGDRgvfaslfarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLL 173
|
170 180 190
....*....|....*....|....*....|...
gi 24580555 207 FFDEPTSGL-DSSTcFQCIHLLKMLaAGGRTVI 238
Cdd:COG4674 174 LLDEPVAGMtDAET-ERTAELLKSL-AGKHSVV 204
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
46-273 |
3.19e-21 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 93.06 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNG---AERNLSAF 121
Cdd:cd03251 1 VEFKNVTFRY----PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRfYDVDS--GRILIDGhdvRDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 122 RKLSAYIMQDNQL-HGnltvqeamTVATNLKLSKKFSKPEK----------HSMIDdilltlSLSEHRYTMT----RNLS 186
Cdd:cd03251 75 RRQIGLVSQDVFLfND--------TVAENIAYGRPGATREEveeaaraanaHEFIM------ELPEGYDTVIgergVKLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 187 GGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVICTIHQPSArlFEMFDQLYTLADGQCVYQ 266
Cdd:cd03251 141 GGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLST--IENADRIVVLEDGKIVER 217
|
....*..
gi 24580555 267 GSTKQLV 273
Cdd:cd03251 218 GTHEELL 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
62-216 |
6.00e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.77 E-value: 6.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTS--SIEGSVTMNGAERN-LSAFRKLSAYIMQDNQL--Hg 136
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafSASGEVLLNGRRLTaLPAEQRRIGILFQDDLLfpH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 nltvqeaMTVATNLK--LSKKFSKPEKHSMIDDILLTLSLS--EHRYTMTrnLSGGQKKRLSIALELVSNPPIMFFDEPT 212
Cdd:COG4136 91 -------LSVGENLAfaLPPTIGRAQRRARVEQALEEAGLAgfADRDPAT--LSGGQRARVALLRALLAEPRALLLDEPF 161
|
....
gi 24580555 213 SGLD 216
Cdd:COG4136 162 SKLD 165
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
63-219 |
6.04e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.00 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 63 AKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG-------AERnlsafrklsAYIMQDNQLH 135
Cdd:COG4525 19 PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS-SGEITLDGvpvtgpgADR---------GVVFQKDALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 136 GNLTVQEamTVATNLKLsKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGL 215
Cdd:COG4525 89 PWLNVLD--NVAFGLRL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGAL 165
|
....
gi 24580555 216 DSST 219
Cdd:COG4525 166 DALT 169
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
46-262 |
6.11e-21 |
|
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: 91.38 E-value: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNRSNAKTiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNGAErnlsAFRKLS 125
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFT-LKDINLEVPKGELVAIVGPVGSGKSSLLSALLG-ELEKLSGSVSVPGSI----AYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMqdnqlhgNLTVQEamtvatNLKLSKKFSKPEKHSMIDDILLT--LSLSEHRyTMTR------NLSGGQKKRLSIAL 197
Cdd:cd03250 75 PWIQ-------NGTIRE------NILFGKPFDEERYEKVIKACALEpdLEILPDG-DLTEigekgiNLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24580555 198 ELVSNPPIMFFDEPTSGLDSST----CFQCIhlLKMLaAGGRTVICTIHQPSarLFEMFDQLYTLADGQ 262
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVgrhiFENCI--LGLL-LNNKTRILVTHQLQ--LLPHADQIVVLDNGR 204
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
64-262 |
8.33e-21 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 91.16 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG--------AERNLsafrklsAYIMQDNQLH 135
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-SGRIYIGGrdvtdlppKDRDI-------AMVFQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 136 GNLTVQEAMtvATNLKLsKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGL 215
Cdd:cd03301 85 PHMTVYDNI--AFGLKL-RKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24580555 216 DSSTCFQC-IHLLKMLAAGGRTVICTIH-QPSArlFEMFDQLYTLADGQ 262
Cdd:cd03301 162 DAKLRVQMrAELKRLQQRLGTTTIYVTHdQVEA--MTMADRIAVMNDGQ 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
46-273 |
9.21e-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: 91.78 E-value: 9.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFR 122
Cdd:cd03252 1 ITFEHVRFRY----KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDGhdlALADPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 KLSAYIMQDNQLHGNltvqeamTVATNLKLSKKFSKPEK----HSMIDDILLTLSLSEHRYTMT----RNLSGGQKKRLS 194
Cdd:cd03252 76 RQVGVVLQENVLFNR-------SIRDNIALADPGMSMERvieaAKLAGAHDFISELPEGYDTIVgeqgAGLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24580555 195 IALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVICTIHQPSArlFEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLST--VKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
48-243 |
1.18e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 91.69 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTyrvkegNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSS----IEGSVTMNGAERNLSAFRK 123
Cdd:PRK09493 4 FKNVS------KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITsgdlIVDGLKVNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQDNQLHGNLTVQEamTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNP 203
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALE--NVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24580555 204 PIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQ 243
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
50-273 |
1.22e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.49 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEGNRSnaktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE---RNLSAFRKLSA 126
Cdd:PRK13647 9 DLHFRYKDGTKA-----LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ-RGRVKVMGREvnaENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 127 YIMQ--DNQLHGNlTVQEAMTVA-TNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNP 203
Cdd:PRK13647 83 LVFQdpDDQVFSS-TVWDDVAFGpVNMGLDKD----EVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 204 PIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLfEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
65-272 |
1.24e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 91.43 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 65 TILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAERN-LSAFRKLS---AYIMQDNQLHGNLT 139
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGlLPVKS--GSIRLDGEDITkLPPHERARagiAYVPQGREIFPRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEamtvatNLKLSKkFSKPEKHSMIDDILLTL--SLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:TIGR03410 92 VEE------NLLTGL-AALPRRSRKIPDEIYELfpVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 218 STCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:TIGR03410 165 SIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
48-272 |
2.48e-20 |
|
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: 90.36 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVKEGnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE---RNLSAFRKL 124
Cdd:cd03254 5 FENVNFSYDEK-----KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-KGQILIDGIDirdISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 125 SAYIMQDNQLHgnltvqeAMTVATNLKLSKKFSKPE------KHSMIDDILLtlSLSEHRYTMTR----NLSGGQKKRLS 194
Cdd:cd03254 79 IGVVLQDTFLF-------SGTIMENIRLGRPNATDEevieaaKEAGAHDFIM--KLPNGYDTVLGenggNLSQGERQLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 195 IALELVSNPPIMFFDEPTSGLDSSTcFQCIH--LLKMLAagGRTVICTIHQPSARLFEmfDQLYTLADGQCVYQGSTKQL 272
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTET-EKLIQeaLEKLMK--GRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEGTHDEL 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
48-284 |
3.62e-20 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 90.97 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVKEGNrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGA------ERNLSA 120
Cdd:TIGR04521 3 LKNVSYIYQPGT-PFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPTS--GTVTIDGRditakkKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQ--DNQLHGNlTVQEamTVA---TNLKLSKKfskpEKHSMIDDILLTLSLSEHryTMTRN---LSGGQKKR 192
Cdd:TIGR04521 80 LRKKVGLVFQfpEHQLFEE-TVYK--DIAfgpKNLGLSEE----EAEERVKEALELVGLDEE--YLERSpfeLSGGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 193 LSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLA-AGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTKQ 271
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSME-DVAEYADRVIVMHKGKIVLDGTPRE 229
|
250
....*....|....*.
gi 24580555 272 L---VPFLSTLNLECP 284
Cdd:TIGR04521 230 VfsdVDELEKIGLDVP 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
60-267 |
6.80e-20 |
|
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: 88.96 E-value: 6.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 60 RSNAKTI--LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERN---LSAFRKLSAyimqdnqL 134
Cdd:cd03266 12 RDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGFDVVkepAEARRRLGF-------V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 135 HGNLTVQEAMTVATNLKLSKKF---SKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLyglKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 212 TSGLDSSTCFQCIHLLKMLAAGGRTVICTIH--QPSARLfemFDQLYTLADGQCVYQG 267
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRALGKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
38-262 |
7.71e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 93.57 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 38 LPkRPAVDLAFHNLTYRVKEGNrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAER 116
Cdd:TIGR01842 310 LP-EPEGHLSVENVTIVPPGGK----KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGiWPPTS--GSVRLDGADL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 117 NLSAFRKLS---AYIMQDNQLHgnltvqeAMTVATNLKLSKKFSKPEK----------HSMIddilltLSLSEHRYTMT- 182
Cdd:TIGR01842 383 KQWDRETFGkhiGYLPQDVELF-------PGTVAENIARFGENADPEKiieaaklagvHELI------LRLPDGYDTVIg 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 183 ---RNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSarLFEMFDQLYTLA 259
Cdd:TIGR01842 450 pggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS--LLGCVDKILVLQ 527
|
...
gi 24580555 260 DGQ 262
Cdd:TIGR01842 528 DGR 530
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
64-244 |
1.53e-19 |
|
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: 87.16 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFRKLsAYIMQDNQLHGNLTV 140
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL-AGRVLLNGgplDFQRDSIARGL-LYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 QEamtvatNLKLSKKFSKPEKhsmIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTC 220
Cdd:cd03231 91 LE------NLRFWHADHSDEQ---VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....
gi 24580555 221 FQCIHLLKMLAAGGRTVICTIHQP 244
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-244 |
1.58e-19 |
|
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: 92.42 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 16 GTAGAGQLKAQIVPAQPKTLqhLPKRPavDLAFHNLTYRVKEGNRsnaktILKGVSGRLRSGELTAIMGPSGAGKSTLLN 95
Cdd:TIGR02868 309 EVLDAAGPVAEGSAPAAGAV--GLGKP--TLELRDLSAGYPGAPP-----VLDGVSLDLPPGERVAILGPSGSGKSTLLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 96 ILSGYkTSSIEGSVTMNG---AERNLSAFRKLSAYIMQDNQLHgnltvqeAMTVATNLKLSKKFSKPEK----------H 162
Cdd:TIGR02868 380 TLAGL-LDPLQGEVTLDGvpvSSLDQDEVRRRVSVCAQDAHLF-------DTTVRENLRLARPDATDEElwaalervglA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 163 SMIDDILLTLSLSEHryTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQcihLLKMLAAG--GRTVICT 240
Cdd:TIGR02868 452 DWLRALPDGLDTVLG--EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE---LLEDLLAAlsGRTVVLI 526
|
....
gi 24580555 241 IHQP 244
Cdd:TIGR02868 527 THHL 530
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
48-284 |
3.21e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.12 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE---RNLSAFRK 123
Cdd:PRK13632 10 VENVSFSY----PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQS--GEIKIDGITiskENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQ--DNQLHGnLTVQEamTVATNLKlSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVS 201
Cdd:PRK13632 84 KIGIIFQnpDNQFIG-ATVED--DIAFGLE-NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 202 NPPIMFFDEPTSGLD---SSTCFQCIHLLKmlAAGGRTVICTIHQPSARLfeMFDQLYTLADGQCVYQGSTKQLV---PF 275
Cdd:PRK13632 160 NPEIIIFDESTSMLDpkgKREIKKIMVDLR--KTRKKTLISITHDMDEAI--LADKVIVFSEGKLIAQGKPKEILnnkEI 235
|
....*....
gi 24580555 276 LSTLNLECP 284
Cdd:PRK13632 236 LEKAKIDSP 244
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
48-228 |
3.36e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.47 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNL--TYRVKegnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG------AERNLS 119
Cdd:PRK11153 4 LKNIskVFPQG----GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPT-SGRVLVDGqdltalSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 120 AFRKLSAYIMQdnqlHGNL----TVQEamTVATNLKLSKKfSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSI 195
Cdd:PRK11153 79 KARRQIGMIFQ----HFNLlssrTVFD--NVALPLELAGT-PKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190
....*....|....*....|....*....|...
gi 24580555 196 ALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLK 228
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLK 184
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
64-216 |
4.35e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 87.00 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFRKLSAYIMQDNQLHGNLTV 140
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT-SGEVRVAGlvpWKRRKKFLRRIGVVFGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 141 QEAMTVatnLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:cd03267 113 IDSFYL---LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
66-243 |
7.61e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.95 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAFRKLSAYIMQDNQL----------- 134
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPS-EGSIVVNGQTINLVRDKDGQLKVADKNQLrllrtrltmvf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 135 -HGNLtvQEAMTVATN--------LKLSKKFSKPEKHSMIDDILLTLSlSEHRYTMtrNLSGGQKKRLSIALELVSNPPI 205
Cdd:PRK10619 99 qHFNL--WSHMTVLENvmeapiqvLGLSKQEARERAVKYLAKVGIDER-AQGKYPV--HLSGGQQQRVSIARALAMEPEV 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 24580555 206 MFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQ 243
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
66-244 |
8.28e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 8.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILsGY--KTSSIEGSV------TMNGAErnLSAFRKLS-AYIMQDNQLHG 136
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNIL-GCldKPTSGTYRVagqdvaTLDADA--LAQLRREHfGFIFQRYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 NLTVQEAMTV-ATNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGL 215
Cdd:PRK10535 100 HLTAAQNVEVpAVYAGLERK----QRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180
....*....|....*....|....*....
gi 24580555 216 DSSTCFQCIHLLKMLAAGGRTVICTIHQP 244
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
46-230 |
8.77e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.02 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNRSNakTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERN-LSAFRKL 124
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQT--DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT-SGDVIFNGQPMSkLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 125 S------AYIMQDNQLHGNLTVQEamTVATNLKLSKKfsKP-EKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIAL 197
Cdd:PRK11629 83 ElrnqklGFIYQFHHLLPDFTALE--NVAMPLLIGKK--KPaEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190
....*....|....*....|....*....|...
gi 24580555 198 ELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKML 230
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGEL 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
67-272 |
1.27e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLS----AFRKLSAYIMQDNQLHGNLTVQE 142
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD-SGEILLDGEPVRFRsprdAQAAGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 143 amtvatNLKLSKkfsKPEKHSMID---------DILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTS 213
Cdd:COG1129 99 ------NIFLGR---EPRRGGLIDwramrrrarELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 214 GLDSStcfQCIHLLKM---LAAGGRTVICTIHqpsaRLFEMF---DQLYTLADGQCVYQGSTKQL 272
Cdd:COG1129 170 SLTER---EVERLFRIirrLKAQGVAIIYISH----RLDEVFeiaDRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
46-272 |
1.36e-18 |
|
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: 85.82 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFR 122
Cdd:cd03295 1 IEFENVTKRYGGG-----KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPT-SGEIFIDGediREQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 KLSAYIMQDNQLHGNLTVQEamTVATNLKLsKKFSKPEKHSMIDDILLTLSLSE----HRYTmtRNLSGGQKKRLSIALE 198
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEE--NIALVPKL-LKWPKEKIRERADELLALVGLDPaefaDRYP--HELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 199 LVSNPPIMFFDEPTSGLDSSTCFQC----IHLLKMLaagGRTVICTIHQpsarLFEMF---DQLYTLADGQCVYQGSTKQ 271
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLqeefKRLQQEL---GKTIVFVTHD----IDEAFrlaDRIAIMKNGEIVQVGTPDE 222
|
.
gi 24580555 272 L 272
Cdd:cd03295 223 I 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
61-285 |
1.63e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 61 SNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFRKLSAYIMQ--DNQLH 135
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT-SGSVLIRGepiTKENIREVRKFVGLVFQnpDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 136 GNLTVQEAMTVATNLKLSKKfskPEKHSmIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGL 215
Cdd:PRK13652 93 SPTVEQDIAFGPINLGLDEE---TVAHR-VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 216 DSSTCFQCIHLLKMLAAG-GRTVICTIHQPSArLFEMFDQLYTLADGQCVYQGSTKQLV---PFLSTLNLECPS 285
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTVEEIFlqpDLLARVHLDLPS 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
66-277 |
2.17e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.06 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLS---------AFRKLSAYIMQDNQLHG 136
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPD-SGQLNIAGHQFDFSqkpsekairLLRQKVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 NLTVQEAMTVA--TNLKLSKKFSKPEKhsmiDDILLTLSLSE--HRYTMtrNLSGGQKKRLSIALELVSNPPIMFFDEPT 212
Cdd:COG4161 96 HLTVMENLIEApcKVLGLSKEQAREKA----MKLLARLRLTDkaDRFPL--HLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 213 SGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPS-ARlfEMFDQLYTLADGQCVYQG--------STKQLVPFLS 277
Cdd:COG4161 170 AALDPEITAQVVEIIRELSQTGITQVIVTHEVEfAR--KVASQVVYMEKGRIIEQGdashftqpQTEAFAHYLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
76-240 |
2.58e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 76 SGELTAIMGPSGAGKSTLLNIL-------SGykTSSIEGS---VTMNGAERNLSAFRKLSAYIMQDNQLHGNLTVQEAMT 145
Cdd:PRK11124 27 QGETLVLLGPSGAGKSSLLRVLnllemprSG--TLNIAGNhfdFSKTPSDKAIRELRRNVGMVFQQYNLWPHLTVQQNLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 146 VATNLKLskKFSKPEKHSMIDDILLTLSLSEH--RYTMtrNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQC 223
Cdd:PRK11124 105 EAPCRVL--GLSKDQALARAEKLLERLRLKPYadRFPL--HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQI 180
|
170
....*....|....*...
gi 24580555 224 IHLLKMLAAGGRT-VICT 240
Cdd:PRK11124 181 VSIIRELAETGITqVIVT 198
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
28-273 |
2.88e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.75 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 28 VPAQPKTLQHLPKRPAVDLAFHNLTYRVKEGnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYktSSIEG 107
Cdd:PRK11174 332 LAHPQQGEKELASNDPVTIEAEDLEILSPDG-----KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPYQG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 108 SVTMNGAER---NLSAFRKLSAYIMQDNQL-HGnltvqeamTVATNLKLSKKFSKPE------KHSMIDDILLTLSLSEH 177
Cdd:PRK11174 405 SLKINGIELrelDPESWRKHLSWVGQNPQLpHG--------TLRDNVLLGNPDASDEqlqqalENAWVSEFLPLLPQGLD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 178 RYTMTRN--LSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTiHQPSArLFEMfDQL 255
Cdd:PRK11174 477 TPIGDQAagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQLED-LAQW-DQI 553
|
250
....*....|....*...
gi 24580555 256 YTLADGQCVYQGSTKQLV 273
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELS 571
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
46-268 |
3.63e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.06 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG-----AERNLSA 120
Cdd:PRK13638 2 LATSDLWFRYQD------EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ-KGAVLWQGkpldySKRGLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQDnqlhgnltvQEAMTVATNLKLSKKFS-------KPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRL 193
Cdd:PRK13638 75 LRQQVATVFQD---------PEQQIFYTDIDSDIAFSlrnlgvpEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 194 SIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSArLFEMFDQLYTLADGQCVYQGS 268
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGA 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
67-294 |
3.64e-18 |
|
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: 84.05 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAFRKLsaYIMQDNQLHGNLTVQEAMTV 146
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPT-SGGVILEGKQITEPGPDRM--VVFQNYSLLPWLTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 147 ATNlKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST--CFQcI 224
Cdd:TIGR01184 78 AVD-RVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTrgNLQ-E 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 225 HLLKMLAAGGRTVICTIHQPSARLFeMFDQLYTLADGQCVYQGSTKQlVPFLSTLN----LECPSYHNPASYVI 294
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALL-LSDRVVMLTNGPAANIGQILE-VPFPRPRDrlevVEDPSYYDLRNEAL 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-271 |
4.06e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 88.27 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 28 VPAQPKTLQhLPkRPAVDLAFHNLTYRVKEGNRsnakTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSie 106
Cdd:COG4618 315 VPAEPERMP-LP-RPKGRLSVENLTVVPPGSKR----PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGvWPPTA-- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 107 GSVTMNGAE-RNLS--AFRKLSAYIMQDNQLHgnltvqeAMTVATNLklsKKFSK--PEK----------HSMIddillt 171
Cdd:COG4618 387 GSVRLDGADlSQWDreELGRHIGYLPQDVELF-------DGTIAENI---ARFGDadPEKvvaaaklagvHEMI------ 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 172 LSLsEHRYTmTR------NLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPS 245
Cdd:COG4618 451 LRL-PDGYD-TRigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS 528
|
250 260
....*....|....*....|....*.
gi 24580555 246 ArLFEMfDQLYTLADGQCVYQGSTKQ 271
Cdd:COG4618 529 L-LAAV-DKLLVLRDGRVQAFGPRDE 552
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
48-216 |
4.30e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVkegnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNGAERnlsafrklSAY 127
Cdd:COG0488 1 LENLSKSF------GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-ELEPDSGEVSIPKGLR--------IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 128 IMQDNQLHGNLTV-QEAMTVATNL--------KLSKKFSKPEK--------------------HSMIDDILLTLSLSEHR 178
Cdd:COG0488 66 LPQEPPLDDDLTVlDTVLDGDAELraleaeleELEAKLAEPDEdlerlaelqeefealggweaEARAEEILSGLGFPEED 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 24580555 179 YTM-TRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:COG0488 146 LDRpVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
65-217 |
4.96e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.97 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 65 TILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG--AERNLSAFRKLSAYIMQDNQL--Hgnltv 140
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPD-SGRIVLNGrdLFTNLPPRERRVGFVFQHYALfpH----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 qeaMTVATN----LKlSKKFSKPEKHSMIDDILLTLSLS--EHRYtmTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSG 214
Cdd:COG1118 90 ---MTVAENiafgLR-VRPPSKAEIRARVEELLELVQLEglADRY--PSQLSGGQRQRVALARALAVEPEVLLLDEPFGA 163
|
...
gi 24580555 215 LDS 217
Cdd:COG1118 164 LDA 166
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
46-273 |
8.75e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 8.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNG---AERNLSAFR 122
Cdd:PRK13537 8 IDFRNVEKRYGD------KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL-THPDAGSISLCGepvPSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 KLSAYIMQDNqLHGNLTVQEAMTVatnlkLSKKF--SKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELV 200
Cdd:PRK13537 81 RVGVVPQFDN-LDPDFTVRENLLV-----FGRYFglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24580555 201 SNPPIMFFDEPTSGLDSstcfQCIHL----LKMLAAGGRTVICTIH--QPSARLfemFDQLYTLADGQCVYQGSTKQLV 273
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDP----QARHLmwerLRSLLARGKTILLTTHfmEEAERL---CDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
67-217 |
9.87e-18 |
|
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: 83.16 E-value: 9.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLSAYIMQDNQLHGNLTVQEamT 145
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD-SGTILFGGEDaTDVPVQERNVGFVFQHYALFRHMTVFD--N 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24580555 146 VATNLKLSKKFSKPEKHSM---IDDILLTLSLS--EHRYtmTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:cd03296 95 VAFGLRVKPRSERPPEAEIrakVHELLKLVQLDwlADRY--PAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
43-273 |
1.57e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 43 AVDLAFHNLTYRvkegnrsnAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNGAE--RNLSA 120
Cdd:PRK13536 41 AIDLAGVSKSYG--------DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGM-TSPDAGKITVLGVPvpARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQDNQLHGNLTVQEAMTVatnlkLSKKF--SKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALE 198
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVRENLLV-----FGRYFgmSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24580555 199 LVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIH--QPSARLfemFDQLYTLADGQCVYQGSTKQLV 273
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
66-272 |
2.05e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.27 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG----YKTSSIEGSVTMNGAE---RNLSAFRKLSAYIMQDNQLHGNL 138
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGQDifkMDVIELRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 139 TVQEamTVATNLKLSKKF-SKPEKHSMIDDILLTLSLSEHRYTM----TRNLSGGQKKRLSIALELVSNPPIMFFDEPTS 213
Cdd:PRK14247 98 SIFE--NVALGLKLNRLVkSKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 214 GLDSSTCFQcIHLLKMLAAGGRTVICTIHQP--SARLFEMFDQLYTladGQCVYQGSTKQL 272
Cdd:PRK14247 176 NLDPENTAK-IESLFLELKKDMTIVLVTHFPqqAARISDYVAFLYK---GQIVEWGPTREV 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
64-261 |
2.11e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG-------AERnlsafrklsAYIMQDNQLHG 136
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGkpvegpgAER---------GVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 NLTVQEamTVATNLKLSkKFSKPEKHSMIDDILLTLSLS--EHRYTMtrNLSGGQKKRLSIALELVSNPPIMFFDEPTSG 214
Cdd:PRK11248 84 WRNVQD--NVAFGLQLA-GVEKMQRLEIAHQMLKKVGLEgaEKRYIW--QLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24580555 215 LDSSTCFQCIH-LLKMLAAGGRTVICTIHQPSARLFeMFDQLYTLADG 261
Cdd:PRK11248 159 LDAFTREQMQTlLLKLWQETGKQVLLITHDIEEAVF-MATELVLLSPG 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
55-271 |
2.54e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 2.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 55 VKEGNRsnaktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGykTSSIEGSVTMNGaeRNLSAF--RKLS---AYIM 129
Cdd:COG4138 6 VAVAGR------LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG--LLPGQGEILLNG--RPLSDWsaAELArhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 130 QDNQLHGNLTVQEAMTvatnLKLSKKFSKPEKHSMIDDILLTLSLSE--HRytMTRNLSGGQKKRLSIA---LEL--VSN 202
Cdd:COG4138 76 QQQSPPFAMPVFQYLA----LHQPAGASSEAVEQLLAQLAEALGLEDklSR--PLTQLSGGEWQRVRLAavlLQVwpTIN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 203 PP--IMFFDEPTSGLDsstcfqcIH-------LLKMLAAGGRTVICTIHQPSARLFEMfDQLYTLADGQCVYQGSTKQ 271
Cdd:COG4138 150 PEgqLLLLDEPMNSLD-------VAqqaaldrLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASGETAE 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
39-219 |
2.82e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.78 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 39 PKRPAVDLAFHNLTYRVkeGNRSNAktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNIL-------SGykTSSIEGsvtM 111
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSY--DNSRQG---VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSG--RILIDG---T 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 112 NGAERNLSAFRKLSAYIMQDNQLHgNLTVQEAMTV----ATNLKLSKKFSKPEKHSMIDDilltlslSEHRY-TMT---- 182
Cdd:PRK13657 398 DIRTVTRASLRRNIAVVFQDAGLF-NRSIEDNIRVgrpdATDEEMRAAAERAQAHDFIER-------KPDGYdTVVgerg 469
|
170 180 190
....*....|....*....|....*....|....*..
gi 24580555 183 RNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST 219
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
50-268 |
3.12e-17 |
|
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: 80.65 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSIEGSVTMNGaeRNLSafrklsayi 128
Cdd:cd03217 5 DLHVSVGG------KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhPKYEVTEGEILFKG--EDIT--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 129 mqdnqlhgNLTVQE----AMTVAtnlklskkFSKPEKHSMIDDILLTLSLSEhrytmtrNLSGGQKKRLSIALELVSNPP 204
Cdd:cd03217 68 --------DLPPEErarlGIFLA--------FQYPPEIPGVKNADFLRYVNE-------GFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 205 IMFFDEPTSGLDsstcfqcIHLLKMLAAG-------GRTVICTIHQpsARLFEMF--DQLYTLADGQCVYQGS 268
Cdd:cd03217 125 LAILDEPDSGLD-------IDALRLVAEVinklreeGKSVLIITHY--QRLLDYIkpDRVHVLYDGRIVKSGD 188
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
62-267 |
3.54e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 81.54 E-value: 3.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSI-EGSVTMNGAerNLSAFR-----KLSAYI-MQDNQL 134
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVtSGTILFKGQ--DLLELEpderaRAGLFLaFQYPEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 135 HGNLTVQEAMTVATNLKLSKKFSKPEK----HSMIDDILLTLSLSE---HRYtMTRNLSGGQKKRLSIALELVSNPPIMF 207
Cdd:TIGR01978 89 IPGVSNLEFLRSALNARRSARGEEPLDlldfEKLLKEKLALLDMDEeflNRS-VNEGFSGGEKKRNEILQMALLEPKLAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24580555 208 FDEPTSGLDsstcfqcIHLLKMLAAG-------GRTVICTIHQPsaRLFEMF--DQLYTLADGQCVYQG 267
Cdd:TIGR01978 168 LDEIDSGLD-------IDALKIVAEGinrlrepDRSFLIITHYQ--RLLNYIkpDYVHVLLDGRIVKSG 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
64-273 |
4.86e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSsIEGSVTMNGAERNLSAFRKLSAYI---MQDNQLHGNLTV 140
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP-AHGHVWLDGEHIQHYASKEVARRIgllAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 QEAMTVA--TNLKLSKKFSKpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSS 218
Cdd:PRK10253 99 QELVARGryPHQPLFTRWRK-EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 219 TCFQCIHLLKML-AAGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:PRK10253 178 HQIDLLELLSELnREKGYTLAAVLHDLN-QACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
65-264 |
5.11e-17 |
|
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: 79.01 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 65 TILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNlsafrklsayimqdnqlhgNLTVQEAM 144
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-SGEILVDGKEVS-------------------FASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 145 tvatnlklskkfskpekhsmiddilltlslsEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCI 224
Cdd:cd03216 74 -------------------------------RAGIAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24580555 225 HLLKMLAAGGRTVICTIHqpsaRLFEMF---DQLYTLADGQCV 264
Cdd:cd03216 123 KVIRRLRAQGVAVIFISH----RLDEVFeiaDRVTVLRDGRVV 161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
67-264 |
5.14e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.58 E-value: 5.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAERNLS----AFRKLSAYIMQDNQLhgnltVQ 141
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGnYQPDA--GSILIDGQEMRFAsttaALAAGVAIIYQELHL-----VP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EaMTVATNLKLSKkfsKPEKHSMID---------DILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPT 212
Cdd:PRK11288 93 E-MTVAENLYLGQ---LPHKGGIVNrrllnyearEQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 213 SGLDSSTCFQCIHLLKMLAAGGRTVICTIHqpsaRLFEMF---DQLYTLADGQCV 264
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSH----RMEEIFalcDAITVFKDGRYV 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
82-297 |
6.98e-17 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 82.16 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 82 IMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLSAYIMQDNQLHGNLTVQEamTVATNLKLsKKFSKPE 160
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD-SGSIMLDGEDvTNVPPHLRHINMVFQSYALFPHMTVEE--NVAFGLKM-RKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 161 KHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVIC 239
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFVF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 240 TIHQPSARLfEMFDQLYTLADGQCVYQGSTKQLvpflstlnLECPSYHNPASYVIEVS 297
Cdd:TIGR01187 157 VTHDQEEAM-TMSDRIAIMRKGKIAQIGTPEEI--------YEEPANLFVARFIGEIN 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
64-284 |
9.54e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.00 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGY--KTSSIEGSVTMNG---AERNLSAFRKLSAYIMQ--DNQLHG 136
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllPDDNPNSKITVDGitlTAKTVWDIREKVGIVFQnpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 nLTVQEamTVATNLKlSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK13640 100 -ATVGD--DVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 217 SSTCFQCIHLLKMLAA-GGRTVICTIHQPSARlfEMFDQLYTLADGQCVYQGSTKQLVP---FLSTLNLECP 284
Cdd:PRK13640 176 PAGKEQILKLIRKLKKkNNLTVISITHDIDEA--NMADQVLVLDDGKLLAQGSPVEIFSkveMLKEIGLDIP 245
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
64-216 |
1.00e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.07 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNG-----------AERNL-------SAFRKLs 125
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVG-LVKPDSGRIFLDGedithlpmhkrARLGIgylpqeaSIFRKL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 ayimqdnqlhgnltvqeamTVATNLKL---SKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSN 202
Cdd:COG1137 94 -------------------TVEDNILAvleLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170
....*....|....
gi 24580555 203 PPIMFFDEPTSGLD 216
Cdd:COG1137 155 PKFILLDEPFAGVD 168
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
70-304 |
1.04e-16 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 82.07 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 70 VSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG-------AERNLSAFRKLSAYIMQDNQLHGNLTVQE 142
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD-SGRIRLGGevlqdsaRGIFLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 143 amtvatNLKLSKKFS-KPEKHSMIDDILLTLSLSE--HRYtmTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST 219
Cdd:COG4148 97 ------NLLYGRKRApRAERRISFDEVVELLGIGHllDRR--PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 220 CFQCIHLLKMLAAGGRTVICTI-HQPS--ARLfemFDQLYTLADGQCVYQGSTKQLvpfLSTLNLECPSYHNPASYVIEV 296
Cdd:COG4148 169 KAEILPYLERLRDELDIPILYVsHSLDevARL---ADHVVLLEQGRVVASGPLAEV---LSRPDLLPLAGGEEAGSVLEA 242
|
....*...
gi 24580555 297 SCGEHGDH 304
Cdd:COG4148 243 TVAAHDPD 250
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
30-273 |
1.67e-16 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 83.64 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 30 AQPKTLQHLPKRpAVDLAFHNLTYRVKEgnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSV 109
Cdd:TIGR01846 441 PRSAGLAALPEL-RGAITFENIRFRYAP----DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQ-HGQV 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 110 TMNG---AERNLSAFRKLSAYIMQDNQLHGNltvqeamTVATNLKLSKKfSKPEKHSM-------IDDILLTL------S 173
Cdd:TIGR01846 515 LVDGvdlAIADPAWLRRQMGVVLQENVLFSR-------SIRDNIALCNP-GAPFEHVIhaaklagAHDFISELpqgyntE 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 174 LSEHrytmTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVICTIHQPSArlFEMFD 253
Cdd:TIGR01846 587 VGEK----GANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLST--VRACD 659
|
250 260
....*....|....*....|
gi 24580555 254 QLYTLADGQCVYQGSTKQLV 273
Cdd:TIGR01846 660 RIIVLEKGQIAESGRHEELL 679
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
64-216 |
2.00e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.53 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLSAYIMQDNQLHGNLTVQE 142
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-SGRIMLDGQDiTHVPAENRHVNTVFQSYALFPHMTVFE 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 143 amTVATNLKLsKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK09452 106 --NVAFGLRM-QKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-223 |
2.24e-16 |
|
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: 78.67 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 32 PKTLQHLPKrpavdlaFHNLTYRVKegNRSnAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNIL-------------- 97
Cdd:cd03248 5 PDHLKGIVK-------FQNVTFAYP--TRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqggqvlld 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 98 ----SGYKTSSIEGSVTMNGAERNLSAfRKLsayimQDNQLHGnltvqeaMTVATNLKLSKKFSKPEKHSMIddilltlS 173
Cdd:cd03248 75 gkpiSQYEHKYLHSKVSLVGQEPVLFA-RSL-----QDNIAYG-------LQSCSFECVKEAAQKAHAHSFI-------S 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 174 LSEHRYTMT-----RNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQC 223
Cdd:cd03248 135 ELASGYDTEvgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
67-272 |
2.46e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.67 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKT--SSIEGSVTMNG--------AERNLSAFRKLSAYIMQDNQLHG 136
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGSHIELLGrtvqregrLARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 NLTVQE-----AMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:PRK09984 100 RLSVLEnvligALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 212 TSGLDSSTCFQCIHLLKML-AAGGRTVICTIHQPSARLfEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:PRK09984 180 IASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
37-267 |
2.80e-16 |
|
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: 78.34 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 37 HLPKRPAVDLAFHNLTYRVKEGNRsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGae 115
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGE---FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPDS--GTVTVRG-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 116 rnlsafrKLSAYIMQDNQLHGNLTVQEamtvatNLKLS---KKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKR 192
Cdd:cd03220 84 -------RVSSLLGLGGGFNPELTGRE------NIYLNgrlLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24580555 193 LSIALELVSNPPIMFFDEPTSGLDSStcFQ--CIHLLKMLAAGGRTVICTIHQPSArLFEMFDQLYTLADGQCVYQG 267
Cdd:cd03220 151 LAFAIATALEPDILLIDEVLAVGDAA--FQekCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
51-242 |
2.89e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 51 LTYRvkegnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNGAERNLSAFRKLSAYIMQ 130
Cdd:PRK15056 14 VTWR-------NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGF-VRLASGKISILGQPTRQALQKNLVAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 131 DNQLHGNLTVQEAMTVAT----NLKLSKKfSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIM 206
Cdd:PRK15056 86 SEEVDWSFPVLVEDVVMMgrygHMGWLRR-AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 24580555 207 FFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIH 242
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTH 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
78-243 |
3.07e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 83.52 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 78 ELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA--ERNLSAFRKLSAYIMQDNQLHGNLTVQEAMTVATNLK-LSK 154
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPT-SGTVLVGGKdiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKgRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 155 KFSKPEKHSMIDDIlltlSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTcFQCIHLLKMLAAGG 234
Cdd:TIGR01257 1036 EEAQLEMEAMLEDT----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS-RRSIWDLLLKYRSG 1110
|
....*....
gi 24580555 235 RTVICTIHQ 243
Cdd:TIGR01257 1111 RTIIMSTHH 1119
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
58-218 |
3.23e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.22 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 58 GNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNG---AERNLSAFRKLSAYIMQDNQL 134
Cdd:PRK10247 14 GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASL-ISPTSGTLLFEGediSTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 135 HGNltvqeamTVATNLKLSKKFSK--PEKHSMIDDiLLTLSLSEHryTMTRN---LSGGQKKRLSIALELVSNPPIMFFD 209
Cdd:PRK10247 93 FGD-------TVYDNLIFPWQIRNqqPDPAIFLDD-LERFALPDT--ILTKNiaeLSGGEKQRISLIRNLQFMPKVLLLD 162
|
....*....
gi 24580555 210 EPTSGLDSS 218
Cdd:PRK10247 163 EITSALDES 171
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
46-262 |
3.27e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA------ERNLS 119
Cdd:PRK10584 7 VEVHHLKKSVGQGE--HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS-SGEVSLVGQplhqmdEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 120 AFR-KLSAYIMQDNQLHGNLTVQEAMTVATnlkLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALE 198
Cdd:PRK10584 84 KLRaKHVGFVFQSFMLIPTLNALENVELPA---LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 199 LVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQPsaRLFEMFDQLYTLADGQ 262
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL--QLAARCDRRLRLVNGQ 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
65-261 |
3.48e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 65 TILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG-AERNLSAfRKLS---AYIMQDNQLHGNLTV 140
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGdDVEALSA-RAASrrvASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 QEAMTVATNLKLSKkFSK--PEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSS 218
Cdd:PRK09536 95 RQVVEMGRTPHRSR-FDTwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24580555 219 TCFQCIHLLKMLAAGGRTVICTIH--QPSARLfemFDQLYTLADG 261
Cdd:PRK09536 174 HQVRTLELVRRLVDDGKTAVAAIHdlDLAARY---CDELVLLADG 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
67-216 |
5.25e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.75 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG--YKTSsieGSVTMNGAE--RNLSAFRKLSAYIM-QDNQLHGNLTVQ 141
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilVPTS---GEVRVLGYVpfKRRKEFARRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 142 EamtvatNLKLSK---KFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:COG4586 115 D------SFRLLKaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
39-268 |
5.86e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.51 E-value: 5.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 39 PKRPAVD---LAFHNLTYRVKEgNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLN-----ILSGYKTSSIE---- 106
Cdd:PRK13631 12 VPNPLSDdiiLRVKNLYCVFDE-KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGdiyi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 107 ------GSVTMNGAERNLSAF---RKLSAYIMQ--DNQLHGNLTVQEAMTVATNLKLSKKfskpEKHSMIDDILLTLSLS 175
Cdd:PRK13631 91 gdkknnHELITNPYSKKIKNFkelRRRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKKS----EAKKLAKFYLNKMGLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 176 EHryTMTRN---LSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQpSARLFEMF 252
Cdd:PRK13631 167 DS--YLERSpfgLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVA 243
|
250
....*....|....*.
gi 24580555 253 DQLYTLADGQCVYQGS 268
Cdd:PRK13631 244 DEVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
48-242 |
6.00e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 78.72 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVKEGNRSNAKTiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGY-KTSS----IEG-SVTMNGAERNLSAF 121
Cdd:PRK13641 5 FENVDYIYSPGTPMEKKG-LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALlKPSSgtitIAGyHITPETGNKNLKKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 122 RKLSAYIMQ--DNQLHGNLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRytmTRNLSGGQKKRLSIALEL 199
Cdd:PRK13641 84 RKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKS---PFELSGGQMRRVAIAGVM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24580555 200 VSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIH 242
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
64-272 |
9.56e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.23 E-value: 9.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTL----LNILSGYktssiEGSVTMNGAERNLSAFRKLsAYIMQDNQLHGNLT 139
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTiriiLGILAPD-----SGEVLWDGEPLDPEDRRRI-GYLPEERGLYPKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEAMTVATNLK-LSKKFSKPEkhsmIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSs 218
Cdd:COG4152 88 VGEQLVYLARLKgLSKAEAKRR----ADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 219 tcfqcI------HLLKMLAAGGRTVICTIHQ-PSARlfEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:COG4152 163 -----VnvellkDVIRELAAKGTTVIFSSHQmELVE--ELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-273 |
1.09e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 35 LQHLPKRPAVDLAFHNLTYRVKegnrsnAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG- 113
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVP------GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-EGEILLDAq 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 114 --AERNLSAFRKLSAYIMQdnqlhgNLTVQEAMTVATNLKLSK--------KFSKpEKHSMIDDILLTLSLSEHRYTMTR 183
Cdd:PRK10575 74 plESWSSKAFARKVAYLPQ------QLPAAEGMTVRELVAIGRypwhgalgRFGA-ADREKVEEAISLVGLKPLAHRLVD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 184 NLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLA-AGGRTVICTIH--QPSARlfeMFDQLYTLAD 260
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHdiNMAAR---YCDYLVALRG 223
|
250
....*....|...
gi 24580555 261 GQCVYQGSTKQLV 273
Cdd:PRK10575 224 GEMIAQGTPAELM 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
59-272 |
1.11e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 59 NRSNaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFRKLSAYIMQDNQLH 135
Cdd:TIGR00958 490 NRPD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT-GGQVLLDGvplVQYDHHYLHRQVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 136 GNlTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLslsEHRYTMT-----RNLSGGQKKRLSIALELVSNPPIMFFDE 210
Cdd:TIGR00958 568 SG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEF---PNGYDTEvgekgSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 211 PTSGLDSstcfQCIHLLKML-AAGGRTVICTIHQPSarLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:TIGR00958 644 ATSALDA----ECEQLLQESrSRASRTVLLIAHRLS--TVERADQILVLKKGSVVEMGTHKQL 700
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
62-219 |
1.40e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.43 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAER-NLSAFRKlSAYI---MQDNQL-- 134
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGsLPPDS--GSILIDGKDVtKLPEYKR-AKYIgrvFQDPMMgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 135 HGNLTVQEAMTVATNLKLSKKFSKPEKHSMID---DILLTLSLS-EHR-YTMTRNLSGGQKKRLSIALELVSNPPIMFFD 209
Cdd:COG1101 94 APSMTIEENLALAYRRGKRRGLRRGLTKKRRElfrELLATLGLGlENRlDTKVGLLSGGQRQALSLLMATLTKPKLLLLD 173
|
170
....*....|
gi 24580555 210 EPTSGLDSST 219
Cdd:COG1101 174 EHTAALDPKT 183
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
64-216 |
1.59e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNgaeRNLSafrklSAYIMQDN-QLHGNLTVQE 142
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTVKLG---ETVK-----IGYFDQHQeELDPDKTVLD 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 143 AMTvatnlKLSKKFSKPEKHSMIDDILLTlslSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:COG0488 399 ELR-----DGAPGGTEQEVRGYLGRFLFS---GDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD 464
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
67-270 |
1.88e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAERNlSAFRKLSA-----YIMQDNQLHGNLTV 140
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGiHEPTK--GTITINNINYN-KLDHKLAAqlgigIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 QEAMTVAtNLKLSKKFSKP-----EKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGL 215
Cdd:PRK09700 98 LENLYIG-RHLTKKVCGVNiidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 216 DSSTCFQCIHLLKMLAAGGRTVICTIHQpSARLFEMFDQLYTLADGQCVYQGSTK 270
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
48-268 |
1.94e-15 |
|
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: 75.99 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILsgYKTSSI-EGSVTMNG---AERNLSAFRK 123
Cdd:cd03244 5 FKNVSLRY----RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLAL--FRLVELsSGSILIDGvdiSKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQDNQLhgnltvqEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTM-------TRNLSGGQKKRLSIA 196
Cdd:cd03244 79 RISIIPQDPVL-------FSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLdtvveegGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 197 LELVSNPPIMFFDEPTSGLDSSTcFQCIHLLKMLAAGGRTVICTIHqpsaRLFEM--FDQLYTLADGQCVYQGS 268
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPET-DALIQKTIREAFKDCTVLTIAH----RLDTIidSDRILVLDKGRVVEFDS 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
64-273 |
2.15e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAF----RKLSAYIMQDNQLHGNLT 139
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD-AGNIIIDDEDISLLPLharaRRGIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEAMTVAtnLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST 219
Cdd:PRK10895 95 VYDNLMAV--LQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24580555 220 CFQCIHLLKMLAAGGRTVICTIHQPSARLfEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:PRK10895 173 VIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
50-241 |
2.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 76.66 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEGNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA----ERNLSAFRKLS 125
Cdd:PRK13633 9 NVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPS-EGKVYVDGLdtsdEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQ--DNQLHGNLTVQEAMTVATNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNP 203
Cdd:PRK13633 88 GMVFQnpDNQIVATIVEEDVAFGPENLGIPPE----EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 24580555 204 PIMFFDEPTSGLDSStcfqcihllkmlaaGGRTVICTI 241
Cdd:PRK13633 164 ECIIFDEPTAMLDPS--------------GRREVVNTI 187
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
66-242 |
4.16e-15 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 75.61 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLL---NILsgyKTSSiEGSVTMNGAERNLSAFRKLSAYIMQDNQL-------- 134
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFLrciNLL---ETPD-SGEIRVGGEEIRLKPDRDGELVPADRRQLqrirtrlg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 135 ----HGNLTVQeaMTVATN--------LKLSKKFSKPEKHSMIDDIlltlSLSEHRYTMTRNLSGGQKKRLSIALELVSN 202
Cdd:COG4598 99 mvfqSFNLWSH--MTVLENvieapvhvLGRPKAEAIERAEALLAKV----GLADKRDAYPAHLSGGQQQRAAIARALAME 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24580555 203 PPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIH 242
Cdd:COG4598 173 PEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
50-285 |
5.03e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.79 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEGNRSnaktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE----RNLSAFRKLS 125
Cdd:PRK13644 6 NVSYSYPDGTPA-----LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ-KGKVLVSGIDtgdfSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQ--DNQLHGNlTVQEAMTVA-TNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSN 202
Cdd:PRK13644 80 GIVFQnpETQFVGR-TVEEDLAFGpENLCLPPI----EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 203 PPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHqpSARLFEMFDQLYTLADGQCVYQGSTKQLV--PFLSTLN 280
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLsdVSLQTLG 232
|
....*
gi 24580555 281 LECPS 285
Cdd:PRK13644 233 LTPPS 237
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
46-240 |
6.24e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.11 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRvkegnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAFRKLS 125
Cdd:PRK13543 12 LAAHALAFS------RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQDNQLHGNLTVQEamtvatNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPI 205
Cdd:PRK13543 85 AYLGHLPGLKADLSTLE------NLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24580555 206 MFFDEPTSGLDsstcFQCIHLL-KMLAA----GGRTVICT 240
Cdd:PRK13543 159 WLLDEPYANLD----LEGITLVnRMISAhlrgGGAALVTT 194
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
67-273 |
7.43e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.53 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE----RNLSAFRKLSAYIMQDNQLHGNLTVQE 142
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAT-SGRIVFDGKDitdwQTAKIMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 143 amtvatNLKLSKKFSKPEKHSM-IDDIL-LTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTC 220
Cdd:PRK11614 100 ------NLAMGGFFAERDQFQErIKWVYeLFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24580555 221 FQCIHLLKMLAAGGRTvICTIHQPSARLFEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:PRK11614 174 QQIFDTIEQLREQGMT-IFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
48-273 |
8.04e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 74.73 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVKE------GNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGaerNLSA 120
Cdd:COG1134 17 YHEPSRSLKElllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPTS--GRVEVNG---RVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAyimqdnQLHGNLTVQE-AMTVATNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALEL 199
Cdd:COG1134 92 LLELGA------GFHPELTGREnIYLNGRLLGLSRK----EIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 200 VSNPPIMFFDEPTSGLDSStcFQ--CIHLLKMLAAGGRTVICTIHQPSArLFEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAA--FQkkCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
62-268 |
9.00e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.68 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSI-EGSVTMNGA--------ER-NLSAFrklsayimqd 131
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIlEGDILFKGEsildlepeERaHLGIF---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 132 nqlhgnLTVQEAMTVA--TN---LKLS-----KKFSKPEKH-----SMIDDILLTLSLSEHryTMTRNL----SGGQKKR 192
Cdd:CHL00131 88 ------LAFQYPIEIPgvSNadfLRLAynskrKFQGLPELDpleflEIINEKLKLVGMDPS--FLSRNVnegfSGGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 193 LSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPsaRLFEMF--DQLYTLADGQCVYQGS 268
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKTGD 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
50-284 |
9.76e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.16 E-value: 9.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYrvkEGNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSV-------TMNGAERNLSAFR 122
Cdd:PRK13643 8 NYTY---QPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPT-EGKVtvgdivvSSTSKQKEIKPVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 KLSAYIMQ--DNQLHGNLTVQEAMTVATNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTR-NLSGGQKKRLSIALEL 199
Cdd:PRK13643 84 KKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKE----KAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 200 VSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTK---QLVPFL 276
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSdvfQEVDFL 238
|
....*...
gi 24580555 277 STLNLECP 284
Cdd:PRK13643 239 KAHELGVP 246
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
36-273 |
1.31e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 77.06 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 36 QHLP-KRPAVDLAFHNLTYRvkegnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTmnga 114
Cdd:PRK10789 305 EPVPeGRGELDVNIRQFTYP------QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-EGDIR---- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 115 ernlsaFRKLSAYIMQDNQLHGNLTVQEAM------TVATNLKLSKKFSKPEK-------HSMIDDILltlSLSE----- 176
Cdd:PRK10789 374 ------FHDIPLTKLQLDSWRSRLAVVSQTpflfsdTVANNIALGRPDATQQEiehvarlASVHDDIL---RLPQgydte 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 177 --HRYTMtrnLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVICTIHQPSArLFEMfDQ 254
Cdd:PRK10789 445 vgERGVM---LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSA-LTEA-SE 518
|
250
....*....|....*....
gi 24580555 255 LYTLADGQCVYQGSTKQLV 273
Cdd:PRK10789 519 ILVMQHGHIAQRGNHDQLA 537
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
69-244 |
1.32e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 69 GVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNGaeRNLSAfrklsayimQDNQLHGNLT-------VQ 141
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGL-ARPDAGEVLWQG--EPIRR---------QRDEYHQDLLylghqpgIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCF 221
Cdd:PRK13538 87 TELTALENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|...
gi 24580555 222 QCIHLLKMLAAGGRTVICTIHQP 244
Cdd:PRK13538 167 RLEALLAQHAEQGGMVILTTHQD 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
46-284 |
1.42e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.78 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNRSNAKTiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-------RNL 118
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRA-LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPT-QGSVRVDDTLitstsknKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 119 SAFRKLSAYIMQ--DNQLHGNLTVQEAMTVATNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTmtRN---LSGGQKKRL 193
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQE----EAEALAREKLALVGISESLFE--KNpfeLSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 194 SIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTK--- 270
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSGKPKdif 233
|
250
....*....|....
gi 24580555 271 QLVPFLSTLNLECP 284
Cdd:PRK13649 234 QDVDFLEEKQLGVP 247
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
65-272 |
1.57e-14 |
|
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: 77.17 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 65 TILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNG---AERNLSAFRKLSAYIMQDnqlhgnlTV 140
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRfYDVTS--GRILIDGqdiRDVTQASLRAAIGIVPQD-------TV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 QEAMTVATNLKlskkFSKPE----------KHSMIDDILLtlSLSEHRYTMT--R--NLSGGQKKRLSIALELVSNPPIM 206
Cdd:COG5265 443 LFNDTIAYNIA----YGRPDaseeeveaaaRAAQIHDFIE--SLPDGYDTRVgeRglKLSGGEKQRVAIARTLLKNPPIL 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 207 FFDEPTSGLDSSTcFQCI-HLLKMLAAgGRTVICTIHQPS----ArlfemfDQLYTLADGQCVYQGSTKQL 272
Cdd:COG5265 517 IFDEATSALDSRT-ERAIqAALREVAR-GRTTLVIAHRLStivdA------DEILVLEAGRIVERGTHAEL 579
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
46-230 |
1.80e-14 |
|
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: 75.09 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLT--YRVKEGnrsnAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGY--KTSSIEGSVTMNGAE-RNLS- 119
Cdd:COG0444 2 LEVRNLKvyFPTRRG----VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlpPPGITSGEILFDGEDlLKLSe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 120 -AFRKLS----AYIMQD--NQLHGNLTVQEAMTVAtnLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTR---NLSGGQ 189
Cdd:COG0444 78 kELRKIRgreiQMIFQDpmTSLNPVMTVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24580555 190 KKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKML 230
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDL 196
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
58-272 |
1.80e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.03 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 58 GNRSnaktILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNG------AERNLSAFRKLSAYIMQD 131
Cdd:PRK11831 18 GNRC----IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGG-QIAPDHGEILFDGenipamSRSRLYTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 132 NQLHGNLTVQEamTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:PRK11831 93 GALFTDMNVFD--NVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 212 TSGLDSSTCFQCIHLLKML-AAGGRTVICTIHQPSARLfEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:PRK11831 171 FVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVL-SIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
67-262 |
1.89e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSIEGSVTMNGAErnlsafrkLSAYIMQDNQ------LHGNLT 139
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTYEGEIIFEGEE--------LQASNIRDTEragiaiIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEAMTVATNLKLSkkfSKPEKHSMIDD---------ILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDE 210
Cdd:PRK13549 93 LVKELSVLENIFLG---NEITPGGIMDYdamylraqkLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 211 PTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHqpsaRLFEMF---DQLYTLADGQ 262
Cdd:PRK13549 170 PTASLTESETAVLLDIIRDLKAHGIACIYISH----KLNEVKaisDTICVIRDGR 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
62-278 |
2.38e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSgyKTSSIEGSVTMNGA---------ER--NLSAFRKLSAYIMQ 130
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRveffnqniyERrvNLNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 131 DNQLHgnltvqeAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRN--------LSGGQKKRLSIALELVSN 202
Cdd:PRK14258 96 KPNLF-------PMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHkihksaldLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 203 PPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGR-TVICTIHQpsarlfemFDQLYTLADGQCVYQGSTK---QLVPFLST 278
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHN--------LHQVSRLSDFTAFFKGNENrigQLVEFGLT 240
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
63-306 |
4.45e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.21 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 63 AKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNIL-------SGYKTSsieGSVTMNGAE----RNLSAFRKLSAYIMQ- 130
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYS---GDVLLGGRSifnyRDVLEFRRRVGMLFQr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 131 DNQLHGNLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDE 210
Cdd:PRK14271 110 PNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 211 PTSGLDSSTCFQCIHLLKMLAagGRTVICTIHQPSARLFEMFDQLYTLADGQCVYQGSTKQLvpflstlnLECPSYHNPA 290
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL--------FSSPKHAETA 259
|
250
....*....|....*.
gi 24580555 291 SYVIEVScGEHGDHTR 306
Cdd:PRK14271 260 RYVAGLS-GDVKDAKR 274
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
64-272 |
4.60e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKST----LLNILSGyktssiEGSVTMNG------AERNLSAFRKLSAYIMQD-- 131
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS------QGEIWFDGqplhnlNRRQLLPVRHRIQVVFQDpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 132 NQLHGNLTVQEamTVATNLKL-SKKFSKPEKHSMIDDILLTLSL---SEHRYTMtrNLSGGQKKRLSIALELVSNPPIMF 207
Cdd:PRK15134 373 SSLNPRLNVLQ--IIEEGLRVhQPTLSAAQREQQVIAVMEEVGLdpeTRHRYPA--EFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 208 FDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
80-216 |
4.82e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 74.14 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 80 TAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNG-----AER--NLSAFRKLSAYIMQDNQL--HgnltvqeaMTVATNL 150
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGL-TRPQKGRIVLNGrvlfdAEKgiCLPPEKRRIGYVFQDARLfpH--------YKVRGNL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 151 KLS-KKFSKPEkhsmIDDILLTLSLsEH---RYTMTrnLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK11144 98 RYGmAKSMVAQ----FDKIVALLGI-EPlldRYPGS--LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
67-238 |
6.67e-14 |
|
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: 70.54 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE---RNLSAFRKL-SAYIMQDNQLHGnlTVQ 141
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGlRPPAS--GEITLDGKPvtrRSPRDAIRAgIAYVPEDRKREG--LVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EaMTVATNLklskkfskpekhsmiddilltlslsehryTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCF 221
Cdd:cd03215 92 D-LSVAENI-----------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170
....*....|....*...
gi 24580555 222 QcIH-LLKMLAAGGRTVI 238
Cdd:cd03215 142 E-IYrLIRELADAGKAVL 158
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
70-216 |
7.07e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 73.72 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 70 VSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLSAYIMQDNQLHGNLTVQEamTVAT 148
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT-AGQIMLDGVDlSHVPPYQRPINMMFQSYALFPHMTVEQ--NIAF 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 149 NLKlSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK11607 115 GLK-QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
64-273 |
7.29e-14 |
|
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: 74.84 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKT-SSIEGSVTMNGA--------ER------------------ 116
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyEPTSGRIIYHVAlcekcgyvERpskvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 117 -----NLS-----AFRKLSAYIMQDN-QLHGNLTVQEAMTVATNlklSKKFSKPEKHSMIDDILLTLSLsEHRYT-MTRN 184
Cdd:TIGR03269 93 evdfwNLSdklrrRIRKRIAIMLQRTfALYGDDTVLDNVLEALE---EIGYEGKEAVGRAVDLIEMVQL-SHRIThIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 185 LSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCfQCIH--LLKMLAAGGRTVICTIHQPSArLFEMFDQLYTLADGQ 262
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA-KLVHnaLEEAVKASGISMVLTSHWPEV-IEDLSDKAIWLENGE 246
|
250
....*....|.
gi 24580555 263 CVYQGSTKQLV 273
Cdd:TIGR03269 247 IKEEGTPDEVV 257
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
70-273 |
7.92e-14 |
|
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: 72.29 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 70 VSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNG------AERNLSAFR-KLSAYIMQDNQLHGNLTVQ 141
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRlIEPTS--GKVLIDGqdiaamSRKELRELRrKKISMVFQSFALLPHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 EamTVATNLKLsKKFSKPEKHSMIDDILLTLSL--SEHRYTmtRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSst 219
Cdd:cd03294 121 E--NVAFGLEV-QGVPRAEREERAAEALELVGLegWEHKYP--DELSGGMQQRVGLARALAVDPDILLMDEAFSALDP-- 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 220 cfqCI------HLLKMLAAGGRTVICTIHQPsARLFEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:cd03294 194 ---LIrremqdELLRLQAELQKTIVFITHDL-DEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
66-260 |
7.96e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKT-SSIE---GSVTMNG---AERNLsafrklsAYIMQDNQLHGNL 138
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDlfiGEKRMNDvppAERGV-------GMVFQSYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 139 TVQEAMtvATNLKLSKKfSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSS 218
Cdd:PRK11000 91 SVAENM--SFGLKLAGA-KKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 24580555 219 TCFQC-IHLLKMLAAGGRTVICTIHqpsarlfemfDQL--YTLAD 260
Cdd:PRK11000 168 LRVQMrIEISRLHKRLGRTMIYVTH----------DQVeaMTLAD 202
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
46-264 |
1.12e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGN---RSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG------AER 116
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS-QGNVSWRGeplaklNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 117 NLSAFRKLSAYIMQD-----NQLHgnlTV----QEAMTVATNLklskkfSKPEKHSMIDDILLTLSLS-EHRYTMTRNLS 186
Cdd:PRK10419 83 QRKAFRRDIQMVFQDsisavNPRK---TVreiiREPLRHLLSL------DKAERLARASEMLRAVDLDdSVLDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 187 GGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTI-HqpSARLFEMFDQ-LYTLADGQCV 264
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFItH--DLRLVERFCQrVMVMDNGQIV 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
67-243 |
2.07e-13 |
|
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: 70.05 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMN-------GAERNLSAFRKLSAYIMQDNQLHgNLT 139
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG-EMQTLEGKVHWSnknesepSFEATRSRNRYSVAYAAQKPWLL-NAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEAMTVATNLKLSKKFSKPEKHSMIDDILLtLSLSEHRYTMTR--NLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDs 217
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDL-LPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSALD- 172
|
170 180 190
....*....|....*....|....*....|....*
gi 24580555 218 stcfqcIHL---------LKMLAAGGRTVICTIHQ 243
Cdd:cd03290 173 ------IHLsdhlmqegiLKFLQDDKRTLVLVTHK 201
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
45-273 |
2.96e-13 |
|
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: 73.24 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 45 DLAFHNLTYrvKEGNRSNaktILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAF 121
Cdd:TIGR01193 473 DIVINDVSY--SYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGfslKDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 122 RKLSAYIMQDNQLHgnltvqeAMTVATNLKLSKKfskpeKHSMIDDILLTLSLSEHRYTMTR--------------NLSG 187
Cdd:TIGR01193 547 RQFINYLPQEPYIF-------SGSILENLLLGAK-----ENVSQDEIWAACEIAEIKDDIENmplgyqtelseegsSISG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 188 GQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHllKMLAAGGRTVICTIHQPSarLFEMFDQLYTLADGQCVYQG 267
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVN--NLLNLQDKTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQG 690
|
....*.
gi 24580555 268 STKQLV 273
Cdd:TIGR01193 691 SHDELL 696
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
66-217 |
3.60e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 71.27 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLSAYIMQDNQLHGNLTVQEam 144
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT-SGHIRFHGTDvSRLHARDRKVGFVFQHYALFRHMTVFD-- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 145 TVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTR---NLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:PRK10851 94 NIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRypaQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
48-272 |
4.18e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.19 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 48 FHNLTYRVKEGNRSNAKTIlKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-------RNLSA 120
Cdd:PRK13646 5 FDNVSYTYQKGTPYEHQAI-HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT-TGTVTVDDITithktkdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQ--DNQLHGNLTVQEAMTVATNLKLSKKFSKPEKHsmidDILLTLSLSehRYTMTRN---LSGGQKKRLSI 195
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAH----RLLMDLGFS--RDVMSQSpfqMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 196 ALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAA-GGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMN-EVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
69-216 |
4.73e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.63 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 69 GVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE-RNLSAF---RKLSAYIMQDNQLHGNLTVQEA 143
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGfYKPTG--GTILLRGQHiEGLPGHqiaRMGVVRTFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 144 MTVATNLKL----------SKKFSKPEKHSMIDDI--LLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:PRK11300 101 LLVAQHQQLktglfsgllkTPAFRRAESEALDRAAtwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
....*
gi 24580555 212 TSGLD 216
Cdd:PRK11300 181 AAGLN 185
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
43-227 |
4.73e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 70.76 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 43 AVDLAFHnltYRVKEGNRSNAKTI--LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERnLSA 120
Cdd:PRK11308 8 AIDLKKH---YPVKRGLFKPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPT-GGELYYQGQDL-LKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQDNQL-----HGNL--------TVQEAMTVATNLklskkfSKPEKHSMIDDILLTLSL-SEH--RYT-Mtr 183
Cdd:PRK11308 83 DPEAQKLLRQKIQIvfqnpYGSLnprkkvgqILEEPLLINTSL------SAAERREKALAMMAKVGLrPEHydRYPhM-- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 24580555 184 nLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLL 227
Cdd:PRK11308 155 -FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
38-272 |
5.97e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 38 LPKRPAVD----LAFHNLTYRVKEGNRSNAKtiLKGVSGRLRSGELTAIMGPSGAGKS-TLLNIL-----SGYKTSSieG 107
Cdd:PRK10261 1 MPHSDELDardvLAVENLNIAFMQEQQKIAA--VRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQC--D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 108 SVTMNGAERNLSAFRKLSAYIMQDnqLHGN---LTVQEAMT-----------VATNLKLSKKFSKPEKHSMIDDILLTLS 173
Cdd:PRK10261 77 KMLLRRRSRQVIELSEQSAAQMRH--VRGAdmaMIFQEPMTslnpvftvgeqIAESIRLHQGASREEAMVEAKRMLDQVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 174 LSEHRYTMTR---NLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFE 250
Cdd:PRK10261 155 IPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAE 234
|
250 260
....*....|....*....|..
gi 24580555 251 MFDQLYTLADGQCVYQGSTKQL 272
Cdd:PRK10261 235 IADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
67-242 |
7.51e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE------RNLSAFRKLSAYIMQDNQLHGNLTV 140
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPS-AGKIWFSGHDitrlknREVPFLRRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 QEamTVATNLKLSKKfSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTC 220
Cdd:PRK10908 97 YD--NVAIPLIIAGA-SGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180
....*....|....*....|..
gi 24580555 221 FQCIHLLKMLAAGGRTVICTIH 242
Cdd:PRK10908 174 EGILRLFEEFNRVGVTVLMATH 195
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
62-247 |
7.77e-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: 68.61 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTI--LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSS-------IEGSVTMNGA-ERNLSAFRKLS-AYIM 129
Cdd:COG4778 20 GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSgsilvrhDGGWVDLAQAsPREILALRRRTiGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 130 QdnqlhgNLTV---QEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMT-RNLSGGQKKRLSIALELVSNPPI 205
Cdd:COG4778 100 Q------FLRViprVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPpATFSGGEQQRVNIARGFIADPPL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24580555 206 MFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSAR 247
Cdd:COG4778 174 LLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVR 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
50-216 |
1.01e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 69.31 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEGNrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGY-KTSSieGSVTMNGAE-----RNLSAFRK 123
Cdd:PRK13637 7 NLTHIYMEGT-PFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLlKPTS--GKIIIDGVDitdkkVKLSDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 LSAYIMQ--DNQLHGNLTVQEAMTVATNLKLSK-KFSKPEKHSMIddiLLTLSLSEHRYTMTRNLSGGQKKRLSIALELV 200
Cdd:PRK13637 84 KVGLVFQypEYQLFEETIEKDIAFGPINLGLSEeEIENRVKRAMN---IVGLDYEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170
....*....|....*.
gi 24580555 201 SNPPIMFFDEPTSGLD 216
Cdd:PRK13637 161 MEPKILILDEPTAGLD 176
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
41-238 |
1.13e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 41 RPAVDLAFHNLTYRVKEGNRSNAKTIlKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKtSSIEGSVTMNGAERN--- 117
Cdd:PRK09700 254 KENVSNLAHETVFEVRNVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVD-KRAGGEIRLNGKDISprs 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 118 -LSAFRKLSAYIMQ---DNQLHGNLTVQEAMTVATNLKLSKK------FSKPEKHSMIDDILLTLSLSEHryTMTRN--- 184
Cdd:PRK09700 332 pLDAVKKGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDGGYkgamglFHEVDEQRTAENQRELLALKCH--SVNQNite 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24580555 185 LSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVI 238
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
55-271 |
1.21e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 55 VKEGNRsnaktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGykTSSIEGSVTMNGaeRNLSAFR--KLS---AYIM 129
Cdd:PRK03695 6 VAVSTR------LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG--LLPGSGSIQFAG--QPLEAWSaaELArhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 130 QDNqlhgnlTVQEAMTVATNLKLSK--KFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGG--QKKRLSIALELV---SN 202
Cdd:PRK03695 76 QQQ------TPPFAMPVFQYLTLHQpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVwpdIN 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 203 P--PIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTKQ 271
Cdd:PRK03695 150 PagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLN-HTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
62-272 |
1.24e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 68.54 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG----YKTS-SIEGSVTMNGAER---NLSAFRKLSAYIMQDNQ 133
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlieiYDSKiKVDGKVLYFGKDIfqiDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 134 LHGNLTVQEamTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRY----TMTRNLSGGQKKRLSIALELVSNPPIMFFD 209
Cdd:PRK14246 101 PFPHLSIYD--NIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYdrlnSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 210 EPTSGLDSSTCfQCIHLLKMLAAGGRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:PRK14246 179 EPTSMIDIVNS-QAIEKLITELKNEIAIVIVSHNPQ-QVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
45-219 |
1.54e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.05 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 45 DLAFHNLTYRVkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLlnILSGYKTS-SIEGSVTMNG---AERNLSA 120
Cdd:cd03369 6 EIEVENLSVRY----APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLeAEEGKIEIDGidiSTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQDNQLHgnltvqeAMTVATNLKLSKKFSKpekhsmiDDILLTLSLSEHrytmTRNLSGGQKKRLSIALELV 200
Cdd:cd03369 80 LRSSLTIIPQDPTLF-------SGTIRSNLDPFDEYSD-------EEIYGALRVSEG----GLNLSQGQRQLLCLARALL 141
|
170
....*....|....*....
gi 24580555 201 SNPPIMFFDEPTSGLDSST 219
Cdd:cd03369 142 KRPRVLVLDEATASIDYAT 160
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
69-271 |
2.17e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.64 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 69 GVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTmngaernlsafrklsaYIMQDNQLHGNLTVQEA----- 143
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD-AGEVH----------------YRMRDGQLRDLYALSEAerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 144 -----------------MTVATNLKLSKKF-SKPEKH-------------------SMIDDilltlslsehrytMTRNLS 186
Cdd:PRK11701 87 lrtewgfvhqhprdglrMQVSAGGNIGERLmAVGARHygdiratagdwlerveidaARIDD-------------LPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 187 GGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAA--GGRTVICTIHQPSARLFEmfDQLYTLADGQCV 264
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLLA--HRLLVMKQGRVV 231
|
....*..
gi 24580555 265 YQGSTKQ 271
Cdd:PRK11701 232 ESGLTDQ 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
67-311 |
2.46e-12 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 69.71 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTL----LNILSGyktssiEGSVTMNGAE---RNLSAFRKLSAYI---MQD--NQL 134
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS------EGEIRFDGQDldgLSRRALRPLRRRMqvvFQDpfGSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 135 HGNLTVQEamTVATNLKL-SKKFSKPEKHSMIDDILLTLSLSE---HRYTMTrnLSGGQKKRLSIALELVSNPPIMFFDE 210
Cdd:COG4172 376 SPRMTVGQ--IIAEGLRVhGPGLSAAERRARVAEALEEVGLDPaarHRYPHE--FSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 211 PTSGLDSSTCFQCIHLLKMLaaggrtvictihqpSAR-----LF---------EMFDQLYTLADGQCVYQGSTKQLvpfl 276
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDL--------------QREhglayLFishdlavvrALAHRVMVMKDGKVVEQGPTEQV---- 513
|
250 260 270
....*....|....*....|....*....|....*
gi 24580555 277 stlnlecpsYHNPASyvievscgehgDHTRKLVDA 311
Cdd:COG4172 514 ---------FDAPQH-----------PYTRALLAA 528
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
64-216 |
3.22e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 67.37 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG----YKTSSIEGSVTMNGA-----ERNLSAFRKLSAYIMQ---- 130
Cdd:COG1117 24 KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndlIPGARVEGEILLDGEdiydpDVDVVELRRRVGMVFQkpnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 131 ------DNqlhgnltvqeamtVATNLKLSKKFSKPEkhsmIDDI----LLTLSLSE------HRYTMtrNLSGGQKKRLS 194
Cdd:COG1117 104 fpksiyDN-------------VAYGLRLHGIKSKSE----LDEIveesLRKAALWDevkdrlKKSAL--GLSGGQQQRLC 164
|
170 180
....*....|....*....|..
gi 24580555 195 IALELVSNPPIMFFDEPTSGLD 216
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALD 186
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
46-228 |
3.25e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.43 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNRSNAktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNG---AERNLSAFR 122
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQ---LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGL-FEEFEGKVKIDGellTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 KLSAYIMQ--DNQLHGnLTVQEAMTVATNlklSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELV 200
Cdd:PRK13642 81 RKIGMVFQnpDNQFVG-ATVEDDVAFGME---NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190
....*....|....*....|....*....|.
gi 24580555 201 SNPPIMFFDEPTSGLD---SSTCFQCIHLLK 228
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgRQEIMRVIHEIK 187
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
60-271 |
3.36e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.47 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 60 RSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFRKLSAYIMQ--DNQL 134
Cdd:PRK13648 18 QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK-SGEIFYNNqaiTDDNFEKLRKHIGIVFQnpDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 135 HGNlTVQeaMTVATNLKlskKFSKP--EKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPT 212
Cdd:PRK13648 97 VGS-IVK--YDVAFGLE---NHAVPydEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24580555 213 SGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMfDQLYTLADGQcVYQGSTKQ 271
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEA-DHVIVMNKGT-VYKEGTPT 227
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-264 |
4.91e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 69.06 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 22 QLKAQIVPAQPKTLQHLPKRPAVD---LAFHNLTYRVKEGNRSNAKTIlkG-VSGRLRSGELTAIMGPSGAGKSTLLNIL 97
Cdd:COG4615 301 ELELALAAAEPAAADAAAPPAPADfqtLELRGVTYRYPGEDGDEGFTL--GpIDLTIRRGELVFIVGGNGSGKSTLAKLL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 98 SG-YKTSSieGSVTMNGA---ERNLSAFRKLSAYIMQDN-------QLHGNLTVQEAMTVATNLKLSKKfskpekhsmid 166
Cdd:COG4615 379 TGlYRPES--GEILLDGQpvtADNREAYRQLFSAVFSDFhlfdrllGLDGEADPARARELLERLELDHK----------- 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 167 dilltLSLSEHRYTmTRNLSGGQKKRLSIALELVSNPPIMFFDE------PTsgldsstcFQCI---HLLKMLAAGGRTV 237
Cdd:COG4615 446 -----VSVEDGRFS-TTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPE--------FRRVfytELLPELKARGKTV 511
|
250 260
....*....|....*....|....*..
gi 24580555 238 ICTIHQPsaRLFEMFDQLYTLADGQCV 264
Cdd:COG4615 512 IAISHDD--RYFDLADRVLKMDYGKLV 536
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
50-216 |
5.62e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.96 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEgnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFRKLSA 126
Cdd:PRK13635 10 HISFRYPD----AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-AGTITVGGmvlSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 127 YIMQ--DNQLHGNlTVQEamTVATNLKlSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPP 204
Cdd:PRK13635 85 MVFQnpDNQFVGA-TVQD--DVAFGLE-NIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
|
170
....*....|..
gi 24580555 205 IMFFDEPTSGLD 216
Cdd:PRK13635 161 IIILDEATSMLD 172
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
50-219 |
5.66e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKE-------GNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSIEGSVTmngaernlsaf 121
Cdd:COG2401 22 DLSERVAIvleafgvELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGaLKGTPVAGCVD----------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 122 rklsayiMQDNQLHGNLTVQEAMTVATNLKLSKKfskpekhsmiddILLTLSLSE-----HRYtmtRNLSGGQKKRLSIA 196
Cdd:COG2401 91 -------VPDNQFGREASLIDAIGRKGDFKDAVE------------LLNAVGLSDavlwlRRF---KELSTGQKFRFRLA 148
|
170 180
....*....|....*....|...
gi 24580555 197 LELVSNPPIMFFDEPTSGLDSST 219
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQT 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
70-238 |
7.05e-12 |
|
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: 68.31 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 70 VSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSIEGSVTMNGAERN----LSAFRKLSAYIMQDNQLHGNLTVqeaMT 145
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPVDirnpAQAIRAGIAMVPEDRKRHGIVPI---LG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 146 VATNLKLS--KKFSK------PEKHSMIDDILLTLSL-SEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:TIGR02633 356 VGKNITLSvlKSFCFkmridaAAELQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180
....*....|....*....|..
gi 24580555 217 SSTCFQCIHLLKMLAAGGRTVI 238
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAII 457
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
66-216 |
1.23e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.79 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYK--TS---SIEGSV--TMNGAERNLsafrklsAYIMQDNQLHGNL 138
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLEriTSgeiWIGGRVvnELEPADRDI-------AMVFQNYALYPHM 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 139 TVQEAMtvATNLKLsKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK11650 92 SVRENM--AYGLKI-RGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
67-238 |
1.34e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.36 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAFRK-LSAYI-MqdnqLHGNLTVQEAM 144
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPD-SGEILIDGKPVRIRSPRDaIALGIgM----VHQHFMLVPNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 145 TVATNLKLS---KKFSKPEKHSMIDDIlltLSLSEhRY-------TMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSG 214
Cdd:COG3845 96 TVAENIVLGlepTKGGRLDRKAARARI---RELSE-RYgldvdpdAKVEDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180
....*....|....*....|....*....
gi 24580555 215 L-----DsstcfQCIHLLKMLAAGGRTVI 238
Cdd:COG3845 172 LtpqeaD-----ELFEILRRLAAEGKSII 195
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
67-284 |
1.60e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.88 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTL---LNIL----SG------------YKTSSIEGSVTMNGAER-------NLSA 120
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALllpdTGtiewifkdeknkKKTKEKEKVLEKLVIQKtrfkkikKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQ--DNQLHGNLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRytmTRNLSGGQKKRLSIALE 198
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRS---PFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 199 LVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLfEMFDQLYTLADGQCVYQGSTKQL---VPF 275
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVL-EWTKRTIFFKDGKIIKDGDTYDIlsdNKF 258
|
....*....
gi 24580555 276 LSTLNLECP 284
Cdd:PRK13651 259 LIENNMEPP 267
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
46-242 |
1.70e-11 |
|
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: 62.47 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNGAERnlsafrklS 125
Cdd:cd03221 1 IELENLSKTYGG------KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK--------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQdnqlhgnltvqeamtvatnlklskkfskpekhsmiddilltlslsehrytmtrnLSGGQKKRLSIALELVSNPPI 205
Cdd:cd03221 66 GYFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*..
gi 24580555 206 MFFDEPTSGLDSSTcfqCIHLLKMLAAGGRTVICTIH 242
Cdd:cd03221 92 LLLDEPTNHLDLES---IEALEEALKEYPGTVILVSH 125
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
40-273 |
1.71e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.35 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 40 KRPAVDLAFHNLT--YRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGA--- 114
Cdd:PRK11176 336 ERAKGDIEFRNVTftYPGKE------VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-EGEILLDGHdlr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 115 ERNLSAFRKLSAYIMQDNQLHGNltvqeamTVATNLKLSK--KFSKPE-------KHSM-----IDDILLTLsLSEHryt 180
Cdd:PRK11176 409 DYTLASLRNQVALVSQNVHLFND-------TIANNIAYARteQYSREQieeaarmAYAMdfinkMDNGLDTV-IGEN--- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 181 mTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAgGRTVICTIHQPSArlFEMFDQLYTLAD 260
Cdd:PRK11176 478 -GVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLST--IEKADEILVVED 553
|
250
....*....|...
gi 24580555 261 GQCVYQGSTKQLV 273
Cdd:PRK11176 554 GEIVERGTHAELL 566
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
46-242 |
1.77e-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: 68.12 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTyRVKEGNRSNA-KTILKGVsgrlRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNGAE--RNLSAFR 122
Cdd:TIGR01257 1938 LRLNELT-KVYSGTSSPAvDRLCVGV----RPGECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGKSilTNISDVH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 KLSAYIMQDNQLHGNLTVQEAMTVATNLK--LSKKFSKPEKHSmiddiLLTLSLSEHRYTMTRNLSGGQKKRLSIALELV 200
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGREHLYLYARLRgvPAEEIEKVANWS-----IQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24580555 201 SNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIH 242
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
68-230 |
1.83e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.88 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 68 KGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG------AERNLSAFRKLSAYIMQD--NQLHGNLT 139
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT-DGEVAWLGkdllgmKDDEWRAVRSDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEamTVATNL-----KLSKKFSKPEKHSMIDDILLTLSLSeHRYTmtRNLSGGQKKRLSIALELVSNPPIMFFDEPTSG 214
Cdd:PRK15079 117 IGE--IIAEPLrtyhpKLSRQEVKDRVKAMMLKVGLLPNLI-NRYP--HEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170
....*....|....*.
gi 24580555 215 LDSSTCFQCIHLLKML 230
Cdd:PRK15079 192 LDVSIQAQVVNLLQQL 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
66-272 |
2.02e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLN----ILSGYKTSSIEGSVTMNG-----AERNLSAFRKLSAYIMQDNQLHG 136
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARVEGEVRLFGrniysPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 NLTVQEamTVATNLKLSKKF-SKPEKHSMIDDILLTLSLSEHRYTMTR----NLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:PRK14267 99 HLTIYD--NVAIGVKLNGLVkSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 212 TSGLDSSTCFQCIHLLKMLAAgGRTVICTIHQP--SARLFEMFDQLYTladGQCVYQGSTKQL 272
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKK-EYTIVLVTHSPaqAARVSDYVAFLYL---GKLIEVGPTRKV 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
46-269 |
2.02e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.20 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNL--TYRVKEG--NRSNAKTIlKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAF 121
Cdd:PRK15112 5 LEVRNLskTFRYRTGwfRRQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 122 RKLSA---YIMQDNQLHGNLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSL-SEHRYTMTRNLSGGQKKRLSIAL 197
Cdd:PRK15112 83 SYRSQrirMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 198 ELVSNPPIMFFDEPTSGLDSSTCFQCIHLlkMLAAGGRTVICTIH--QPSARLFEMFDQLYTLADGQCVYQGST 269
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINL--MLELQEKQGISYIYvtQHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
33-238 |
2.27e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.59 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 33 KTLQHLPKRPAVD----LAFHNLTYRVKEGnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGS 108
Cdd:COG3845 241 EVLLRVEKAPAEPgevvLEVENLSVRDDRG-----VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA-SGS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 109 VTMNGAE-RNLS--AFRKLS-AYIMQDNQLHGnlTVQEaMTVATNLkLSKKFSKPE--KHSMIDD---ILLTLSLSEhRY 179
Cdd:COG3845 315 IRLDGEDiTGLSprERRRLGvAYIPEDRLGRG--LVPD-MSVAENL-ILGRYRRPPfsRGGFLDRkaiRAFAEELIE-EF 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 180 --------TMTRNLSGG--QKkrLSIALELVSNPPIMFFDEPTSGLD-SSTCFqcIH-LLKMLAAGGRTVI 238
Cdd:COG3845 390 dvrtpgpdTPARSLSGGnqQK--VILARELSRDPKLLIAAQPTRGLDvGAIEF--IHqRLLELRDAGAAVL 456
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
28-262 |
2.81e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.75 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 28 VPAQPKTLQHLPKRPAVDLAFHNLTYRvkegnRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyktssI-- 105
Cdd:COG4178 345 ADALPEAASRIETSEDGALALEDLTLR-----TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-----Lwp 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 106 --EGSVTMNGAERnlSAFrkLS--AYIMQDN---QL--------HGNLTVQEAMTvATNLklskkfskPEKHSMIDDill 170
Cdd:COG4178 415 ygSGRIARPAGAR--VLF--LPqrPYLPLGTlreALlypataeaFSDAELREALE-AVGL--------GHLAERLDE--- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 171 tlslsEHRYtmTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFqciHLLKMLAA--GGRTVICTIHQPSarL 248
Cdd:COG4178 479 -----EADW--DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA---ALYQLLREelPGTTVISVGHRST--L 546
|
250
....*....|....
gi 24580555 249 FEMFDQLYTLADGQ 262
Cdd:COG4178 547 AAFHDRVLELTGDG 560
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
67-273 |
2.89e-11 |
|
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: 67.28 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNGAernlsafrklSAYIMQDNQLHgNLTVQEamtv 146
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLA-EMDKVEGHVHMKGS----------VAYVPQQAWIQ-NDSLRE---- 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 147 atNLKLSKKFSKPEKHSMIDDILLTLSL----SEHRYTMTR---NLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST 219
Cdd:TIGR00957 718 --NILFGKALNEKYYQQVLEACALLPDLeilpSGDRTEIGEkgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 220 ---CFQ-CIHLLKMLAagGRTVICTIHQPSarLFEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:TIGR00957 796 gkhIFEhVIGPEGVLK--NKTRILVTHGIS--YLPQVDVIIVMSGGKISEMGSYQELL 849
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
62-216 |
3.41e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.03 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYK----TSSIEGSVTMNGAerNLSA-------FRK-LSAYIM 129
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpEVTITGSIVYNGH--NIYSprtdtvdLRKeIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 130 QDNQLhgNLTVQEamTVATNLKLSKKFSKPEKHSMIDDILLTLSL----SEHRYTMTRNLSGGQKKRLSIALELVSNPPI 205
Cdd:PRK14239 94 QPNPF--PMSIYE--NVVYGLRLKGIKDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170
....*....|.
gi 24580555 206 MFFDEPTSGLD 216
Cdd:PRK14239 170 ILLDEPTSALD 180
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
74-241 |
4.42e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.75 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 74 LRSGELTAIMGPSGAGKS----TLLNILSgyKTSSIEGSVTMNGAE-RNLS--AFRKLSA----YIMQD--NQLHGNLTV 140
Cdd:PRK09473 39 LRAGETLGIVGESGSGKSqtafALMGLLA--ANGRIGGSATFNGREiLNLPekELNKLRAeqisMIFQDpmTSLNPYMRV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 QEA-MTVatnLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMT---RNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK09473 117 GEQlMEV---LMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180
....*....|....*....|....*
gi 24580555 217 SSTCFQCIHLLKMLAAGGRTVICTI 241
Cdd:PRK09473 194 VTVQAQIMTLLNELKREFNTAIIMI 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
69-230 |
8.11e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 63.98 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 69 GVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE------RNLSAFRKLSAYIMQDNQ--LHGNLT 139
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRlEEPTS--GEILFDGQDitglsgRELRPLRRRMQMVFQDPYasLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEamTVATNLKLSKKFSKPEKHSMIDDILLTLSLS-EHrytMTRN---LSGGQKKRLSIALELVSNPPIMFFDEPTSGL 215
Cdd:COG4608 114 VGD--IIAEPLRIHGLASKAERRERVAELLELVGLRpEH---ADRYpheFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170
....*....|....*
gi 24580555 216 DSSTCFQCIHLLKML 230
Cdd:COG4608 189 DVSIQAQVLNLLEDL 203
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
67-216 |
8.52e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.50 E-value: 8.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGY-----KTSSIEGSVTMNGA-ERNLSAFRKLSAYIMQ--DNQLHGNl 138
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlqptsGTVTIGERVITAGKkNKKLKPLRKKVGIVFQfpEHQLFEE- 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24580555 139 TVQEAMTVA-TNLKLSKKFSKPEKHSMIDDILLTLSLSEHRytmTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK13634 102 TVEKDICFGpMNFGVSEEDAKQKAREMIELVGLPEELLARS---PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
49-295 |
1.16e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.83 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 49 HNLTYRVKEgnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNG---AERNLSAFRKLS 125
Cdd:PRK13650 8 KNLTFKYKE---DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGdllTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQ--DNQLHGnLTVQEamTVATNLKlSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNP 203
Cdd:PRK13650 84 GMVFQnpDNQFVG-ATVED--DVAFGLE-NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 204 PIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQpsarLFE--MFDQLYTLADGQCVYQGSTKQL-------- 272
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHD----LDEvaLSDRVLVMKNGQVESTSTPRELfsrgndll 235
|
250 260 270
....*....|....*....|....*....|
gi 24580555 273 -----VPFLSTL--NLECPSYHNPASYVIE 295
Cdd:PRK13650 236 qlgldIPFTTSLvqSLRQNGYDLPEGYLTE 265
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
67-262 |
1.46e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAERNLSAFRklsayimqDNQ------LHGNLT 139
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGiYTRDA--GSILYLGKEVTFNGPK--------SSQeagigiIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEAMTVATNLKLSKKFSKP-------EKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIA--LELVSNPPIMffDE 210
Cdd:PRK10762 90 LIPQLTIAENIFLGREFVNRfgridwkKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAkvLSFESKVIIM--DE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 211 PTSGL-DSST--CFQCIHLLKmlAAGgrtviCTIHQPSARLFEMF---DQLYTLADGQ 262
Cdd:PRK10762 168 PTDALtDTETesLFRVIRELK--SQG-----RGIVYISHRLKEIFeicDDVTVFRDGQ 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
64-272 |
1.62e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGaeRNLS-----AFRKLSAYIMQDnqlhgnl 138
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT-EGEIRLDG--RPLSslshsVLRQGVAMVQQD------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 139 TVQEAMTVATNLKLSKKFSkpEKHsmIDDILLTLSLSEHRYTM-----TR------NLSGGQKKRLSIALELVSNPPIMF 207
Cdd:PRK10790 424 PVVLADTFLANVTLGRDIS--EEQ--VWQALETVQLAELARSLpdglyTPlgeqgnNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 208 FDEPTSGLDSSTcFQCI-HLLKMLAAggRTVICTIHQPSARLFEMfDQLYTLADGQCVYQGSTKQL 272
Cdd:PRK10790 500 LDEATANIDSGT-EQAIqQALAAVRE--HTTLVVIAHRLSTIVEA-DTILVLHRGQAVEQGTHQQL 561
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
64-219 |
1.67e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.00 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAErnLSAFRKLSAYIMQDNQLhgnLTVQea 143
Cdd:PRK11247 25 RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS-AGELLAGTAP--LAEAREDTRLMFQDARL---LPWK-- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24580555 144 mTVATNLKLSKKFS-KPEKHsmidDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST 219
Cdd:PRK11247 97 -KVIDNVGLGLKGQwRDAAL----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
46-341 |
2.28e-10 |
|
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: 63.55 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLtyRVKEGNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKS-TLLNILS--GYKTSSIEGSVTMNGaeRNLSAfr 122
Cdd:COG4172 7 LSVEDL--SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRllPDPAAHPSGSILFDG--QDLLG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 123 kLSAYIMQdnQLHGN---LTVQEAMT-----------VATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTR---NL 185
Cdd:COG4172 81 -LSERELR--RIRGNriaMIFQEPMTslnplhtigkqIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAyphQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 186 SGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVIctihqpsarLF---------EMFDQLY 256
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMAL---------LLithdlgvvrRFADRVA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 257 TLADGQCVYQGSTKQLvpflstlnlecpsYHNPasyvievscgEHgDHTRKLVDAIDNG-KRDVRSSADyaglkarnDLV 335
Cdd:COG4172 229 VMRQGEIVEQGPTAEL-------------FAAP----------QH-PYTRKLLAAEPRGdPRPVPPDAP--------PLL 276
|
....*.
gi 24580555 336 KVQNLK 341
Cdd:COG4172 277 EARDLK 282
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
75-242 |
2.37e-10 |
|
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: 61.61 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 75 RSGELTAIMGPSGAGKSTLLNILSGYKTSSIeGSVTMNGAERN-LSAFR--KLSAYI--MQDNQLHGNLTVQ--EAMTVA 147
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNL-GKFDDPPDWDEiLDEFRgsELQNYFtkLLEGDVKVIVKPQyvDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 148 TNLKLSKKFSKPEKHSMIDDILLTLSLsehRYTMTRN---LSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCI 224
Cdd:cd03236 103 VKGKVGELLKKKDERGKLDELVDQLEL---RHVLDRNidqLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
|
170
....*....|....*...
gi 24580555 225 HLLKMLAAGGRTVICTIH 242
Cdd:cd03236 180 RLIRELAEDDNYVLVVEH 197
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
46-311 |
2.50e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.64 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYrvkegnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKS----TLLNIL-SGYKTSSieGSVTMNGAERNLSA 120
Cdd:PRK10418 5 IELRNIAL-------QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQTA--GRVLLDGKPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FR-KLSAYIMQD-----NQLHgnltvqeamTVATN-LKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTR---NLSGGQK 190
Cdd:PRK10418 76 LRgRKIATIMQNprsafNPLH---------TMHTHaRETCLALGKPADDATLTAALEAVGLENAARVLKLypfEMSGGML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 191 KRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQPS--ARLfemFDQLYTLADGQCVYQG 267
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGvvARL---ADDVAVMSHGRIVEQG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 24580555 268 STKQLvpflstlnlecpsYHNPASYVievscgehgdhTRKLVDA 311
Cdd:PRK10418 224 DVETL-------------FNAPKHAV-----------TRSLVSA 243
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
46-260 |
3.02e-10 |
|
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: 59.47 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYrvkegNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERnlsafrklS 125
Cdd:cd03223 1 IELENLSL-----ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-SGRIGMPEGED--------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQdnqlhgnltvQEAMTVATnLKlskkfskpekhsmidDILLtlslsehrYTMTRNLSGGQKKRLSIALELVSNPPI 205
Cdd:cd03223 67 LFLPQ----------RPYLPLGT-LR---------------EQLI--------YPWDDVLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 206 MFFDEPTSGLDSSTCFQcihLLKMLAAGGRTVICTIHQPSARLFemFDQLYTLAD 260
Cdd:cd03223 113 VFLDEATSALDEESEDR---LYQLLKELGITVISVGHRPSLWKF--HDRVLDLDG 162
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
46-233 |
3.56e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.96 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEgnrsnaKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSI-EGSVTMNG----------- 113
Cdd:PRK09580 2 LSIKDLHVSVED------KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVtGGTVEFKGkdllelspedr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 114 -AERNLSAFRklsaYIMQDNQLHGNLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNL--SGGQK 190
Cdd:PRK09580 76 aGEGIFMAFQ----YPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 24580555 191 KRLSIALELVSNPPIMFFDEPTSGLDsstcfqcIHLLKMLAAG 233
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLD-------IDALKIVADG 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
64-270 |
4.07e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.26 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLL-NILSGYKTSsiEGSVTmngAERNLsAFRKLSAYIMqdnqlhgNLTVQE 142
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQFEIS--EGRVW---AERSI-AYVPQQAWIM-------NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 143 AMTV-----ATNLKLSKKFSKPEKhsmiDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:PTZ00243 740 NILFfdeedAARLADAVRVSQLEA----DLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24580555 218 STCFQCIHLLKMLAAGGRTVICTIHQpsARLFEMFDQLYTLADGQCVYQGSTK 270
Cdd:PTZ00243 816 HVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDGRVEFSGSSA 866
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
70-238 |
4.65e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 70 VSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSIEGSVTMNGAE---RN-LSAFRKLSAYIMQDNQLHGNLTVqeaMT 145
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPvkiRNpQQAIAQGIAMVPEDRKRDGIVPV---MG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 146 VATNLKLS--KKFSKpekHSMIDDillTLSLSEHRYTMTR-------------NLSGGQKKRLSIALELVSNPPIMFFDE 210
Cdd:PRK13549 358 VGKNITLAalDRFTG---GSRIDD---AAELKTILESIQRlkvktaspelaiaRLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180
....*....|....*....|....*...
gi 24580555 211 PTSGLDSSTCFQCIHLLKMLAAGGRTVI 238
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQGVAII 459
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
484-695 |
8.73e-10 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 59.06 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 484 MLFLMYTSMTITILSFPLEMpvlLKENFNRWY----SLKSYYLAISVADLPFQAIFCVIYVSIVYYFTSQPWELFRFSMF 559
Cdd:COG0842 11 AMSLLFTALMLTALSIARER---EQGTLERLLvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 560 LSACLLISFVAQSVGLVVGA-AMNVQNGVFLAPVMSVPFLLFSGFFVSFDAIPVYLRWITYLSYIRYGFEGTALATYGyg 638
Cdd:COG0842 88 LLVLLLFALAFSGLGLLISTlARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLG-- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24580555 639 reklrcfqtychfkspittleelDMVNANFTLDIVALIVIFVVLRISAYLFLRWKLK 695
Cdd:COG0842 166 -----------------------GAGLADVWPSLLVLLAFAVVLLALALRLFRRRLR 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
65-243 |
1.06e-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: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 65 TILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSIEGSVTMNGAERNLSAFRKLSAYIMQdnQLHGNLTVQEA 143
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTWDGEIYWSGSPLKASNIRDTERAGIV--IIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 144 MTVATNLKLSKKFSKP----EKHSMI---DDILLTLSLSEHRYTM-TRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGL 215
Cdd:TIGR02633 93 LSVAENIFLGNEITLPggrmAYNAMYlraKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180
....*....|....*....|....*...
gi 24580555 216 DSSTCFQCIHLLKMLAAGGRTVICTIHQ 243
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
66-264 |
1.17e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.34 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTL-LNILSGYKTSSIEGSVTMNGAERNLS----AFRKLSAYIMQDNQLHG-NL- 138
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNISGTVFKDGKEVDVStvsdAIDAGLAYVTEDRKGYGlNLi 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 139 -TVQEAMTVAtNLKlskKFSKpekHSMIDDILLTLSLSEHRYTM----------TRNLSGGQKKRLSIALELVSNPPIMF 207
Cdd:NF040905 355 dDIKRNITLA-NLG---KVSR---RGVIDENEEIKVAEEYRKKMniktpsvfqkVGNLSGGNQQKVVLSKWLFTDPDVLI 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 208 FDEPTSGLDSSTCFQCIHLLKMLAAGGRTVIcTIhqpSARLFE---MFDQLYTLADGQCV 264
Cdd:NF040905 428 LDEPTRGIDVGAKYEIYTIINELAAEGKGVI-VI---SSELPEllgMCDRIYVMNEGRIT 483
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
46-262 |
1.17e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.53 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNRSnaktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNGAE---RNLSAF 121
Cdd:PRK10522 323 LELRNVTFAYQDNGFS-----VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQS--GEILLDGKPvtaEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 122 RKLSAYIMQDNQLHGNLTVQEAMTVAT--------NLKLSKKfskpekhsmiddilltLSLSEHRYTMTRnLSGGQKKRL 193
Cdd:PRK10522 396 RKLFSAVFTDFHLFDQLLGPEGKPANPalvekwleRLKMAHK----------------LELEDGRISNLK-LSKGQKKRL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 194 SIALELVSNPPIMFFDEPTSglDSSTCFQCI---HLLKMLAAGGRTVICTIHQPSarLFEMFDQLYTLADGQ 262
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAA--DQDPHFRREfyqVLLPLLQEMGKTIFAISHDDH--YFIHADRLLEMRNGQ 526
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
77-217 |
1.76e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.12 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 77 GELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAFRKLSAYIM-QDNQLHGNLTVQEamTVATNLKLsKK 155
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKPT-EGQIFIDGEDVTHRSIQQRDICMVfQSYALFPHMSLGE--NVGYGLKM-LG 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24580555 156 FSKPEKHSMIDDILLTLSLS--EHRYTmtRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:PRK11432 108 VPKEERKQRVKEALELVDLAgfEDRYV--DQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
66-272 |
2.04e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSIeGSVTMNGAER-NLSAFR--KLSAYIM-QDNQLHGNLTVQ 141
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS-GTLEIGGNPCaRLTPAKahQLGIYLVpQEPLLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 E------AMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRytMTRNLSGgqkkrlsialeLVSNPPIMFFDEPTSGL 215
Cdd:PRK15439 105 EnilfglPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQ--IVEILRG-----------LMRDSRILILDEPTASL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 216 ---DSSTCFQCIhllKMLAAGGRTVICTIHQ-PSARlfEMFDQLYTLADGQCVYQGSTKQL 272
Cdd:PRK15439 172 tpaETERLFSRI---RELLAQGVGIVFISHKlPEIR--QLADRISVMRDGTIALSGKTADL 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
67-216 |
2.81e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLS---AYIMQDNQLHG---NLT 139
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT-SGYVTLDGHEvVTRSPQDGLAngiVYISEDRKRDGlvlGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEAMTVATNLKLSKKF----SKPEKHSMIDDILL----TLSLSEhrytMTRNLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:PRK10762 347 VKENMSLTALRYFSRAGgslkHADEQQAVSDFIRLfnikTPSMEQ----AIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
....*
gi 24580555 212 TSGLD 216
Cdd:PRK10762 423 TRGVD 427
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
67-273 |
2.90e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.66 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNGAE---------RNLSafRKLSAYIMQDNQLHGN 137
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL-IEPTRGQVLIDGVDiakisdaelREVR--RKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 138 LTVQEAMTVATNLKlskKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:PRK10070 121 MTVLDNTAFGMELA---GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 218 --STCFQcIHLLKMLAAGGRTVICTIHQPSARLfEMFDQLYTLADGQCVYQGSTKQLV 273
Cdd:PRK10070 198 liRTEMQ-DELVKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
39-238 |
2.92e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 39 PKRPAVD----LAFHNLTyrvkegnrsnAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSieGSVTMNG 113
Cdd:COG1129 246 PKRAAAPgevvLEVEGLS----------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGaDPADS--GEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 114 AERNLS----AFRKLSAYIMQDNQLHG---NLTVQEAMTVATNLKLSKKF--SKPEKHSMIDDILLTLSL-SEHRYTMTR 183
Cdd:COG1129 314 KPVRIRsprdAIRAGIAYVPEDRKGEGlvlDLSIRENITLASLDRLSRGGllDRRRERALAEEYIKRLRIkTPSPEQPVG 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24580555 184 NLSGG--QKkrLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVI 238
Cdd:COG1129 394 NLSGGnqQK--VVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVI 448
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
67-230 |
2.98e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSIEGSVTMNGAERnlsAFRKLSayimqDNQLHGNLTV-QE-- 142
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvYPHGSYEGEILFDGEVC---RFKDIR-----DSEALGIVIIhQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 143 ---AMTVATNLKLSkkfSKPEKHSMID---------DILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDE 210
Cdd:NF040905 89 lipYLSIAENIFLG---NERAKRGVIDwnetnrrarELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180
....*....|....*....|...
gi 24580555 211 PTSGL---DSStcfqciHLLKML 230
Cdd:NF040905 166 PTAALneeDSA------ALLDLL 182
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
62-216 |
3.08e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 62 NAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSIEGSVTMNGAER----NLSAFRKLSAYImqDNQLHGN 137
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRgsgeTIWDIKKHIGYV--SSSLHLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 138 LTVQeamTVATNLKLSKKFSK-------PEKHSMIDDILLTL-----SLSEHRYtmtRNLSGGQKKRLSIALELVSNPPI 205
Cdd:PRK10938 349 YRVS---TSVRNVILSGFFDSigiyqavSDRQQKLAQQWLDIlgidkRTADAPF---HSLSWGQQRLALIVRALVKHPTL 422
|
170
....*....|.
gi 24580555 206 MFFDEPTSGLD 216
Cdd:PRK10938 423 LILDEPLQGLD 433
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
63-268 |
3.58e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 63 AKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSS-------IEGSVTMNGAE-RNLSAFR--KLSAYIMQDN 132
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarVTGDVTLNGEPlAAIDAPRlaRLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 133 QLHGNLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSE---HRYTMTrnLSGGQKKRLSIALEL---------V 200
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATalvGRDVTT--LSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 201 SNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRT-VICTIHQP--SARlfeMFDQLYTLADGQCVYQGS 268
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPnlAAR---HADRIAMLADGAIVAHGA 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
70-227 |
7.62e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 70 VSGRLRSGELTAIMGPSGAGKST----LLNILSgyktsSIEGSVTMNG------AERNLSAFRKLSAYIMQD--NQLHGN 137
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTtgraLLRLVE-----SQGGEIIFNGqridtlSPGKLQALRRDIQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 138 LTVqeAMTVATNLKLSKKFSKPEKHSMIDDILLTLSL-SEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK10261 418 QTV--GDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170
....*....|.
gi 24580555 217 SSTCFQCIHLL 227
Cdd:PRK10261 496 VSIRGQIINLL 506
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
64-219 |
8.93e-09 |
|
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: 58.41 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSIEGSVTMNGAERnlsafrklsAYIMQDNQLHGNLTV--- 140
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKV---------GYLPQEPQLDPTKTVren 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 -QEAMTVATNL-----KLSKKFSKP--------EKHSMIDDILLTLSLSEHRYTMTR---------------NLSGGQKK 191
Cdd:TIGR03719 89 vEEGVAEIKDAldrfnEISAKYAEPdadfdklaAEQAELQEIIDAADAWDLDSQLEIamdalrcppwdadvtKLSGGERR 168
|
170 180
....*....|....*....|....*...
gi 24580555 192 RLSIALELVSNPPIMFFDEPTSGLDSST 219
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
70-216 |
9.32e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 70 VSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE---RNLSAfRKLSAYIMQDNQLHGNLTVQEamtv 146
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPvdaGDIAT-RRRVGYMSQAFSLYGELTVRQ---- 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 147 atNLKL-SKKFSKPEKH--SMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:NF033858 359 --NLELhARLFHLPAAEiaARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
66-288 |
1.10e-08 |
|
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: 58.77 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAFRKLSAYIMQDNQLHGnLTVQE--A 143
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS-EGKIKHSGRISFSPQTSWIMPGTIKDNIIFG-LSYDEyrY 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 144 MTVATNLKLSKKFSK-PEKHSMIddilltlsLSEHRYTmtrnLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST--- 219
Cdd:TIGR01271 519 TSVIKACQLEEDIALfPEKDKTV--------LGEGGIT----LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeke 586
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 220 CFQ-CihLLKMLAAGGRTVICTIHQPSARLfemfDQLYTLADGQCVYQGSTKQLV---PFLSTLNLECPSYHN 288
Cdd:TIGR01271 587 IFEsC--LCKLMSNKTRILVTSKLEHLKKA----DKILLLHEGVCYFYGTFSELQakrPDFSSLLLGLEAFDN 653
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-272 |
1.14e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 25 AQIVPAQPKTlqhlpkrPAVDLAFHNLTYRVKegnrsNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSS 104
Cdd:PLN03232 603 AQNPPLQPGA-------PAISIKNGYFSWDSK-----TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 105 IEGSVTMNGAernlsafrklSAYIMQDNQLHgNLTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLtlsLSEHRYTMTR- 183
Cdd:PLN03232 671 ETSSVVIRGS----------VAYVPQVSWIF-NATVRENILFGSDFESERYWRAIDVTALQHDLDL---LPGRDLTEIGe 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 184 ---NLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQpsARLFEMFDQLYTLAD 260
Cdd:PLN03232 737 rgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSE 814
|
250
....*....|..
gi 24580555 261 GQCVYQGSTKQL 272
Cdd:PLN03232 815 GMIKEEGTFAEL 826
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
46-272 |
3.00e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.64 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNrsNAKTILKGVSGRLRSGELTAIMGPSGAGKS-TLLNILS-------GYKTSSI--EGSVTMNGAE 115
Cdd:PRK15134 6 LAIENLSVAFRQQQ--TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRllpsppvVYPSGDIrfHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 116 RNLSAFR-KLSAYIMQD-----NQLHgNLTVQEAMTVATNLKLSKKFSKPEkhsmiddILLTLSLSEHRYTMTR------ 183
Cdd:PRK15134 84 QTLRGVRgNKIAMIFQEpmvslNPLH-TLEKQLYEVLSLHRGMRREAARGE-------ILNCLDRVGIRQAAKRltdyph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 184 NLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQLYTLADGQC 263
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
....*....
gi 24580555 264 VYQGSTKQL 272
Cdd:PRK15134 236 VEQNRAATL 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
77-219 |
6.54e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 77 GELTAIMGPSGAGKSTLLNILSG----------YKTS------------SIEGSVTMNGAE------RNLSAFRKLSAYI 128
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGevllddgriiYEQDlivarlqqdpprNVEGTVYDFVAEgieeqaEYLKRYHDISHLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 129 MQD------NQLHgnlTVQEAMTVATNLKLSKKfskpekhsmIDDILLTLSLSEHryTMTRNLSGGQKKRLSIALELVSN 202
Cdd:PRK11147 109 ETDpseknlNELA---KLQEQLDHHNLWQLENR---------INEVLAQLGLDPD--AALSSLSGGWLRKAALGRALVSN 174
|
170
....*....|....*..
gi 24580555 203 PPIMFFDEPTSGLDSST 219
Cdd:PRK11147 175 PDVLLLDEPTNHLDIET 191
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
72-217 |
8.02e-08 |
|
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: 53.95 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 72 GRLRSGELTAIMGPSGAGKSTLLNILSGyktsSIEGSVTMNGAERNLSAFRklSAYIMQDNQLhgnlTVQEAMTVATNLK 151
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAG----VLKPDEGDIEIELDTVSYK--PQYIKADYEG----TVRDLLSSITKDF 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24580555 152 LSKKFSKPE--KHSMIDDILltlslsEHRYTmtrNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:cd03237 90 YTHPYFKTEiaKPLQIEQIL------DREVP---ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
64-216 |
1.30e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.19 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERnlsafrklSAYIMQdnQLHGNLTVqeA 143
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD-EGVIKRNGKLR--------IGYVPQ--KLYLDTTL--P 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24580555 144 MTVATNLKLskkfsKPEKHSmiDDILLTLSLSE----HRYTMTRnLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK09544 84 LTVNRFLRL-----RPGTKK--EDILPALKRVQaghlIDAPMQK-LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
156-262 |
1.49e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 156 FSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGR 235
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110
....*....|....*....|....*....|..
gi 24580555 236 TVICTIH-----QPSARLFEMFDQLYTLADGQ 262
Cdd:NF000106 196 TVLLTTQymeeaEQLAHELTVIDRGRVIADGK 227
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
66-243 |
2.47e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSSIEGSVTMNGAERNLSAFRKLSAYIMQDNQLHGNLTVQEam 144
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRE-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 145 tvatNLKLSKKFSKPEKHsmIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCI 224
Cdd:PRK13540 94 ----NCLYDIHFSPGAVG--ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*....
gi 24580555 225 HLLKMLAAGGRTVICTIHQ 243
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
45-287 |
2.48e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.09 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 45 DLAFHNLTYRVKEGNRSNAKTiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTS----SIEGSVTMNGAERNLSA 120
Cdd:PRK13645 6 DIILDNVSYTYAKKTPFEFKA-LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISetgqTIVGDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYI-----MQDNQLHGNLTVQEAMTVATNLKLSKKfskpEKHSMIDDILLTLSLSEHRYTMTR-NLSGGQKKRLS 194
Cdd:PRK13645 85 VKRLRKEIglvfqFPEYQLFQETIEKDIAFGPVNLGENKQ----EAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 195 IALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAG-GRTVICTIHQPSaRLFEMFDQLYTLADGQCVYQGSTKQL- 272
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIGSPFEIf 239
|
250
....*....|....*..
gi 24580555 273 --VPFLSTLNLECPSYH 287
Cdd:PRK13645 240 snQELLTKIEIDPPKLY 256
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
74-216 |
2.59e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 74 LRSGELTAIMGPSGAGKSTLLNILSGYKTSSIeGSVTMNGA-ERNLSAFR--KLSAYI--MQDNQLHGNLTVQ--EAMTV 146
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNL-GDYEEEPSwDEVLKRFRgtELQNYFkkLYNGEIKVVHKPQyvDLIPK 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 147 ATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK13409 175 VFKGKVRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
66-219 |
2.64e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNIL----------------------------SGYKTSSI------EGSVTM 111
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyQGDEEQNVgmknvnEFSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 112 NGAERNLSAFRKLSAYIMQD--NQLHGNL---------TVQEA----MTVATNLKLSKKFSKPE------KHSMIDDILL 170
Cdd:PTZ00265 1263 EGGSGEDSTVFKNSGKILLDgvDICDYNLkdlrnlfsiVSQEPmlfnMSIYENIKFGKEDATREdvkracKFAAIDEFIE 1342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24580555 171 TLSlseHRYTMT-----RNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST 219
Cdd:PTZ00265 1343 SLP---NKYDTNvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
67-251 |
4.41e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.71 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLL-------NILSGYKtssIEGSVTMNGaeRNLSA---------------FRKL 124
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR---VEGKVTFHG--KNLYApdvdpvevrrrigmvFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 125 S----------AYIMQDNQLHGNLTvqeaMTVATNLKLSKKFSKpekhsmIDDILLTLSLSehrytmtrnLSGGQKKRLS 194
Cdd:PRK14243 101 NpfpksiydniAYGARINGYKGDMD----ELVERSLRQAALWDE------VKDKLKQSGLS---------LSGGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24580555 195 IALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTiH--QPSARLFEM 251
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT-HnmQQAARVSDM 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
67-245 |
4.74e-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: 50.40 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLN-ILSGYKTSSIEGSVTMNgaERNLSAF-RKLSAYImqDNQLhGNLTVQEAM 144
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNeGLYASGKARLISFLPKF--SRNKLIFiDQLQFLI--DVGL-GYLTLGQKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 145 TvatnlklskkfskpekhsmiddilltlslsehrytmtrNLSGGQKKRLSIALELVSNPP--IMFFDEPTSGLDSSTCFQ 222
Cdd:cd03238 86 S--------------------------------------TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180
....*....|....*....|...
gi 24580555 223 CIHLLKMLAAGGRTVICTIHQPS 245
Cdd:cd03238 128 LLEVIKGLIDLGNTVILIEHNLD 150
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
71-217 |
8.50e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 71 SGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNgaernlsafRKLS---AYIMQDNqlhgNLTVQEAMTVA 147
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPD-EGEVDED---------LKISykpQYISPDY----DGTVEEFLRSA 425
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 148 TNLKLSKKFSKPEkhsmiddILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:COG1245 426 NTDDFGSSYYKTE-------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
74-216 |
9.26e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 74 LRSGELTAIMGPSGAGKSTLLNILSGyktssiE-----GSVTMNGA-ERNLSAFRK--LSAYI--MQDNQLHgnlTVQEA 143
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSG------ElkpnlGDYDEEPSwDEVLKRFRGteLQDYFkkLANGEIK---VAHKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 144 MTVAtnlKLSKKFS--------KPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGL 215
Cdd:COG1245 167 QYVD---LIPKVFKgtvrelleKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
.
gi 24580555 216 D 216
Cdd:COG1245 244 D 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
50-248 |
9.47e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.61 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEGNRSnaktILKGVSGRLRSGELTAIMGPSGAGKSTLLNILsgYKTSSIEGSVTMNGAERN---LSAFRK--- 123
Cdd:TIGR01271 1222 GLTAKYTEAGRA----VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL--LRLLSTEGEIQIDGVSWNsvtLQTWRKafg 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 124 --------LSAYIMQDNQLHGNLTVQEAMTVATNLKLSKKFSK-PEKhsmiddilLTLSLSEHRYTmtrnLSGGQKKRLS 194
Cdd:TIGR01271 1296 vipqkvfiFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQfPDK--------LDFVLVDGGYV----LSNGHKQLMC 1363
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 24580555 195 IALELVSNPPIMFFDEPTSGLDSSTcFQCIHLLKMLAAGGRTVICTIHQPSARL 248
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDPVT-LQIIRKTLKQSFSNCTVILSEHRVEALL 1416
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
67-238 |
1.04e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLS---AYIMQDNQ---LHGNLT 139
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKS-AGTITLHGKKiNNHNANEAINhgfALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VqEAMTVATNLK--------LSKKFSKPEKHSMIDDilLTLSLSEHRyTMTRNLSGGQKKRLSIALELVSNPPIMFFDEP 211
Cdd:PRK10982 343 I-GFNSLISNIRnyknkvglLDNSRMKSDTQWVIDS--MRVKTPGHR-TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180
....*....|....*....|....*..
gi 24580555 212 TSGLDSSTCFQCIHLLKMLAAGGRTVI 238
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKKDKGII 445
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
67-264 |
1.42e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSG-YKTSsiEGSVTMNGAERNL-SAFRKLSAYImqdNQLHGNLTVQEAM 144
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiYQKD--SGSILFQGKEIDFkSSKEALENGI---SMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 145 TVATNLKLSKkfsKPEKHSMID---------DILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGL 215
Cdd:PRK10982 89 SVMDNMWLGR---YPTKGMFVDqdkmyrdtkAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24580555 216 ---DSSTCFQCIHLLKMLAAGgrtvICTIHQPSARLFEMFDQLYTLADGQCV 264
Cdd:PRK10982 166 tekEVNHLFTIIRKLKERGCG----IVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
50-248 |
2.18e-06 |
|
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: 49.85 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 50 NLTYRVKEGnrsnAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILsgYKTSSIEGSVTMNGAERN---LSAFRKLSA 126
Cdd:cd03289 7 DLTAKYTEG----GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAF--LRLLNTEGDIQIDGVSWNsvpLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 127 YIMQDNQLHGNltvqeamTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEH----RYTMTRN---LSGGQKKRLSIALEL 199
Cdd:cd03289 81 VIPQKVFIFSG-------TFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFpgqlDFVLVDGgcvLSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24580555 200 VSNPPIMFFDEPTSGLDSSTcFQCIHLLKMLAAGGRTVICTIHQPSARL 248
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPIT-YQVIRKTLKQAFADCTVILSEHRIEAML 201
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
76-245 |
2.41e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.75 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 76 SGELTAIMGPSGAGKSTLLNILSGYKTSSIEGSVTMNGaernlsafrklsayimqdnqlhgnltvqeamtvatnlklskk 155
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 156 fskpekhSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSST------CFQCIHLLKM 229
Cdd:smart00382 39 -------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLL 111
|
170
....*....|....*.
gi 24580555 230 LAAGGRTVICTIHQPS 245
Cdd:smart00382 112 KSEKNLTVILTTNDEK 127
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
76-258 |
2.87e-06 |
|
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: 47.74 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 76 SGELTAIMGPSGAGKSTLLNILsGYktssiegsvtmngaernlsafrklsAYIMQDNQLHGNLTVQEAMTVATnlklskk 155
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI-GL-------------------------ALGGAQSATRRRSGVKAGCIVAA------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 156 fSKPEKHSMIDdilltlslsehrytmtrNLSGGQKKRLSIALEL----VSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLA 231
Cdd:cd03227 67 -VSAELIFTRL-----------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHL 128
|
170 180
....*....|....*....|....*..
gi 24580555 232 AGGRTVICTIHQPsaRLFEMFDQLYTL 258
Cdd:cd03227 129 VKGAQVIVITHLP--ELAELADKLIHI 153
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
54-242 |
3.09e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.43 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 54 RVKE----GNRSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVTMNGaERNLSAFrklsayim 129
Cdd:PRK13546 23 RMKDalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGG-SLSPTVGKVDRNG-EVSVIAI-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 130 qDNQLHGNLTVQEAMTVATnlkLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFD 209
Cdd:PRK13546 93 -SAGLSGQLTGIENIEFKM---LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190
....*....|....*....|....*....|...
gi 24580555 210 EPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIH 242
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSH 201
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
64-216 |
3.68e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTsSIEGSVT-MNGAERnlsafrklsAYIMQDNQLHGNLTV-- 140
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-EFEGEARpAPGIKV---------GYLPQEPQLDPEKTVre 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 --QEAMTVATNLK-----LSKKFSKP--------EKHSMIDDILLTLSL--SEHRYTMT-------------RNLSGGQK 190
Cdd:PRK11819 90 nvEEGVAEVKAALdrfneIYAAYAEPdadfdalaAEQGELQEIIDAADAwdLDSQLEIAmdalrcppwdakvTKLSGGER 169
|
170 180
....*....|....*....|....*.
gi 24580555 191 KRLSIALELVSNPPIMFFDEPTSGLD 216
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-219 |
4.23e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 33 KTLQHLPKRPAVDLAFHNLTYRVKEgnrsnaktILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMN 112
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYDTRKDVE--------IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT-EGDIIIN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 113 GAER----NLSAFRKLSAYIMQDNQLHGN------------LTVQEAM-------TVATNLKLSKKFSKPEK-------- 161
Cdd:PTZ00265 446 DSHNlkdiNLKWWRSKIGVVSQDPLLFSNsiknnikyslysLKDLEALsnyynedGNDSQENKNKRNSCRAKcagdlndm 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 162 ---------------HSMIDD---------ILL---TLSLSEHRYTMT----RNLSGGQKKRLSIALELVSNPPIMFFDE 210
Cdd:PTZ00265 526 snttdsneliemrknYQTIKDsevvdvskkVLIhdfVSALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDE 605
|
....*....
gi 24580555 211 PTSGLDSST 219
Cdd:PTZ00265 606 ATSSLDNKS 614
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
66-288 |
5.27e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 48.70 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 66 ILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAernlSAFRKLSAYIM----QDNQLHGnLTVQ 141
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS-EGKIKHSGR----ISFSSQFSWIMpgtiKENIIFG-VSYD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 142 E--AMTVATNLKLSKKFSK-PEKHSMIddilltlsLSEHRYTmtrnLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSS 218
Cdd:cd03291 126 EyrYKSVVKACQLEEDITKfPEKDNTV--------LGEGGIT----LSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 219 TCFQCIH--LLKMLAAGGRTVICTihqpSARLFEMFDQLYTLADGQCVYQGSTKQLV---PFLSTLNLECPSYHN 288
Cdd:cd03291 194 TEKEIFEscVCKLMANKTRILVTS----KMEHLKKADKILILHEGSSYFYGTFSELQslrPDFSSKLMGYDTFDQ 264
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
67-245 |
5.75e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.50 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYkTSSIEGSVTMNGAernlsafrklSAYIMQDNQLHGNLTVQEAMtv 146
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGV-TMPNKGTVDIKGS----------AALIAISSGLNGQLTGIENI-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 147 atNLK-LSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIH 225
Cdd:PRK13545 107 --ELKgLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180
....*....|....*....|
gi 24580555 226 LLKMLAAGGRTVICTIHQPS 245
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLS 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
70-262 |
1.07e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.51 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 70 VSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAE-RNLSAFRKLSA---YIMQDNQLHG-----NLTV 140
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR-GGRIMLNGKEiNALSTAQRLARglvYLPEDRQSSGlyldaPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 141 QEAMTVATNLKLskkFSKPEKHSMIDD---ILLTLSLSEHRYTMtRNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:PRK15439 361 NVCALTHNRRGF---WIKPARENAVLEryrRALNIKFNHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 24580555 218 STCFQCIHLLKMLAAGGRTVICTihqpSARLFE---MFDQLYTLADGQ 262
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGE 480
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
77-217 |
2.33e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 77 GELTAIMGPSGAGKSTLLNILSGYKTSSIEGSVTMNGAernlsafrklSAYIMQDNQLHgNLTVQEamtvatNLKLSKKF 156
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGT----------VAYVPQVSWIF-NATVRD------NILFGSPF 705
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 157 SKPEKHSMID--------DILLTLSLSE--HRYTmtrNLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:PLN03130 706 DPERYERAIDvtalqhdlDLLPGGDLTEigERGV---NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
70-227 |
2.94e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 70 VSGRLRSGELTAIMGPSGAGKS-TLLNI--LSGYKTSSIEGSVTMNGaeRNLSAF-----RKLS----AYIMQDNQLHGN 137
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAImgLIDYPGRVMAEKLEFNG--QDLQRIsekerRNLVgaevAMIFQDPMTSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 138 LTVQEAMTVATNLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMT---RNLSGGQKKRLSIALELVSNPPIMFFDEPTSG 214
Cdd:PRK11022 104 PCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDvypHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170
....*....|...
gi 24580555 215 LDSSTCFQCIHLL 227
Cdd:PRK11022 184 LDVTIQAQIIELL 196
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
45-248 |
7.08e-05 |
|
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: 44.90 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 45 DLAFHNLTYRVKegnrSNAKTILKGVSGRLRSGELTAIMGPSGAGKSTLlnILSGYKTSSI-EGSVTMNG---AERNLSA 120
Cdd:cd03288 19 EIKIHDLCVRYE----NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDIfDGKIVIDGidiSKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 121 FRKLSAYIMQDNQLHGNltvqeamTVATNLklskkfsKPEKHSMIDDILLTLSLSEHRYTMT--------------RNLS 186
Cdd:cd03288 93 LRSRLSIILQDPILFSG-------SIRFNL-------DPECKCTDDRLWEALEIAQLKNMVKslpggldavvteggENFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 187 GGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTcFQCIHLLKMLAAGGRTVICTIHQPSARL 248
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVSTIL 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
64-216 |
7.61e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 64 KTILKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGyKTSSIEGSVtmngaernlsafrKLS-----AYIMQDN--QLHG 136
Cdd:PRK15064 332 GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-ELEPDSGTV-------------KWSenaniGYYAQDHayDFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 137 NLTVQEAMTVATNlklskkfskpEKHS--MIDDILLTLSLSEHRYTMT-RNLSGGQKKRLSIALELVSNPPIMFFDEPTS 213
Cdd:PRK15064 398 DLTLFDWMSQWRQ----------EGDDeqAVRGTLGRLLFSQDDIKKSvKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTN 467
|
...
gi 24580555 214 GLD 216
Cdd:PRK15064 468 HMD 470
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
185-242 |
9.95e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 9.95e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24580555 185 LSGGQKKRLSIALEL---VSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIH 242
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
79-217 |
2.14e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.98 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 79 LTAIMGPSGAGKSTLLNILSgYKTSSiEGSVTMNGAERNLSAFRK----LSAYIMQDNQLHGNLTVQEAMTVATNLKlsk 154
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK-YALTG-ELPPNSKGGAHDPKLIREgevrAQVKLAFENANGKKYTITRSLAILENVI--- 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24580555 155 kFSKPEKhsmIDDILLTlslsehrytMTRNLSGGQKKRLSIALELV------SNPPIMFFDEPTSGLDS 217
Cdd:cd03240 99 -FCHQGE---SNWPLLD---------MRGRCSGGEKVLASLIIRLAlaetfgSNCGILALDEPTTNLDE 154
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
76-99 |
2.31e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 43.16 E-value: 2.31e-04
10 20
....*....|....*....|....
gi 24580555 76 SGELTAIMGPSGAGKSTLLNILSG 99
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
242-296 |
3.00e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 43.74 E-value: 3.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 242 HQPSARLFEMFDQLYTLAD-GQCVYQGSTKQLVPFLSTLNLECPSYHNPASYVIEV 296
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDI 56
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
475-620 |
4.04e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 43.15 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 475 SNLGFLFFNMLFLMYTSMTITILSFPLEMpvlLKENFNR--------WYSLKSYYLAISVADLPFQAIFCVIYVSIVYYF 546
Cdd:pfam12698 155 PQSGYAYYLVGLILMIIILIGAAIIAVSI---VEEKESRikerllvsGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGI 231
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24580555 547 TSQPWELFR-FSMFLSACLLISFVAQSVGLVVGAAMNVQNGVFLapvMSVPFLLFSGFFVSFDAIPVYLRWITYL 620
Cdd:pfam12698 232 GIPFGNLGLlLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGI---VILLLSGFFGGLFPLEDPPSFLQWIFSI 303
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
46-245 |
9.19e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 46 LAFHNLTYRVKEGNrsnaktiLKGVSGRLRSGELTAIMGPSGAGKSTLLNILSGYKTSSiEGSVTMNGAERNLSAfRKLS 125
Cdd:PRK13541 2 LSLHQLQFNIEQKN-------LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPS-SGNIYYKNCNINNIA-KPYC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 126 AYIMQdnqlhgNLTVQEAMTVATNLKLSKKF--SKPEKHSMIDDILLTLSLSEHRYtmtrNLSGGQKKRLSIALELVSNP 203
Cdd:PRK13541 73 TYIGH------NLGLKLEMTVFENLKFWSEIynSAETLYAAIHYFKLHDLLDEKCY----SLSSGMQKIVAIARLIACQS 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24580555 204 PIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPS 245
Cdd:PRK13541 143 DLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLES 184
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
76-99 |
1.09e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 40.60 E-value: 1.09e-03
10 20
....*....|....*....|....
gi 24580555 76 SGELTAIMGPSGAGKSTLLNILSG 99
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
67-242 |
1.19e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLN-ILSGYKTSSIEGSVTMNGAERNLSAFRKLSAYIMQDNQLHGN------LT 139
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdTLYPALANRLNGAKTVPGRYTSIEGLEHLDKVIHIDQSPIGRtprsnpAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEAMTVATNL----KLSKK-------FS---------------------------------------KPE------KHS 163
Cdd:TIGR00630 704 YTGVFDEIRELfaetPEAKVrgytpgrFSfnvkggrceacqgdgvikiemhflpdvyvpcevckgkryNREtlevkyKGK 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 164 MIDDILlTLSLSE-----------HRYTMT---------------RNLSGGQKKRLSIALEL---VSNPPIMFFDEPTSG 214
Cdd:TIGR00630 784 NIADVL-DMTVEEayeffeavpsiSRKLQTlcdvglgyirlgqpaTTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTG 862
|
250 260
....*....|....*....|....*...
gi 24580555 215 LDSSTCFQCIHLLKMLAAGGRTVICTIH 242
Cdd:TIGR00630 863 LHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
67-243 |
1.23e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.06 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 67 LKGVSGRLRSGELTAIMGPSGAGKSTLLN-ILSGYKTSSIEGSVTMNGAERNLSAFRKLSAYIMQDNQLHGN------LT 139
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPIGRtprsnpAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 140 VQEAMTVATNLKLS----KKFSkPE------KHSMIDDILlTLSLSE-----------HRYTMT---------------R 183
Cdd:cd03271 91 YTGVFDEIRELFCEvckgKRYN-REtlevryKGKSIADVL-DMTVEEaleffenipkiARKLQTlcdvglgyiklgqpaT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24580555 184 NLSGGQKKRLSIALEL---VSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQ 243
Cdd:cd03271 169 TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
73-107 |
2.06e-03 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 40.93 E-value: 2.06e-03
10 20 30
....*....|....*....|....*....|....*...
gi 24580555 73 RLRSGELTAIMGPSGAGKSTLLNILSGYKT---SSIEG 107
Cdd:pfam12631 90 ILREGIKVVIVGKPNVGKSSLLNALLGEERaivTDIPG 127
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
74-99 |
2.71e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 40.69 E-value: 2.71e-03
10 20
....*....|....*....|....*.
gi 24580555 74 LRSGELTAIMGPSGAGKSTLLNILSG 99
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLG 217
|
|
| trmE |
cd04164 |
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ... |
75-107 |
3.38e-03 |
|
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.
Pssm-ID: 206727 [Multi-domain] Cd Length: 159 Bit Score: 38.63 E-value: 3.38e-03
10 20 30
....*....|....*....|....*....|....*.
gi 24580555 75 RSGELTAIMGPSGAGKSTLLNILSGYK---TSSIEG 107
Cdd:cd04164 1 REGIKVVIAGKPNVGKSSLLNALAGRDraiVSDIAG 36
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
72-217 |
4.13e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.71 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 72 GRLRSGELTAIMGPSGAGKSTLLNILSGyktssiegsvTMNGAERNLSAFRKLSAYimqdnqlhgnltvqeamtvatnlk 151
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAG----------QLIPNGDNDEWDGITPVY------------------------ 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24580555 152 lskkfsKPEKHSmiddilltlslsehrytmtrnLSGGQKKRLSIALELVSNPPIMFFDEPTSGLDS 217
Cdd:cd03222 66 ------KPQYID---------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
73-107 |
6.46e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 39.66 E-value: 6.46e-03
10 20 30
....*....|....*....|....*....|....*...
gi 24580555 73 RLRSGELTAIMGPSGAGKSTLLNILSGYK---TSSIEG 107
Cdd:COG0486 209 LLREGIKVVIVGRPNVGKSSLLNALLGEEraiVTDIAG 246
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
50-105 |
6.59e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 39.03 E-value: 6.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24580555 50 NLTYRVKEgnrSNAKTiLKGVSgRLRS---GELTAIMGPSGAGKSTLLNILSG---YKTSSI 105
Cdd:PRK00098 139 AIGYDVLE---LSAKE-GEGLD-ELKPllaGKVTVLAGQSGVGKSTLLNALAPdleLKTGEI 195
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
149-245 |
7.56e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 149 NLKLSKKFSKPEKHSMIDDILLTLSLSEHRYTMTRNL-----SGGQKK---RLSIALELVSNPPIMFFDEPTSGLDSSTC 220
Cdd:pfam13304 196 DLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELpafelSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLL 275
|
90 100
....*....|....*....|....*
gi 24580555 221 FQCIHLLKMLAAGGRTVICTIHQPS 245
Cdd:pfam13304 276 RRLLELLKELSRNGAQLILTTHSPL 300
|
|
| Twinkle_C |
cd01122 |
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ... |
66-98 |
7.75e-03 |
|
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.
Pssm-ID: 410867 Cd Length: 266 Bit Score: 38.76 E-value: 7.75e-03
10 20 30
....*....|....*....|....*....|...
gi 24580555 66 ILKGvsgrLRSGELTAIMGPSGAGKSTLLNILS 98
Cdd:cd01122 36 LLKG----HRRGELTIFTGPTGSGKTTFLSEYS 64
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
185-273 |
9.56e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 38.63 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24580555 185 LSGGQKKRLSIALELVSNPPIMFFDEPTSGLDSSTCFQCIHLLKMLAAGGRTVICTIHQPSARLFEMFDQLYTLADGQCV 264
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
....*....
gi 24580555 265 YQGSTKQLV 273
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| |
