|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
68-687 |
0e+00 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 1050.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 68 LTYAWHNMDIFGAVNQPGSgWRQLVNRTRGLFCNERhipaPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRS 147
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGS-WKQLVSRLRGCFCRER----PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 148 PQGIQVSPSgmRLLNGQPVDAKEMQARCAYVQQDDLFIGSLTAREHLIFQAMVRMPRHLTYRQRVARVDQVIQELSLSKC 227
Cdd:TIGR00955 76 PKGVKGSGS--VLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKC 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 228 QHTIIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFEL 307
Cdd:TIGR00955 154 ANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 308 FDKILLMAEGRVAFLGTPSEAVDFFSYVGAQCPTNYNPADFYVQVLAVVPGREIESRDRIAKICDNFAISKVARDMEQLL 387
Cdd:TIGR00955 234 FDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENESRERIEKICDSFAVSDIGRDMLVNT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 388 ATKNLEKPL----EQPENGYTYKATWFMQFRAVLWRSWLSVLKEPLLVKVRLIQTTMVAILIGLIFLGQQLTQVGVMNIN 463
Cdd:TIGR00955 314 NLWSGKAGGlvkdSENMEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 464 GAIFLFLTNMTFQNVFATINVFTSELPVFMREARSRLYRCDTYFLGKTIAELPLFLTVPLVFTAIAYPMIGLRAGVLHFF 543
Cdd:TIGR00955 394 GALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 544 NCLALVTLVANVSTSFGYLISCASSSTSMALSVGPPVIIPFLLFGGFFLNSGSVPVYLKWLSYLSWFRYANEGLLINQWA 623
Cdd:TIGR00955 474 TFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWS 553
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 624 DVEPGEisCTSSNTT--CPSSGKVILETLNFSAADLPLDYVGLAILIVSFRVLAYLALRLRARRKE 687
Cdd:TIGR00955 554 DVDNIE--CTSANTTgpCPSSGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
110-680 |
2.17e-92 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 300.64 E-value: 2.17e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRspqgIQVSP-SGMRLLNGQPVdAKEMQARCAYVQQDDLFIGSL 188
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGR----IQGNNfTGTILANNRKP-TKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHLIFQAMVRMPRHLTYRQRVARVDQVIQELSLSKCQHTIIGvPGRVKGLSGGERKRLAFASEALTDPPLLICDEPT 268
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIG-NSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 269 SGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPSEAVDFFSYVGAQCPTNYNPADF 348
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADF 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 349 YV-------QVLAVVPGREIESRDRIAKICDNFAISKV--ARDMEQLLATKN----LEKPLEQPENGYTYKATWFMQFRA 415
Cdd:PLN03211 315 LLdlangvcQTDGVSEREKPNVKQSLVASYNTLLAPKVkaAIEMSHFPQANArfvgSASTKEHRSSDRISISTWFNQFSI 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 416 VLWRSwLSVLKEPLLVKVRLIQTTMVAILIGLIFLGQQLtqvgvMNINGAIFLFLTNMTFQNVFATIN---VFTSELPVF 492
Cdd:PLN03211 395 LLQRS-LKERKHESFNTLRVFQVIAAALLAGLMWWHSDF-----RDVQDRLGLLFFISIFWGVFPSFNsvfVFPQERAIF 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 493 MREARSRLYRCDTYFLGKTIAELPLFLTVPLVFTAIAYPMIGLRAGVLHFFNCLALVTLVANVSTSFGYLISCASSSTSM 572
Cdd:PLN03211 469 VKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKK 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 573 ALSVGPPVIIPFLLFGGFFLNsgSVPVYLKWLSYLSWFRYANEgLLINqwadVEPGEISCTSSNTTCPSSGKVILETLNF 652
Cdd:PLN03211 549 ASTIVTVTMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYR-LLIN----VQYGEGKRISSLLGCSLPHGSDRASCKF 621
|
570 580 590
....*....|....*....|....*....|....
gi 17136592 653 SAADL-----PLDYVGLAILI-VSFRVLAYLALR 680
Cdd:PLN03211 622 VEEDVagqisPATSVSVLIFMfVGYRLLAYLALR 655
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
88-650 |
4.86e-82 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 283.92 E-value: 4.86e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 88 WRQLvnrtrglfCNERHIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGiqVSPSGMRLLNGQPVD 167
Cdd:TIGR00956 762 WRNL--------TYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTG--VITGGDRLVNGRPLD 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 168 AKeMQARCAYVQQDDLFIGSLTAREHLIFQAMVRMPRHLTYRQRVARVDQVIQELSLSKCQHTIIGVPGrvKGLSGGERK 247
Cdd:TIGR00956 832 SS-FQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPG--EGLNVEQRK 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 248 RLAFASEALTDPPLLI-CDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEG-RVAFLGTP 325
Cdd:TIGR00956 909 RLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDL 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 326 SEA----VDFFSYVGA-QCPTNYNPADFYVQVLAVVPGreiesrdriAKICDNFAisKVARDMEQLLATKN----LEKPL 396
Cdd:TIGR00956 989 GENshtiINYFEKHGApKCPEDANPAEWMLEVIGAAPG---------AHANQDYH--EVWRNSSEYQAVKNeldrLEAEL 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 397 EQ------PENGYTYKATWFMQFRAVLWRSWLSVLKEPLLVKVRLIQTTMVAILIGLIFLGQQLTQVGVMNINGAIFLFL 470
Cdd:TIGR00956 1058 SKaeddndPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQMFAVFMAT 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 471 tnmtfqnVFATINVfTSELPVFM--------REARSRLYRCDTYFLGKTIAELPLFLTVPLVFTAIAYPMIGL-----RA 537
Cdd:TIGR00956 1138 -------VLFNPLI-QQYLPPFVaqrdlyevRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFywnasKT 1209
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 538 GVLH--FFNCLALVTLVANVSTSFGYLISCASSSTSMALSVGPPVIIPFLLFGGFFLNSGSVPVYLKWLSYLSWFRYANE 615
Cdd:TIGR00956 1210 GQVHerGVLFWLLSTMFFLYFSTLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQ 1289
|
570 580 590
....*....|....*....|....*....|....*
gi 17136592 616 GLLINQWADVePGEISCTSSNTTCPSSGKVILETL 650
Cdd:TIGR00956 1290 ALLSTGLADV-PVTCKVKELLTFNPPSGQTCGEYM 1323
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
112-323 |
7.70e-77 |
|
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: 245.64 E-value: 7.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGiqVSPSGMRLLNGQPVDAKEMQARCAYVQQDDLFIGSLTAR 191
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGG--GTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 192 EHLIFQAMVRMPRHLTYRQRVARVDQViqelSLSKCQHTIIGVPgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 271
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIRKKRVEDV----LLRDLALTRIGGN-LVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17136592 272 DSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLG 323
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
109-323 |
2.35e-71 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 229.75 E-value: 2.35e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIqvspSGMRLLNGQPVDAKEMQARCAYVQQDDLFIGS 187
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGV----SGEVLINGRPLDKRSFRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 LTAREHLIFQAmvrmprhltyrqrvarvdqviqelslskcqhtiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEP 267
Cdd:cd03213 97 LTVRETLMFAA--------------------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 268 TSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLG 323
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
102-626 |
3.41e-62 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 225.50 E-value: 3.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 102 ERHIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQG-----IQVSpsgmrllnGQPvDAKEMQARCA 176
Cdd:PLN03140 885 EQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiegdIRIS--------GFP-KKQETFARIS 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 177 -YVQQDDLFIGSLTAREHLIFQAMVRMPRHLTYRQRVARVDQVIQELSLSKCQHTIIGVPGrVKGLSGGERKRLAFASEA 255
Cdd:PLN03140 956 gYCEQNDIHSPQVTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPG-VTGLSTEQRKRLTIAVEL 1034
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 256 LTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAE-GRVAFLGT----PSEAVD 330
Cdd:PLN03140 1035 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPlgrnSHKIIE 1114
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 331 FFSYVGA--QCPTNYNPADFYVQVLAVVPgrEIesrdriaKICDNFAISKVARDMEQllATKNLEKPLEQPENGYT--YK 406
Cdd:PLN03140 1115 YFEAIPGvpKIKEKYNPATWMLEVSSLAA--EV-------KLGIDFAEHYKSSSLYQ--RNKALVKELSTPPPGASdlYF 1183
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 407 ATWFM-----QFRAVLWRSWLSVLKEPLLVKVRLIQTTMVAILIGLIF--LGQQLTQVGVMN-INGAIFLFLTNMTFQNV 478
Cdd:PLN03140 1184 ATQYSqstwgQFKSCLWKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFwkVGTKRSNANDLTmVIGAMYAAVLFVGINNC 1263
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 479 FATINVFTSELPVFMREARSRLYRCDTYFLGKTIAELPLFLTVPLVFTAIAYPMIGLRAGVLHFFNCLALVTLVANVSTS 558
Cdd:PLN03140 1264 STVQPMVAVERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTY 1343
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136592 559 FGYLISCASSSTSMALSVGPPVIIPFLLFGGFFLNSGSVP---VYLKWLSYLSWFRYaneGLLINQWADVE 626
Cdd:PLN03140 1344 YGMMTVSLTPNQQVAAIFAAAFYGLFNLFSGFFIPRPKIPkwwVWYYWICPVAWTVY---GLIVSQYGDVE 1411
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
86-646 |
3.31e-56 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 207.65 E-value: 3.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 86 SGWRQLVNRTRGlfcnerhipaPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSpQGIQVSPSGMRLLNGQP 165
Cdd:TIGR00956 60 RGFRKLKKFRDT----------KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNT-DGFHIGVEGVITYDGIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 166 VD--AKEMQARCAYVQQDDLFIGSLTAREHLIFQAMVRMPRH-------LTYRQRVArvDQVIQELSLSKCQHTIIGvPG 236
Cdd:TIGR00956 129 PEeiKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQNrpdgvsrEEYAKHIA--DVYMATYGLSHTRNTKVG-ND 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 237 RVKGLSGGERKRLAFAsEALTDPPLLIC-DEPTSGLDSFTAHSVVQVLKKLSQKGK-TVILTIHQPSSELFELFDKILLM 314
Cdd:TIGR00956 206 FVRGVSGGERKRVSIA-EASLGGAKIQCwDNATRGLDSATALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 315 AEGRVAFLGTPSEAVDFFSYVGAQCPTNYNPADFYVQVLAvvPGREI---ESRDRIAKICDNFA--------ISKVARDM 383
Cdd:TIGR00956 285 YEGYQIYFGPADKAKQYFEKMGFKCPDRQTTADFLTSLTS--PAERQikpGYEKKVPRTPQEFEtywrnspeYAQLMKEI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 384 EQLLATKNLEKPLE---------QPENGYT---YKATWFMQFRAVLWRSWLSVLKEPLLVKVRLIQTTMVAILIGLIFLG 451
Cdd:TIGR00956 363 DEYLDRCSESDTKEayreshvakQSKRTRPsspYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYN 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 452 QQLTQVGVMNINGAIFL-FLTNMtFQNvFATINVFTSELPVFMREARSRLYRCDTYFLGKTIAELPLFLTVPLVFTAIAY 530
Cdd:TIGR00956 443 LPKNTSDFYSRGGALFFaILFNA-FSS-LLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILY 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 531 PMIGLRAGVLHFFNCLALVTLVANVSTSFGYLISCASSSTSMALSVGPPVIIPFLLFGGFFLNSGSVPVYLKWLSYLSWF 610
Cdd:TIGR00956 521 FMVNFRRTAGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPL 600
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 17136592 611 RYANEGLLINQWADVE----------PGEISCTSSNTTCPSSGKVI 646
Cdd:TIGR00956 601 AYAFESLMVNEFHGRRfecsqyvpsgGGYDNLGVTNKVCTVVGAEP 646
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
105-317 |
8.08e-52 |
|
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: 177.82 E-value: 8.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 105 IPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGIQvspSGMRLLNGQPVDaKEMQARCAYVQQDDLF 184
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVI---TGEILINGRPLD-KNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSLTAREHLIFQAMVRmprhltyrqrvarvdqviqelslskcqhtiigvpgrvkGLSGGERKRLAFASEALTDPPLLIC 264
Cdd:cd03232 91 SPNLTVREALRFSALLR--------------------------------------GLSVEQRKRLTIGVELAAKPSILFL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEG 317
Cdd:cd03232 133 DEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRG 185
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
416-620 |
2.11e-49 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 171.69 E-value: 2.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 416 VLWRSWLSVLKEPLLVKVRLIQTTMVAILIGLIFlGQQLTQVGVMNINGAIFLFLTNMTFQNVFATINVFTSELPVFMRE 495
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLF-GNLGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 496 ARSRLYRCDTYFLGKTIAELPLFLTVPLVFTAIAYPMIGLRAGVLHFFNCLALVTLVANVSTSFGYLISCASSSTSMALS 575
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17136592 576 VGPPVIIPFLLFGGFFLNSGSVPVYLKWLSYLSWFRYANEGLLIN 620
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
122-338 |
6.72e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.01 E-value: 6.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV--DAKEMQARCAYVQQDDLFIGSLTAREHLIFQAM 199
Cdd:COG1131 25 PGEIFGLLGPNGAGKTTTIRMLL-----GLLRPTSGEVRVLGEDVarDPAEVRRRIGYVPQEPALYPDLTVRENLRFFAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 200 VRmprHLTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSV 279
Cdd:COG1131 100 LY---GLPRKEARERIDELLELFGLTDAADR------KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARREL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 280 VQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSEAVD------FFSYVGAQ 338
Cdd:COG1131 171 WELLRELAAEGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADGTPDELKArlledvFLELTGEE 234
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
112-679 |
1.24e-43 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 169.64 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGIQVSpsGMRLLNGQPVDAKEMQARCAYVQQDDLFIGSLTAR 191
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVS--GEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 192 EHLIFQAMVR-------MPRHLTYRQRVARV------------------------DQVIQELSLSKCQHTIIGvPGRVKG 240
Cdd:PLN03140 258 ETLDFSARCQgvgtrydLLSELARREKDAGIfpeaevdlfmkatamegvksslitDYTLKILGLDICKDTIVG-DEMIRG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAfASEALTDP-PLLICDEPTSGLDSFTAHSVVQVLKKLSQKGK-TVILTIHQPSSELFELFDKILLMAEGR 318
Cdd:PLN03140 337 ISGGQKKRVT-TGEMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILLSEGQ 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 319 VAFLGTPSEAVDFFSYVGAQCPTNYNPADFYVQVLAvVPGREIESRDRiAKICDNFAISKVARDMEQLLATKNLEKPLEQ 398
Cdd:PLN03140 416 IVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTS-KKDQEQYWADR-NKPYRYISVSEFAERFKSFHVGMQLENELSV 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 399 P-ENGYTYKATWF--------MQFRAVLW-RSWLSVLKEPLLVKVRLIQTTMVAILIGLIFLGQQL----TQVGVMNING 464
Cdd:PLN03140 494 PfDKSQSHKAALVfskysvpkMELLKACWdKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMhtrnEEDGALYIGA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 465 AIFLFLTNMTfqNVFATINVFTSELPVFMREARSRLYRCDTYFLGKTIAELPLFLTVPLVFTAIAYPMIGLRAGVLHFFN 544
Cdd:PLN03140 574 LLFSMIINMF--NGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFFK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 545 CLALVTLVANVSTSFGYLISCASSSTSMALSVGPPVIIPFLLFGGFFLNSGSVPVYLKWLSYLSWFRYANEGLLINQ--- 621
Cdd:PLN03140 652 QLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVNEmfa 731
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 622 --WADvepgeiSCTSSNTTcpSSGKVILETLnfsaaDLPLD----YVGLAILI---VSFRVLAYLAL 679
Cdd:PLN03140 732 prWMN------KMASDNST--RLGTAVLNIF-----DVFTDknwyWIGVGALLgftILFNVLFTLAL 785
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
110-327 |
5.38e-40 |
|
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: 146.93 E-value: 5.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVDAKEMQAR--CAYVQQDDLFIG 186
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAgLLKPD------SGSILIDGEDVRKEPREARrqIGVLPDERGLYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 SLTAREHLIFQAMVRmprHLTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:COG4555 88 RLTVRENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDR------RVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
87-323 |
2.03e-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: 143.94 E-value: 2.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 87 GWRQlVNRTRGLFCNERHIpaprkhlLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQgiQVSPSGMRLLNGqpV 166
Cdd:cd03233 5 SWRN-ISFTTGKGRSKIPI-------LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEG--NVSVEGDIHYNG--I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 167 DAKEMQARC----AYVQQDDLFIGSLTAREHLIFQAmvrmprhltyrqrvarvdqviqelslsKCQHTIIgvpgrVKGLS 242
Cdd:cd03233 73 PYKEFAEKYpgeiIYVSEEDVHFPTLTVRETLDFAL---------------------------RCKGNEF-----VRGIS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 243 GGERKRLAFAsEALTDPPLLIC-DEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQPSSELFELFDKILLMAEGRVA 320
Cdd:cd03233 121 GGERKRVSIA-EALVSRASVLCwDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
...
gi 17136592 321 FLG 323
Cdd:cd03233 200 YYG 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
108-327 |
6.40e-37 |
|
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: 137.64 E-value: 6.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV--DAKEMQARCAYVQQDDLFI 185
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLT-----GELRPTSGTAYINGYSIrtDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 GSLTAREHLIFQAMVrmpRHLTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICD 265
Cdd:cd03263 88 DELTVREHLRFYARL---KGLPKSEIKEEVELLLRVLGLTDKANK------RARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 266 EPTSGLDSFTAHSVVQVLKKLsQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSM-DEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
112-318 |
8.28e-37 |
|
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: 136.83 E-value: 8.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDA---KEMQARCAYVQQ--DDLFIG 186
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLN-----GLLGPTSGEVLVDGKDLTKlslKELRRKVGLVFQnpDDQFFG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 SlTAREHLIFqAMVRMprHLTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:cd03225 91 P-TVEEEVAF-GLENL--GLPEEEIEERVEEALELVGLEGLRDR------SPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGR 318
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
110-328 |
7.80e-35 |
|
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: 132.07 E-value: 7.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQA---RCAYVQQ--DDLF 184
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN-----GLLKPTSGEVLVDGKDITKKNLRElrrKVGLVFQnpDDQL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSlTAREHLIFqamvrMPRHL--TYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASeAL-TDPPL 261
Cdd:COG1122 89 FAP-TVEEDVAF-----GPENLglPREEIRERVEEALELVGLEHLADR------PPHELSGGQKQRVAIAG-VLaMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 262 LICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSEA 328
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDL-DLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
109-319 |
5.58e-33 |
|
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: 126.45 E-value: 5.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCA-------YVQQD 181
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG-----GLDRPTSGEVRVDGTDISKLSEKELAAfrrrhigFVFQS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 182 DLFIGSLTAREHlifqamVRMPRHLT---YRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFAsEAL-T 257
Cdd:cd03255 91 FNLLPDLTALEN------VELPLLLAgvpKKERRERAEELLERVGLGDRLNH------YPSELSGGQQQRVAIA-RALaN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 258 DPPLLICDEPTSGLDSFTAHSVVQVLKKLS-QKGKTVILTIHQPssELFELFDKILLMAEGRV 319
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
109-319 |
1.66e-32 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 123.66 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV--DAKEMQARCAYVQQDDLFIG 186
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIL-----GLLKPDSGEIKVLGKDIkkEPEEVKRRIGYLPEEPSLYE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 SLTAREHLIfqamvrmprhltyrqrvarvdqviqelslskcqhtiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:cd03230 87 NLTVRENLK---------------------------------------------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRV 319
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKEGKTILLSSHIL-EEAERLCDRVAILNNGRI 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
110-327 |
2.43e-32 |
|
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: 125.31 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGiQVSP-SGMRLLNGQPVDA---KEMQA---RCAYV-QQD 181
Cdd:cd03261 13 RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV-----G-LLRPdSGEVLIDGEDISGlseAELYRlrrRMGMLfQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 182 DLFiGSLTAREHLIFqamvrmPrhltYRQRVARVDQVIQELSLSKCQhtIIGVPGRVK----GLSGGERKRLAFASEALT 257
Cdd:cd03261 87 ALF-DSLTVFENVAF------P----LREHTRLSEEEIREIVLEKLE--AVGLRGAEDlypaELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136592 258 DPPLLICDEPTSGLDSFTAHSVVQVLKKLSQ-KGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHD-LDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
107-327 |
5.75e-32 |
|
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: 131.03 E-value: 5.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 107 APRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPV---DAKEMQARCAYV-QQD 181
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLgFLPPY------SGSILINGVDLsdlDPASWRRQIAWVpQNP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 182 DLFIGSL---------TAREHLIFQAMvrmprhltyrqRVARVDQVIQELS--LskcqHTIIGVPGRvkGLSGGERKRLA 250
Cdd:COG4988 421 YLFAGTIrenlrlgrpDASDEELEAAL-----------EAAGLDEFVAALPdgL----DTPLGEGGR--GLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 251 FASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSqKGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLA--LLAQADRILVLDDGRIVEQGTHEE 557
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
109-330 |
1.05e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.66 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKemQARCAYVQQDDLFIGS- 187
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIL-----GLLPPTSGTVRLFGKPPRRA--RRRIGYVPQRAEVDWDf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 -LTAREhlifqaMVRMPR--HLTYRQRV-----ARVDQVIQELSLSKCQHTIIGvpgrvkGLSGGERKRLAFAsEAL-TD 258
Cdd:COG1121 91 pITVRD------VVLMGRygRRGLFRRPsradrEAVDEALERVGLEDLADRPIG------ELSGGQQQRVLLA-RALaQD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFlGTPSEAVD 330
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDL-GAVREYFDRVLLLNRGLVAH-GPPEEVLT 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
108-330 |
1.32e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 123.62 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKEMQARCAYVQQDDLF 184
Cdd:COG1120 12 GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-----GLLKPSSGEVLLDGRDLaslSRRELARRIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSLTAREhlifqaMVRMPR--HLTYRQRV-----ARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASeALT 257
Cdd:COG1120 87 PFGLTVRE------LVALGRypHLGLFGRPsaedrEAVEEALERTGLEHLADR------PVDELSGGERQRVLIAR-ALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 258 -DPPLLICDEPTSGLDSFTAHSVVQVLKKLSQ-KGKTVILTIHQPssEL-FELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:COG1120 154 qEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDL--NLaARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
108-318 |
1.78e-31 |
|
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: 120.04 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQArcayvqqddlfigs 187
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA-----GLLKPTSGEILIDGKDIAKLPLEE-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 ltarehlifqamvrmprhltYRQRVARVDQviqelslskcqhtiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEP 267
Cdd:cd00267 71 --------------------LRRRIGYVPQ-----------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17136592 268 TSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGR 318
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
111-319 |
6.07e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 120.92 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 111 HLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKEMQA-RCAYV----QQDD 182
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG-----GLDRPTSGEVLIDGQDIsslSERELARlRRRHIgfvfQFFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 LfIGSLTAREHLifqAMVRMPRHLTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFAsEAL-TDPPL 261
Cdd:COG1136 97 L-LPELTALENV---ALPLLLAGVSRKERRERARELLERVGLGDRLDH------RPSQLSGGQQQRVAIA-RALvNRPKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 262 LICDEPTSGLDSFTAHSVVQVLKKLS-QKGKTVILTIHQPssELFELFDKILLMAEGRV 319
Cdd:COG1136 166 ILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDGRI 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
112-318 |
1.63e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 119.12 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAK--EMQARCAYVQQDDLFIGSLT 189
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILA-----GLLPPSAGEVLWNGEPIRDAreDYRRRLAYLGHADGLKPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 190 AREHLIFQAMVRmprhlTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTS 269
Cdd:COG4133 92 VRENLRFWAALY-----GLRADREAIDEALEAVGLAGLADL------PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17136592 270 GLDSFTAHSVVQVLKKLSQKGKTVILTIHQPsseLFELFDKILLMAEGR 318
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGAVLLTTHQP---LELAAARVLDLGDFK 206
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
106-327 |
2.27e-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: 126.42 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 106 PAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPV---DAKEMQARCAYVQQD 181
Cdd:COG4987 344 PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrFLDPQ------SGSITLGGVDLrdlDEDDLRRRIAVVPQR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 182 -DLFIGSLtaREHLifqamvrmprhltyrqRVARVD-------QVIQELSLSK--CQ-----HTIIGVPGRvkGLSGGER 246
Cdd:COG4987 418 pHLFDTTL--RENL----------------RLARPDatdeelwAALERVGLGDwlAAlpdglDTWLGEGGR--RLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 247 KRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQkGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPS 326
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA--GLERMDRILVLEDGRIVEQGTHE 554
|
.
gi 17136592 327 E 327
Cdd:COG4987 555 E 555
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
113-269 |
4.24e-30 |
|
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: 115.82 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVDAKEMQA---RCAYVQQDDLFIGSL 188
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAgLLSPT------EGTILLDGQDLTDDERKSlrkEIGYVFQDPQLFPRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHLIFqamVRMPRHLTYRQRVARVDQVIQELSLSKCQHTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPT 268
Cdd:pfam00005 75 TVRENLRL---GLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERP--GTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 17136592 269 S 269
Cdd:pfam00005 150 A 150
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
108-323 |
6.33e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 117.29 E-value: 6.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGeLLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV--DAKEMQARCAYVQQDDLFI 185
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILA-----TLTPPSSGTIRIDGQDVlkQPQKLRRRIGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 GSLTAREHLIFQA-MVRMPRhltyRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLIC 264
Cdd:cd03264 85 PNFTVREFLDYIAwLKGIPS----KEVKARVDEVLELVNLGDRAKK------KIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLSqKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 323
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHI-VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
110-327 |
9.77e-30 |
|
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: 117.77 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDA------KEMQARCAYV-QQDD 182
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII-----GLLRPDSGEILVDGQDITGlsekelYELRRRIGMLfQGGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 LFiGSLTAREHLIFQamVRMPRHLTYRQRVARVDQVIQELSLSKCQHTiigVPGRvkgLSGGERKRLAFAsEAL-TDPPL 261
Cdd:COG1127 93 LF-DSLTVFENVAFP--LREHTDLSEAEIRELVLEKLELVGLPGAADK---MPSE---LSGGMRKRVALA-RALaLDPEI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 262 LICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEGTPEE 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
122-327 |
2.61e-29 |
|
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: 124.18 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQP---VDAKEMQARCAYVQQDD-LFIGSLtaREHLIF 196
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLgLYEPT------SGRILIDGIDlrqIDPASLRRQIGVVLQDVfLFSGTI--RENITL 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 197 QAmvrmpRHLTYRQ-----RVARVDQVIQELSLSKcqHTIIGVPGRvkGLSGGERKRLAFASEALTDPPLLICDEPTSGL 271
Cdd:COG2274 572 GD-----PDATDEEiieaaRLAGLHDFIEALPMGY--DTVVGEGGS--NLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 272 DSFTAHSVVQVLKKLSQkGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG2274 643 DAETEAIILENLRRLLK-GRTVIIIAHRLS--TIRLADRIIVLDKGRIVEDGTHEE 695
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
122-318 |
7.44e-29 |
|
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: 112.86 E-value: 7.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPV---DAKEMQARCAYVQQDD-LFIGSLtaREHLif 196
Cdd:cd03228 27 PGEKVAIVGPSGSGKSTLLKLLLrLYDPT------SGEILIDGVDLrdlDLESLRKNIAYVPQDPfLFSGTI--RENI-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 197 qamvrmprhltyrqrvarvdqviqelslskcqhtiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTA 276
Cdd:cd03228 97 --------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17136592 277 HSVVQVLKKLSqKGKTVILTIHQPSSelFELFDKILLMAEGR 318
Cdd:cd03228 133 ALILEALRALA-KGKTVIVIAHRLST--IRDADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
109-323 |
1.21e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 113.78 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGiQVSP-SGMRLLNGQPVdaKEMQARCAYVQQ----DDL 183
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL-----G-LLKPtSGSIRVFGKPL--EKERKRIGYVPQrrsiDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 FigSLTAREhliFQAMVRMP-----RHLTYRQRvARVDQVIQELSLSKCQHTIIGvpgrvkGLSGGERKRLAFASEALTD 258
Cdd:cd03235 83 F--PISVRD---VVLMGLYGhkglfRRLSKADK-AKVDEALERVGLSELADRQIG------ELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSeLFELFDKILLMAeGRVAFLG 323
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLN-RTVVASG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
104-319 |
1.78e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.37 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 104 HIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVDAKEMQA---RCAYVQ 179
Cdd:COG4619 7 SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALAdLDPPT------SGEIYLDGKPLSAMPPPEwrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 180 QD-DLFIGslTAREHLIFqamVRMPRHLTYRQrvARVDQVIQELSLSkcqHTIIGVPgrVKGLSGGERKRLAFASEALTD 258
Cdd:COG4619 81 QEpALWGG--TVRDNLPF---PFQLRERKFDR--ERALELLERLGLP---PDILDKP--VERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKLS-QKGKTVILTIHQPsSELFELFDKILLMAEGRV 319
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLaEEGRAVLWVSHDP-EQIERVADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
112-319 |
7.27e-28 |
|
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: 111.19 E-value: 7.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCAYVQQD-DLFIGSLTA 190
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILA-----GLIKESSGSILLNGKPIKAKERRKSIGYVMQDvDYQLFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 191 REHLIFQAMvrmprhLTYRqRVARVDQVIQELSLS--KCQHTIIgvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPT 268
Cdd:cd03226 90 REELLLGLK------ELDA-GNEQAETVLKDLDLYalKERHPLS--------LSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17136592 269 SGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPssE-LFELFDKILLMAEGRV 319
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDY--EfLAKVCDRVLLLANGAI 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
123-318 |
7.39e-27 |
|
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: 107.66 E-value: 7.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARcayvqqddlfigslTAREH--LIFQAMV 200
Cdd:cd03229 26 GEIVALLGPSGSGKSTLLRCIA-----GLEEPDSGSILIDGEDLTDLEDELP--------------PLRRRigMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 201 RMPrHLTYRQRVARvdqviqelslskcqhtiigvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVV 280
Cdd:cd03229 87 LFP-HLTVLENIAL-------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVR 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 17136592 281 QVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGR 318
Cdd:cd03229 141 ALLKSLQAQlGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
108-327 |
7.71e-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: 109.24 E-value: 7.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNaLAFR--SPQgiqvspSGMRLLNGQP---VDAKEMQARCAYVQQDD 182
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILR-LLFRfyDVS------SGSILIDGQDireVTLDSLRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 -LF---------IGSLTAREHLIFQAMvrmprhltyrqRVARVDQVIqeLSLSKCQHTIIGVPGrVKgLSGGERKRLAFA 252
Cdd:cd03253 85 vLFndtigynirYGRPDATDEEVIEAA-----------KAAQIHDKI--MRFPDGYDTIVGERG-LK-LSGGEKQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 253 SEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSqKGKTVILTIHQPSSELFElfDKILLMAEGRVAFLGTPSE 327
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNA--DKIIVLKDGRIVERGTHEE 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
108-327 |
1.84e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.49 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVspsgmrLLNGQPV---DAKEMQARCAYVQQDD- 182
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrFYDPTSGRI------LIDGVDIrdlTLESLRRQIGVVPQDTf 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 LF---------IGSLTAREHLIFQAMvrmprhltyrqRVARVDQVIQELS--LskcqHTIIGVPGRvkGLSGGERKRLAF 251
Cdd:COG1132 425 LFsgtirenirYGRPDATDEEVEEAA-----------KAAQAHEFIEALPdgY----DTVVGERGV--NLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 252 ASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSqKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLST--IRNADRILVLDDGRIVEQGTHEE 560
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
110-327 |
2.01e-26 |
|
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: 108.42 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVSPSGMRLLNGQPVDAKEMQARCAYVQQDDLFIGSL 188
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNgLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMIFQQFNLIERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TARE---------HLIFQAMVRMPRHLTYRQRVARVDQV-IQELSLSkcqhtiigvpgRVKGLSGGERKRLAFASEALTD 258
Cdd:cd03256 94 SVLEnvlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVgLLDKAYQ-----------RADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKL-SQKGKTVILTIHQPssELF-ELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQV--DLArEYADRIVGLKDGRIVFDGPPAE 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
108-327 |
2.39e-26 |
|
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: 107.70 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVspsgmrLLNGQP---VDAKEMQARCAYVQQDD- 182
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMrFYDPQKGQI------LIDGIDirdISRKSLRSMIGVVLQDTf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 LFIGSLtaREHLifqamvRMPRHLTYRQRVARVDQVIQEL----SLSKCQHTIIGVPGrvKGLSGGERKRLAFASEALTD 258
Cdd:cd03254 88 LFSGTI--MENI------RLGRPNATDEEVIEAAKEAGAHdfimKLPNGYDTVLGENG--GNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKLsQKGKTVILTIHQPSSELFElfDKILLMAEGRVAFLGTPSE 327
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEGTHDE 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
106-327 |
1.17e-25 |
|
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: 111.53 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 106 PAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGIQVSpsGMRLLNGQPV---DAKEMQARCAYVQQD- 181
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS--GEVLLDGRDLlelSEALRGRRIGMVFQDp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 182 DLFIGSLTAREHLIFQAMVRMPRHLTYRQRVARV-DQVIQELSLSKCQHTiigvpgrvkgLSGGERKRLAFASEALTDPP 260
Cdd:COG1123 93 MTQLNPVTVGDQIAEALENLGLSRAEARARVLELlEAVGLERRLDRYPHQ----------LSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 261 LLICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
122-327 |
3.39e-25 |
|
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: 104.37 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV--DAKEMQARCAYVQQDDLFIGSLTAREHLIFQAM 199
Cdd:cd03265 25 RGEIFGLLGPNGAGKTTTIKMLT-----TLLKPTSGRATVAGHDVvrEPREVRRRIGIVFQDLSVDDELTGWENLYIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 200 VR-MPRhltyRQRVARVDQVIQELSLSKCQHTIigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHS 278
Cdd:cd03265 100 LYgVPG----AERRERIDELLDFVGLLEAADRL------VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17136592 279 VVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03265 170 VWEYIEKLKEEfGMTILLTTHY-MEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
122-323 |
4.36e-25 |
|
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: 103.53 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEM-------QARCAYV-QQDDLFiGSLTAREH 193
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIA-----GLEKPDGGTIVLNGTVLFDSRKkinlppqQRKIGLVfQQYALF-PHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 194 LIFQamvrMPRHLTYRQRVaRVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 273
Cdd:cd03297 96 LAFG----LKRKRNREDRI-SVDELLDLLGLDHLLNR------YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17136592 274 FTAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLG 323
Cdd:cd03297 165 ALRLQLLPELKQIKKNlNIPVIFVTHDL-SEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
108-323 |
4.43e-25 |
|
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: 102.51 E-value: 4.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKEMQARCAYVQQddlf 184
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-----GLLKPSSGEILLDGKDLaslSPKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 igsltarehlifqAMvrmprhltyrqrvARVDqvIQELSLSKCQHtiigvpgrvkgLSGGERKRLAFASeALT-DPPLLI 263
Cdd:cd03214 81 -------------AL-------------ELLG--LAHLADRPFNE-----------LSGGERQRVLLAR-ALAqEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136592 264 CDEPTSGLDSFTAHSVVQVLKKLS-QKGKTVILTIHQPSSELfELFDKILLMAEGRVAFLG 323
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAA-RYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
121-362 |
5.49e-25 |
|
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: 109.22 E-value: 5.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 121 YPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDA------KEMQARCAYVQQD--DLFIGSLTARE 192
Cdd:COG1123 289 RRGETLGLVGESGSGKSTLARLLL-----GLLRPTSGSILFDGKDLTKlsrrslRELRRRVQMVFQDpySSLNPRMTVGD 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 193 HLIFQAMVRmpRHLTYRQRVARVDQVIQELSLskcqhtiigvPGRVKG-----LSGGERKRLAFASeAL-TDPPLLICDE 266
Cdd:COG1123 364 IIAEPLRLH--GLLSRAERRERVAELLERVGL----------PPDLADrypheLSGGQRQRVAIAR-ALaLEPKLLILDE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSEavdFFSyvgaqcptnyNP 345
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDLQRElGLTYLFISHD-LAVVRYIADRVAVMYDGRIVEDGPTEE---VFA----------NP 496
|
250
....*....|....*...
gi 17136592 346 ADFYVQVL-AVVPGREIE 362
Cdd:COG1123 497 QHPYTRALlAAVPSLDPA 514
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
121-320 |
6.48e-25 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 103.32 E-value: 6.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 121 YPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVdaKEMQARCAYVQQDDLFIGSLTAREHLIFQA- 198
Cdd:cd03293 28 EEGEFVALVGPSGCGKSTLLRIIAgLERPT------SGEVLVDGEPV--TGPGPDRGYVFQQDALLPWLTVLDNVALGLe 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 MVRMPRhltyRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHS 278
Cdd:cd03293 100 LQGVPK----AEARERAEELLELVGLSGFENA------YPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17136592 279 VVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAE--GRVA 320
Cdd:cd03293 170 LQEELLDIWREtGKTVLLVTHD-IDEAVFLADRVVVLSArpGRIV 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
113-314 |
8.16e-25 |
|
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: 108.91 E-value: 8.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGiqvspsGMRLLNGQPV---DAKEMQARCAYV-QQDDLFIGS 187
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLgFVDPTE------GSIAVNGVPLadaDADSWRDQIAWVpQHPFLFAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 LT---------AREHLIFQAMVRmprhltyrqrvARVDQVIQELSLSkcQHTIIGVPGRvkGLSGGERKRLAFASEALTD 258
Cdd:TIGR02857 412 IAenirlarpdASDAEIREALER-----------AGLDEFVAALPQG--LDTPIGEGGA--GLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKLSQkGKTVILTIHQPssELFELFDKILLM 314
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRL--ALAALADRIVVL 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
112-330 |
8.31e-25 |
|
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: 103.72 E-value: 8.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALafrspQGIQVSPSGMRLLNGQP---VDAKEMQARCAYVQQDD-LFIGS 187
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI-----QRFYVPENGRVLVDGHDlalADPAWLRRQVGVVLQENvLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 LtaREHlIFQAMVRMPRH-LTYRQRVARVDQVIQELSLSkcQHTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:cd03252 92 I--RDN-IALADPGMSMErVIEAAKLAGAHDFISELPEG--YDTIVGEQG--AGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSqKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLST--VKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
110-319 |
1.05e-24 |
|
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: 102.30 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQ-PVDAKEMQARCAYVQQDDLFIGSL 188
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL-----GLIKPDSGEITFDGKsYQKNIEALRRIGALIEAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHLIFQAMVRMPRHltyrqrvARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPT 268
Cdd:cd03268 88 TARENLRLLARLLGIRK-------KRIDEVLDVVGLKDSAKK------KVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17136592 269 SGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRV 319
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHL-LSEIQKVADRIGIINKGKL 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
110-320 |
2.49e-24 |
|
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: 101.44 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQAR-CAYVQQDD-LFiGS 187
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA-----GLERPDSGEILIDGRDVTGVPPERRnIGMVFQDYaLF-PH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 LTAREHLIFQ-AMVRMPRhltyRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:cd03259 87 LTVAENIAFGlKLRGVPK----AEIRARVRELLELVGLEGLLNR------YPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVA 320
Cdd:cd03259 157 PLSALDAKLREELREELKELQRElGITTIYVTHDQ-EEALALADRIAVMNEGRIV 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
122-327 |
3.14e-24 |
|
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: 101.74 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVspsgmrLLNGQPVDAKEMQARCAY-----VQQDDLFiGSLTAREHLI 195
Cdd:cd03219 25 PGEIHGLIGPNGAGKTTLFNLISgFLRPTSGSV------LFDGEDITGLPPHEIARLgigrtFQIPRLF-PELTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 196 FQAMVRMPRHL-------TYRQRVARVDQVIQELSLSKCQHTIIGvpgrvkGLSGGERKRLAFASeAL-TDPPLLICDEP 267
Cdd:cd03219 98 VAAQARTGSGLllararrEEREARERAEELLERVGLADLADRPAG------ELSYGQQRRLEIAR-ALaTDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 268 TSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03219 171 AAGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
105-323 |
6.17e-24 |
|
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: 100.52 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 105 IPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV--DAKEMQARCAYVQQDD 182
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLA-----GLLEPDAGFATVDGFDVvkEPAEARRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 LFIGSLTAREHLIFQAMVrmprH-LTYRQRVARVDQVIQELSLskcQHTIigvPGRVKGLSGGERKRLAFASEALTDPPL 261
Cdd:cd03266 88 GLYDRLTARENLEYFAGL----YgLKGDELTARLEELADRLGM---EELL---DRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 262 LICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 323
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
110-327 |
1.36e-23 |
|
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: 100.54 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQ--GIQVSPSGMRLlnGQpVDAKEMQARCAYVQQD--DLFI 185
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtyGNDVRLFGERR--GG-EDVWELRKRIGLVSPAlqLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 GSLTAREHLI--FQAMVRMPRHLTYRQRvARVDQVIQELSLSKCQHTIIGvpgrvkGLSGGERKRLAFAsEAL-TDPPLL 262
Cdd:COG1119 93 RDETVLDVVLsgFFDSIGLYREPTDEQR-ERARELLELLGLAHLADRPFG------TLSQGEQRRVLIA-RALvKDPELL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 263 ICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTI-HQPsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVtHHV-EEIPPGITHVLLLKDGRVVAAGPKEE 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
113-330 |
1.44e-23 |
|
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: 100.00 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPV---DAKEMQARCAYVQQDD-LFIGS 187
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPrFYDVD------SGRILIDGHDVrdyTLASLRRQIGLVSQDVfLFNDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 L----------TAREHLIFQAmvrmprhltyrqRVARVDQVIQELSLSkcQHTIIGVPGrVKgLSGGERKRLAFASEALT 257
Cdd:cd03251 92 VaeniaygrpgATREEVEEAA------------RAANAHEFIMELPEG--YDTVIGERG-VK-LSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 258 DPPLLICDEPTSGLDSFTAHSVVQVLKKLsQKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERL-MKNRTTFVIAHRLST--IENADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
122-319 |
1.81e-23 |
|
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: 97.67 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKEMQARCAYVQQDD-LFIGSLTarehlifq 197
Cdd:cd03246 27 PGESLAIIGPSGSGKSTLARLIL-----GLLRPTSGRVRLDGADIsqwDPNELGDHVGYLPQDDeLFSGSIA-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 198 amvrmprhltyrqrvarvdQVIqelslskcqhtiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAH 277
Cdd:cd03246 94 -------------------ENI---------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17136592 278 SVVQVLKKLSQKGKTVILTIHQPssELFELFDKILLMAEGRV 319
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRP--ETLASADRILVLEDGRV 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
123-323 |
3.36e-23 |
|
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: 98.33 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQAR--CAYVQQDDLFigsltarEHL-IFQ-- 197
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA-----GFETPQSGRVLINGVDVTAAPPADRpvSMLFQENNLF-------AHLtVEQnv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 198 AMVRMPR-HLTYRQRvARVDQVIQELSLSkcqhtiiGVPGRVKG-LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFT 275
Cdd:cd03298 92 GLGLSPGlKLTAEDR-QAIEVALARVGLA-------GLEKRLPGeLSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17136592 276 AHSVVQVLKKL-SQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLG 323
Cdd:cd03298 164 RAEMLDLVLDLhAETKMTVLMVTHQP-EDAKRLAQRVVFLDNGRIAAQG 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
109-320 |
3.94e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 99.11 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVC-GVAyPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKEMQARCAYVQQDDLf 184
Cdd:COG1124 17 RVPVLKDVSlEVA-PGESFGLVGESGSGKSTLLRALA-----GLERPWSGEVTFDGRPVtrrRRKAFRRRVQMVFQDPY- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 iGSLTAReHLIFQAMVRMPRHLTYRQRVARVDQVIQELslskcqhtiiGVPGRVKG-----LSGGERKRLAFASEALTDP 259
Cdd:COG1124 90 -ASLHPR-HTVDRILAEPLRIHGLPDREERIAELLEQV----------GLPPSFLDryphqLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 260 PLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTI-HQPSSELFeLFDKILLMAEGRVA 320
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVsHDLAVVAH-LCDRVAVMQNGRIV 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
109-327 |
6.58e-23 |
|
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: 98.00 E-value: 6.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLlnalaFRSPQGIQVSPSGMRLLNGQPVDAKEMQARC----AYVQQDDLF 184
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTT-----FYMIVGLVKPDSGKILLDGQDITKLPMHKRArlgiGYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSLTAREHLIfqAMVRMpRHLTYRQRVARVDQVIQELSLSKCQHTiigvPGRvkGLSGGERKRLAFASEALTDPPLLIC 264
Cdd:cd03218 87 FRKLTVEENIL--AVLEI-RGLSKKEREEKLEELLEEFHITHLRKS----KAS--SLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN-VRETLSITDRAYIIYEGKVLAEGTPEE 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
104-319 |
1.66e-22 |
|
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: 96.50 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 104 HIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVspsgmrLLNG---QPVDAKEMQARCAYVQ 179
Cdd:cd03245 11 SYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAgLYKPTSGSV------LLDGtdiRQLDPADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 180 QD-DLFIGSLtaREHLifqaMVRMPRHLTYR----QRVARVDQVIQelslskcQH-----TIIGVPGRvkGLSGGERKRL 249
Cdd:cd03245 85 QDvTLFYGTL--RDNI----TLGAPLADDERilraAELAGVTDFVN-------KHpngldLQIGERGR--GLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 250 AFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSqKGKTVILTIHQPSseLFELFDKILLMAEGRV 319
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRI 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
122-327 |
2.71e-22 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 95.96 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARC----AYVQQDDLFIGSLTAREHLIFQ 197
Cdd:cd03224 25 EGEIVALLGRNGAGKTTLLKTIM-----GLLPPRSGSIRFDGRDITGLPPHERAragiGYVPEGRRIFPELTVEENLLLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 198 AMVRMPRHLtyRQRVARVDQ---VIQELSLSKCQHtiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 274
Cdd:cd03224 100 AYARRRAKR--KARLERVYElfpRLKERRKQLAGT-----------LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17136592 275 TAHSVVQVLKKLSQKGKTVILtIHQPSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTILL-VEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
109-328 |
2.84e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.76 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVD---AKEMQARCAyV--QQDDL 183
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS-----GELSPDSGEVRLNGRPLAdwsPAELARRRA-VlpQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 -FigSLTAREhlifqaMVRMPRhLTYRQRVARVDQVIQE-LSLSKCQHtiigVPGR-VKGLSGGERKRLAFA------SE 254
Cdd:PRK13548 88 sF--PFTVEE------VVAMGR-APHGLSRAEDDALVAAaLAQVDLAH----LAGRdYPQLSGGEQQRVQLArvlaqlWE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 255 ALTDPPLLICDEPTSGLDSFTAHSVVQVLKKL-SQKGKTVILTIHQPSseLFELF-DKILLMAEGRVAFLGTPSEA 328
Cdd:PRK13548 155 PDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLN--LAARYaDRIVLLHQGRLVADGTPAEV 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
122-327 |
3.72e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 96.26 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVDAKEMQARCAY-----VQQDDLFiGSLTAREHL- 194
Cdd:COG0411 29 RGEIVGLIGPNGAGKTTLFNLITgFYRPT------SGRILFDGRDITGLPPHRIARLgiartFQNPRLF-PELTVLENVl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 195 ----------IFQAMVRMPRHLTYRQRV-ARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASeAL-TDPPLL 262
Cdd:COG0411 102 vaaharlgrgLLAALLRLPRARREEREArERAEELLERVGLADRADE------PAGNLSYGQQRRLEIAR-ALaTEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 263 ICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDM-DLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
123-306 |
4.05e-22 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 95.17 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVdAKEMQARCAY-------VQQDDLFIGSLTAREHLI 195
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLIY-----KEELPTSGTIRVNGQDV-SDLRGRAIPYlrrkigvVFQDFRLLPDRNVYENVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 196 FQAMVRMPRHLTYRQRVArvdQVIQELSLSKCQHTIigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFT 275
Cdd:cd03292 101 FALEVTGVPPREIRKRVP---AALELVGLSHKHRAL------PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180 190
....*....|....*....|....*....|.
gi 17136592 276 AHSVVQVLKKLSQKGKTVILTIHqpSSELFE 306
Cdd:cd03292 172 TWEIMNLLKKINKAGTTVVVATH--AKELVD 200
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
109-323 |
7.65e-22 |
|
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: 94.27 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAkEMQARCAYVQQDDLFIGSL 188
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIL-----GIILPDSGEVLFDGKPLDI-AARNRIGYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHLIFQAMVR-MPRhltyRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEP 267
Cdd:cd03269 86 KVIDQLVYLAQLKgLKK----EEARRRIDEWLERLELSEYANK------RVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 268 TSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 323
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
106-327 |
2.36e-21 |
|
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: 98.28 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 106 PAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDA--KEMQARC-AYVQQD- 181
Cdd:COG4618 341 PGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV-----GVWPPTAGSVRLDGADLSQwdREELGRHiGYLPQDv 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 182 DLFIGSLT---AR-----EHLIFQAMvrmprhltyrqRVARVDQVIqeLSLSKCQHTIIGVPGRvkGLSGGERKRLAFAs 253
Cdd:COG4618 416 ELFDGTIAeniARfgdadPEKVVAAA-----------KLAGVHEMI--LRLPDGYDTRIGEGGA--RLSGGQRQRIGLA- 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 254 EAL-TDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG4618 480 RALyGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
122-272 |
2.92e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.54 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAFRSPQGIQVspSGMRLLNGQPVDAKEMQAR-CAYVQQDDLFIGSLTAREHLIFQamv 200
Cdd:COG4136 26 PGEILTLMGPSGSGKSTLLAAIAGTLSPAFSA--SGEVLLNGRRLTALPAEQRrIGILFQDDLLFPHLSVGENLAFA--- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 201 rMPRHLTYRQRVARVDQVIQELSLSkcqhtiiGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 272
Cdd:COG4136 101 -LPPTIGRAQRRARVEQALEEAGLA-------GFADRdPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
121-319 |
2.99e-21 |
|
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: 92.95 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 121 YPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVSPSGMRLLNGQPVDAKEMQARCAYVQQDDlfIGSLTAR---EHLIF 196
Cdd:cd03257 29 KKGETLGLVGESGSGKSTLARAILgLLKPTSGSIIFDGKDLLKLSRRLRKIRRKEIQMVFQDP--MSSLNPRmtiGEQIA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 197 QAMVRmprHLTYRQRVARVDQVIQELSLskcqhtiIGVPGRVKG-----LSGGERKRLAFASEALTDPPLLICDEPTSGL 271
Cdd:cd03257 107 EPLRI---HGKLSKKEARKEAVLLLLVG-------VGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLIADEPTSAL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17136592 272 DSFTAHSVVQVLKKL-SQKGKTVILTIHQPSSeLFELFDKILLMAEGRV 319
Cdd:cd03257 177 DVSVQAQILDLLKKLqEELGLTLLFITHDLGV-VAKIADRVAVMYAGKI 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
123-327 |
3.09e-21 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 93.52 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLL---NALafrspqgiqVSP-SGMRLLNGQPV---DAKEMQARCAYV-QQDDLFigsltarEHL 194
Cdd:cd03295 27 GEFLVLIGPSGSGKTTTMkmiNRL---------IEPtSGEIFIDGEDIreqDPVELRRKIGYViQQIGLF-------PHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 195 -IFQAMVRMPRHLTY--RQRVARVDQVIQELSLSKCQHTiigvpGRVKG-LSGGERKRLAFASEALTDPPLLICDEPTSG 270
Cdd:cd03295 91 tVEENIALVPKLLKWpkEKIRERADELLALVGLDPAEFA-----DRYPHeLSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 271 LDSFTAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQElGKTIVFVTHD-IDEAFRLADRIAIMKNGEIVQVGTPDE 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
122-327 |
4.28e-21 |
|
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: 95.56 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PG-ELLAVMGSSGAGKTTLLNALA-FRSPQGIQVSPSGmRLLN--GQPVDAKEMQARCAYVQQDDLFIGSLTAREHLIFQ 197
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAgLTRPDEGEIVLNG-RTLFdsRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 198 AMVRMPRhltyrQRVARVDQVIQELSLSkcqHTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAH 277
Cdd:TIGR02142 100 MKRARPS-----ERRISFERVIELLGIG---HLLGRLPGR---LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17136592 278 SVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
111-327 |
5.94e-21 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 92.26 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 111 HLLKNVCGVAYPGELLAVMGSSGAGKTTLLnalafRSPQGIQVSPSGMRLLNGQPVDA------KEMQARCAYV-QQDDL 183
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLI-----RCINGLERPTSGSVLVDGTDLTLlsgkelRKARRRIGMIfQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 FiGSLTAREHLIFQAMV-RMPRhltyRQRVARVDQVIQELSLSkcqHTIIGVPGRvkgLSGGERKRLAFASEALTDPPLL 262
Cdd:cd03258 94 L-SSRTVFENVALPLEIaGVPK----AEIEERVLELLELVGLE---DKADAYPAQ---LSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 263 ICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
113-320 |
8.31e-21 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 91.64 E-value: 8.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVdAKEMQARCAYVQQDDL-FIGSLtar 191
Cdd:TIGR02211 21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLG-----GLDNPTSGEVLFNGQSL-SKLSSNERAKLRNKKLgFIYQF--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 192 EHLI--FQAM--VRMPRhLTYRQRVARVDQVIQELsLSKC--QHTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICD 265
Cdd:TIGR02211 92 HHLLpdFTALenVAMPL-LIGKKSVKEAKERAYEM-LEKVglEHRINHRPSE---LSGGERQRVAIARALVNQPSLVLAD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 266 EPTSGLDSFTAHSVVQVLKKL-SQKGKTVILTIHQPssELFELFDKILLMAEGRVA 320
Cdd:TIGR02211 167 EPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDL--ELAKKLDRVLEMKDGQLF 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
123-327 |
1.40e-20 |
|
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: 92.84 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV--DAKEMQARCAYVQQDDLFIGSLTAREHL-IFQAM 199
Cdd:TIGR01188 19 GEVFGFLGPNGAGKTTTIRMLT-----TLLRPTSGTARVAGYDVvrEPRKVRRSIGIVPQYASVDEDLTGRENLeMMGRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 200 VRMPRhltyRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSV 279
Cdd:TIGR01188 94 YGLPK----DEAEERAEELLELFELGEAADR------PVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17136592 280 VQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:TIGR01188 164 WDYIRALKEEGVTILLTTHY-MEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
122-320 |
1.83e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 91.69 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKemQARCAYVQQDDlfigSL----TAREHLIF- 196
Cdd:COG1116 36 AGEFVALVGPSGCGKSTLLRLIA-----GLEKPTSGEVLVDGKPVTGP--GPDRGVVFQEP----ALlpwlTVLDNVALg 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 197 QAMVRMPRhltyRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDSFT 275
Cdd:COG1116 105 LELRGVPK----AERRERARELLELVGLAGFEDA------YPHQLSGGMRQRVAIA-RALaNDPEVLLMDEPFGALDALT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17136592 276 AHSVVQVLKKL-SQKGKTVILTIHQPSSELFeLFDKILLMAE--GRVA 320
Cdd:COG1116 174 RERLQDELLRLwQETGKTVLFVTHDVDEAVF-LADRVVVLSArpGRIV 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
106-323 |
2.23e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.91 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 106 PAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCAyvqqddlfI 185
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT-----GDLKPQQGEITLDGVPVSDLEKALSSL--------I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 GSLTAREHLiFQAmvrmprhlTYRQRVARvdqviqelslskcqhtiigvpgrvkGLSGGERKRLAFASEALTDPPLLICD 265
Cdd:cd03247 78 SVLNQRPYL-FDT--------TLRNNLGR-------------------------RFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 266 EPTSGLDSFTAHSVVQVLKKLSqKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLG 323
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVL-KDKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
122-319 |
4.21e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 89.34 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKEMQA---RCAYVQQDDLFIGSLTAREHLI 195
Cdd:COG2884 27 KGEFVFLTGPSGAGKSTLLKLLY-----GEERPTSGQVLVNGQDLsrlKRREIPYlrrRIGVVFQDFRLLPDRTVYENVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 196 FqAM--VRMPRhltyRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 273
Cdd:COG2884 102 L-PLrvTGKSR----KEIRRRVREVLDLVGLSDKAKA------LPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17136592 274 FTAHSVVQVLKKLSQKGKTVILTIHQPssELFELFDK-ILLMAEGRV 319
Cdd:COG2884 171 ETSWEIMELLEEINRRGTTVLIATHDL--ELVDRMPKrVLELEDGRL 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
122-330 |
4.46e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 4.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVD--AKEMQARCAYVQQDDLFIGSLTAREHL-IFQA 198
Cdd:PRK13537 32 RGECFGLLGPNGAGKTTTLRMLL-----GLTHPDAGSISLCGEPVPsrARHARQRVGVVPQFDNLDPDFTVRENLlVFGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 MVRMPRHlTYRQRVARVdqviqeLSLSKCQHTiigVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHS 278
Cdd:PRK13537 107 YFGLSAA-AARALVPPL------LEFAKLENK---ADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17136592 279 VVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:PRK13537 177 MWERLRSLLARGKTILLTTHF-MEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
122-327 |
4.47e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 92.47 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVDAKEMQAR-CAYVQQDD-LFiGSLTAREHLIFQA 198
Cdd:COG3842 30 PGEFVALLGPSGCGKTTLLRMIAgFETPD------SGRILLDGRDVTGLPPEKRnVGMVFQDYaLF-PHLTVAENVAFGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 MVR-MPRhltyRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGLDSFTA 276
Cdd:COG3842 103 RMRgVPK----AEIRARVAELLELVGLEGLADR------YPHQLSGGQQQRVALA-RALaPEPRVLLLDEPLSALDAKLR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17136592 277 HSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG3842 172 EEMREELRRLQRElGITFIYVTHDQ-EEALALADRIAVMNDGRIEQVGTPEE 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
103-300 |
5.58e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 93.96 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 103 RHIPAPRkhLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVSPSGMRLlngQPVDAKEMQARCAYVQQD 181
Cdd:TIGR02868 343 GYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAgLLDPLQGEVTLDGVPV---SSLDQDEVRRRVSVCAQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 182 -DLFigSLTAREHLifqamvrmprhltyrqRVARVDQVIQEL--------------SLSKCQHTIIGVPGRVkgLSGGER 246
Cdd:TIGR02868 418 aHLF--DTTVRENL----------------RLARPDATDEELwaalervgladwlrALPDGLDTVLGEGGAR--LSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 17136592 247 KRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQkGKTVILTIHQP 300
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
123-298 |
6.72e-20 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 87.86 E-value: 6.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVD-----AKEMQARCAYVQQ---DDLFIGSltarehl 194
Cdd:TIGR01166 18 GEVLALLGANGAGKSTLLLHLN-----GLLRPQSGAVLIDGEPLDysrkgLLERRQRVGLVFQdpdDQLFAAD------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 195 IFQAMVRMPRHLTYRQ-RV-ARVDQVIQELSLSKCQHTIIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 272
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEaEVeRRVREALTAVGASGLRERPTHC------LSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*.
gi 17136592 273 SFTAHSVVQVLKKLSQKGKTVILTIH 298
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
111-319 |
7.84e-20 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 89.03 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 111 HLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCA-------YVQQDDL 183
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLA-----GLDRPTSGTVRLAGQDLFALDEDARARlrarhvgFVFQSFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 FIGSLTAREHlifqamVRMPRHLT-YRQRVARVDQVIQELSLSK-CQHTiigvPgrvKGLSGGERKRLAFASEALTDPPL 261
Cdd:COG4181 101 LLPTLTALEN------VMLPLELAgRRDARARARALLERVGLGHrLDHY----P---AQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 262 LICDEPTSGLDSFTAHSVVQVLKKL-SQKGKTVILTIHQPssELFELFDKILLMAEGRV 319
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDP--ALAARCDRVLRLRAGRL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
110-319 |
9.02e-20 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 88.36 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLL---NALafRSPQGIQVSPSGMRlLNGQPVDAKEMQARCAYV-QQDDLFi 185
Cdd:cd03262 13 FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLrciNLL--EEPDSGTIIIDGLK-LTDDKKNINELRQKVGMVfQQFNLF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 GSLTAREHLIFQAMVRmpRHLTYRQRVARVDQVIQELSLSKCQHtiiGVPGRvkgLSGGERKRLAFASEALTDPPLLICD 265
Cdd:cd03262 89 PHLTVLENITLAPIKV--KGMSKAEAEERALELLEKVGLADKAD---AYPAQ---LSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 266 EPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSselF--ELFDKILLMAEGRV 319
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMG---FarEVADRVIFMDDGRI 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
122-327 |
1.34e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.78 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLlnalaFRSPQGIQVSPSGMRLLNGQPVDAKEMQArcayvqqddlfIG----------SLTAR 191
Cdd:COG4152 26 KGEIFGLLGPNGAGKTTT-----IRIILGILAPDSGEVLWDGEPLDPEDRRR-----------IGylpeerglypKMKVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 192 EHLIFQAMVR-MPRhltyRQRVARVDQVIQELslskcqhtiiGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:COG4152 90 EQLVYLARLKgLSK----AEAKRRADEWLERL----------GLGDRankkVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQ-PSSElfELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELVE--ELCDRIVIINKGRKVLSGSVDE 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
112-318 |
2.06e-19 |
|
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: 87.14 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqgiqvspsG-MRLLNGQpvdaKEMQARCAYVQQDDlFIGSLTA 190
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALL------------GeLEKLSGS----VSVPGSIAYVSQEP-WIQNGTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 191 REHLIFqamvrmprHLTYRQRvaRVDQVIQelslsKCQ------------HTIIGvpgrVKG--LSGGERKRLAFASEAL 256
Cdd:cd03250 83 RENILF--------GKPFDEE--RYEKVIK-----ACAlepdleilpdgdLTEIG----EKGinLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 257 TDPPLLICDEPTSGLDSFTAHSVVQ-VLKKLSQKGKTVILTIHQPssELFELFDKILLMAEGR 318
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQL--QLLPHADQIVVLDNGR 204
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
113-331 |
3.57e-19 |
|
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: 87.14 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQaRCAYVQQDDLFiGSLTARE 192
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLIS-----GLAQPTSGGVILEGKQITEPGPD-RMVVFQNYSLL-PWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 193 HlIFQAMVRMPRHLTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 272
Cdd:TIGR01184 74 N-IALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADK------RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 273 SFTAHSVVQVLKKLSQK-GKTVILTIHQPSSELFeLFDKILLMAEGRVAFLGTPSEaVDF 331
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEhRVTVLMVTHDVDEALL-LSDRVVMLTNGPAANIGQILE-VPF 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
123-348 |
3.71e-19 |
|
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: 87.01 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV-DAKEMQARCAYVQQDDLFIGSLTAREHLIFQ-AMV 200
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIA-----GFIKPDSGKILLNGKDItNLPPEKRDISYVPQNYALFPHMTVYKNIAYGlKKR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 201 RMPRhltyRQRVARVDQVIQELSLSkcqHTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVV 280
Cdd:cd03299 100 KVDK----KEIERKVLEIAEMLGID---HLLNRKPET---LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 281 QVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPSEAvdFFSyvgaqcPTNYNPADF 348
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV--FKK------PKNEFVAEF 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
113-341 |
4.19e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.74 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTL---LNALafRSPQGIQVSPSGMRllNGQPVDAKEMQARCAYVQQ--DDLFIGS 187
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLalhLNGL--LRPQKGKVLVSGID--TGDFSKLQGIRKLVGIVFQnpETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 lTAREHLIFQamvrmPRHLTYR--QRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICD 265
Cdd:PRK13644 94 -TVEEDLAFG-----PENLCLPpiEIRKRVDRALAEIGLEKYRHR------SPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 266 EPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHqpSSELFELFDKILLMAEGRVAFLGTPSEAVDFFS--YVGAQCPT 341
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLSDVSlqTLGLTPPS 237
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
122-320 |
5.76e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 87.22 E-value: 5.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVDAKEmqARCAYVQQDDLFIGSLTAREHLIFQAMV 200
Cdd:COG4525 32 SGEFVVALGASGCGKTTLLNLIAgFLAPS------SGEITLDGVPVTGPG--ADRGVVFQKDALLPWLNVLDNVAFGLRL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 201 R-MPRHltyrQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFAsEALT-DPPLLICDEPTSGLDSFTAHS 278
Cdd:COG4525 104 RgVPKA----ERRARAEELLALVGLADFARR------RIWQLSGGMRQRVGIA-RALAaDPRFLLMDEPFGALDALTREQ 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17136592 279 VVQVLKKLSQK-GKTVILTIHQPSSELFeLFDKILLMA--EGRVA 320
Cdd:COG4525 173 MQELLLDVWQRtGKGVFLITHSVEEALF-LATRLVVMSpgPGRIV 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
109-329 |
7.22e-19 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 86.17 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTllnalAFRSPQGIqVSP-SGMRLLNGQPVDAKEMQARC----AYVQQDDL 183
Cdd:TIGR04406 13 KRKVVNDVSLSVKSGEIVGLLGPNGAGKTT-----SFYMIVGL-VRPdAGKILIDGQDITHLPMHERArlgiGYLPQEAS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 FIGSLTAREHLIfqAMVRMPRHLTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLI 263
Cdd:TIGR04406 87 IFRKLTVEENIM--AVLEIRKDLDRAEREERLEALLEEFQISHLRDN------KAMSLSGGERRRVEIARALATNPKFIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 264 CDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSEAV 329
Cdd:TIGR04406 159 LDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHN-VRETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
122-319 |
7.52e-19 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 84.79 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKE----MQARCAYVQQDdlfigsltarehlifq 197
Cdd:cd03215 25 AGEIVGIAGLVGNGQTELAEALF-----GLRPPASGEITLDGKPVTRRSprdaIRAGIAYVPED---------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 198 amvrmprhltyRQRVArvdqVIQELSLSkcQHTIIGVpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAH 277
Cdd:cd03215 84 -----------RKREG----LVLDLSVA--ENIALSS-----LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17136592 278 SVVQVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRV 319
Cdd:cd03215 142 EIYRLIRELADAGKAVLLI----SSELDELLglcDRILVMYEGRI 182
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
111-327 |
9.04e-19 |
|
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: 85.80 E-value: 9.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 111 HLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARC----AYVQQD-DLFi 185
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAIS-----GLLPPRSGSIRFDGEDITGLPPHRIArlgiGYVPEGrRIF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 GSLTAREHLIFQAMVRMPRHlTYRQRVARVDQVIQELslskcqHTIIGVPGRVkgLSGGERKRLAFASeAL-TDPPLLIC 264
Cdd:COG0410 91 PSLTVEENLLLGAYARRDRA-EVRADLERVYELFPRL------KERRRQRAGT--LSGGEQQMLAIGR-ALmSRPKLLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 265 DEPTSGLdsftAHSVVQ----VLKKLSQKGKTVILtIHQPSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG0410 161 DEPSLGL----APLIVEeifeIIRRLNREGVTILL-VEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
123-300 |
1.04e-18 |
|
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: 84.85 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAK--EMQARCAYVQQDDLFIGSLTAREHLIFQAmv 200
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILA-----GLSPPLAGRVLLNGGPLDFQrdSIARGLLYLGHAPGIKTTLSVLENLRFWH-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 201 rmPRHLTyrqrvARVDQVIQELSLSKCQHTIIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVV 280
Cdd:cd03231 99 --ADHSD-----EQVEEALARVGLNGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170 180
....*....|....*....|
gi 17136592 281 QVLKKLSQKGKTVILTIHQP 300
Cdd:cd03231 166 EAMAGHCARGGMVVLTTHQD 185
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
123-327 |
1.31e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.75 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALafrspQGIQVSPSGMRLLNGQPV---DAKEMQARCAYVQQDDLFIGSLTARehlifqAM 199
Cdd:PRK09536 29 GSLVGLVGPNGAGKTTLLRAI-----NGTLTPTAGTVLVAGDDVealSARAASRRVASVPQDTSLSFEFDVR------QV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 200 VRMPRHlTYRQRVAR--------VDQVIQELSLSKCqhtiigVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 271
Cdd:PRK09536 98 VEMGRT-PHRSRFDTwtetdraaVERAMERTGVAQF------ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 272 DSFTAHSVVQVLKKLSQKGKTVILTIHqpSSELFELF-DKILLMAEGRVAFLGTPSE 327
Cdd:PRK09536 171 DINHQVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADGRVRAAGPPAD 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
122-330 |
1.97e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.81 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVDAKEMQARCAYV--QQDDLFiGSLTAREHLifqA 198
Cdd:COG3840 24 AGERVAILGPSGAGKSTLLNLIAgFLPPD------SGRILWNGQDLTALPPAERPVSMlfQENNLF-PHLTVAQNI---G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 MVRMPR-HLTYRQRvARVDQVIQELSLSKCQhtiigvpGRVKG-LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTA 276
Cdd:COG3840 94 LGLRPGlKLTAEQR-AQVEQALERVGLAGLL-------DRLPGqLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 277 HSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:COG3840 166 QEMLDLVDELCRErGLTVLMVTHDP-EDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
104-327 |
2.30e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 104 HIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLlnalaFRSPQGIQVSPSGMRLLNGQPVDAKEMQARCAYV----Q 179
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTL-----FRHFNGILKPTSGSVLIRGEPITKENIREVRKFVglvfQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 180 QDDLFIGSLTAREHLIFQamvrmPRHLTYRQRVA--RVDQVIQELSLSkcqHTIIGVPGRvkgLSGGERKRLAFASEALT 257
Cdd:PRK13652 86 NPDDQIFSPTVEQDIAFG-----PINLGLDEETVahRVSSALHMLGLE---ELRDRVPHH---LSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136592 258 DPPLLICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ-LDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
122-330 |
2.87e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNA-LAFRSPQGIQVSPSGMRLlngqPVDAKEMQARCAYVQQDDLFIGSLTAREHLI-FQAM 199
Cdd:PRK13536 66 SGECFGLLGPNGAGKSTIARMiLGMTSPDAGKITVLGVPV----PARARLARARIGVVPQFDNLDLEFTVRENLLvFGRY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 200 VRMprhlTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSV 279
Cdd:PRK13536 142 FGM----STREIEAVIPSLLEFARLESKADA------RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17136592 280 VQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:PRK13536 212 WERLRSLLARGKTILLTTHF-MEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
112-300 |
2.92e-18 |
|
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: 83.56 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVD--AKEMQARCAYVQQDDLFIGSLT 189
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA-----GLLRPDSGEVRWNGTPLAeqRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 190 AREHLIFQAmvrmpRHLTYRQRVarVDQVIQELSLSKCQHTIigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTS 269
Cdd:TIGR01189 90 ALENLHFWA-----AIHGGAQRT--IEDALAAVGLTGFEDLP------AAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|.
gi 17136592 270 GLDSFTAHSVVQVLKKLSQKGKTVILTIHQP 300
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
110-327 |
3.02e-18 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 84.15 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGIQVSPSGMRLLNGQPV-----DAKEMQARCAYV-QQDDL 183
Cdd:cd03260 13 KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIydldvDVLELRRRVGMVfQKPNP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 FIGSltarehlIFQAMVRMPRHLTYRQRVARVDQViqELSLSKcqhtiIGVPGRVK------GLSGGERKRLAFASEALT 257
Cdd:cd03260 93 FPGS-------IYDNVAYGLRLHGIKLKEELDERV--EEALRK-----AALWDEVKdrlhalGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 258 DPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILT--IHQPSSelfeLFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVThnMQQAAR----VADRTAFLLNGRLVEFGPTEQ 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
111-327 |
3.33e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 111 HLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALafrspQGIQVSPSGMRLLNGQPVD--AK---EMQARCAYVQQD-DLF 184
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNL-----NGILKPSSGRILFDGKPIDysRKglmKLRESVGMVFQDpDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSLTAREHLIFQAM-VRMPRHLTYRqrvaRVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLI 263
Cdd:PRK13636 95 LFSASVYQDVSFGAVnLKLPEDEVRK----RVDNALKRTGIEHLKDK------PTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 264 CDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHqpSSELFELF-DKILLMAEGRVAFLGTPSE 327
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATH--DIDIVPLYcDNVFVMKEGRVILQGNPKE 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
122-327 |
3.79e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPV---DAKEMQARCAYVQQDDLFIGSLTAREhLIfq 197
Cdd:PRK11231 27 TGKITALIGPNGCGKSTLLKCFArLLTPQ------SGTVFLGDKPIsmlSSRQLARRLALLPQHHLTPEGITVRE-LV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 198 AMVRMPrHLTYRQRVARVDQVIQELSLSKcQHTIIGVPGRVKGLSGGERKRlAFASEALT-DPPLLICDEPTSGLDsfTA 276
Cdd:PRK11231 98 AYGRSP-WLSLWGRLSAEDNARVNQAMEQ-TRINHLADRRLTDLSGGQRQR-AFLAMVLAqDTPVVLLDEPTTYLD--IN 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 277 HSV--VQVLKKLSQKGKTVILTIH---QPSselfELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK11231 173 HQVelMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQGTPEE 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
112-297 |
4.71e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.71 E-value: 4.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCAYVQQDDLFIGSLtar 191
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLG-----GLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 192 EHLI--FQAM--VRMPR---HLTYRQRVARVDQVIQELSLSK-CQHtiigvpgRVKGLSGGERKRLAFASEALTDPPLLI 263
Cdd:PRK11629 96 HHLLpdFTALenVAMPLligKKKPAEINSRALEMLAAVGLEHrANH-------RPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....
gi 17136592 264 CDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTI 297
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVV 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
122-327 |
5.98e-18 |
|
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: 85.92 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQP-VDAKEMQA------RCAYVQQDD-LFiGSLTAREH 193
Cdd:COG4148 24 GRGVTALFGPSGSGKTTLLRAIA-----GLERPDSGRIRLGGEVlQDSARGIFlpphrrRIGYVFQEArLF-PHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 194 LIFqAMVRMPRhltyRQRVARVDQVIQELS----LSKcqhtiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTS 269
Cdd:COG4148 98 LLY-GRKRAPR----AERRISFDEVVELLGighlLDR----------RPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 270 GLDSFTAHSVVQVLKKLSQKGKTVILTI-HQPsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG4148 163 ALDLARKAEILPYLERLRDELDIPILYVsHSL-DEVARLADHVVLLEQGRVVASGPLAE 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
122-300 |
6.40e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAkemqARCAYvQQDDLFIG-------SLTAREHL 194
Cdd:PRK13538 26 AGELVQIEGPNGAGKTSLLRILA-----GLARPDAGEVLWQGEPIRR----QRDEY-HQDLLYLGhqpgiktELTALENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 195 IF-QAMvrmprhltyrQRVARVDQVIQELSLskcqhtiIGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDEPTS 269
Cdd:PRK13538 96 RFyQRL----------HGPGDDEALWEALAQ-------VGLAGFedvpVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190
....*....|....*....|....*....|....
gi 17136592 270 GLDsftAHSVVQVLKKLSQ---KGKTVILTIHQP 300
Cdd:PRK13538 159 AID---KQGVARLEALLAQhaeQGGMVILTTHQD 189
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
113-327 |
1.04e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.97 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLnaLAFrspQGIQVSPSGMRLLNGQPV--DAK---EMQARCAYVQQ---DDLF 184
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLF--LHF---NGILKPTSGEVLIKGEPIkyDKKsllEVRKTVGIVFQnpdDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 igSLTAREHLIFQAM-VRMPRHLTYRqrvaRVDQVIQELSLS----KCQHTiigvpgrvkgLSGGERKRLAFASEALTDP 259
Cdd:PRK13639 93 --APTVEEDVAFGPLnLGLSKEEVEK----RVKEALKAVGMEgfenKPPHH----------LSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 260 PLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpsSELFELF-DKILLMAEGRVAFLGTPSE 327
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEGTPKE 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
111-327 |
1.71e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.42 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 111 HLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVDA-KEMQAR---CAYVQQDDLFI 185
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQ------QGEILLNGQPIADySEAALRqaiSVVSQRVHLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 GSLtaREHLIFQAMVRMPRHLTyrqrvarvdQVIQELSLSKCQHTI------IGVPGRvkGLSGGERKRLAFASEALTDP 259
Cdd:PRK11160 428 ATL--RDNLLLAAPNASDEALI---------EVLQQVGLEKLLEDDkglnawLGEGGR--QLSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 260 PLLICDEPTSGLDSFTAHSVVQVLKKLSQkGKTVILTIHQpsseLFEL--FDKILLMAEGRVAFLGTPSE 327
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHR----LTGLeqFDRICVMDNGQIIEQGTHQE 559
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
122-330 |
1.82e-17 |
|
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: 82.39 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQAR-CAYVQQDDLFIGSLTAREHLIFQAMV 200
Cdd:cd03296 27 SGELVALLGPSGSGKTTLLRLIA-----GLERPDSGTILFGGEDATDVPVQERnVGFVFQHYALFRHMTVFDNVAFGLRV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 201 R----MPRHLTYRQRVARVDQVIQELSLSKcqhtiiGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTA 276
Cdd:cd03296 102 KprseRPPEAEIRAKVHELLKLVQLDWLAD------RYPAQ---LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 277 HSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:cd03296 173 KELRRWLRRLHDElHVTTVFVTHD-QEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
112-300 |
2.84e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.69 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCAYVQQDDLFIGSLTAR 191
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIA-----GLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 192 EHLIFQAMVrmprhltYRQRVARVDQVIQELSLSKCQHtiigVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGL 271
Cdd:PRK13539 92 ENLEFWAAF-------LGGEELDIAAALEAVGLAPLAH----LPFGY--LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*....
gi 17136592 272 DSFTAHSVVQVLKKLSQKGKTVILTIHQP 300
Cdd:PRK13539 159 DAAAVALFAELIRAHLAQGGIVIAATHIP 187
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
110-331 |
3.06e-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: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSpqGIQVSpSGMRLLNGQPVDAKEMQARcayvqqddlfigslt 189
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHP--KYEVT-EGEILFKGEDITDLPPEER--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 190 ARE--HLIFQAMVRMPRhltyrqrvARVDQVIQELSlskcqhtiigvpgrvKGLSGGERKRLAFASEALTDPPLLICDEP 267
Cdd:cd03217 75 ARLgiFLAFQYPPEIPG--------VKNADFLRYVN---------------EGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 268 TSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPssELFELF--DKILLMAEGRVAFLGTPSEAVDF 331
Cdd:cd03217 132 DSGLDIDALRLVAEVINKLREEGKSVLIITHYQ--RLLDYIkpDRVHVLYDGRIVKSGDKELALEI 195
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
94-332 |
3.27e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 94 RTRGLFCNERHIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIqVSP-SGMRLLNGQ---PVdak 169
Cdd:COG1134 23 SLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA-----GI-LEPtSGRVEVNGRvsaLL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 170 EMQARcayvqqddlFIGSLTAREHLIFQAMVR-MPRhltyRQRVARVDQVIQ--ELSlskcQHtiIGVPgrVKGLSGGER 246
Cdd:COG1134 94 ELGAG---------FHPELTGRENIYLNGRLLgLSR----KEIDEKFDEIVEfaELG----DF--IDQP--VKTYSSGMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 247 KRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGTPS 326
Cdd:COG1134 153 ARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDGDPE 231
|
....*.
gi 17136592 327 EAVDFF 332
Cdd:COG1134 232 EVIAAY 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
108-319 |
4.40e-17 |
|
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: 80.98 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVspsgmrLLNGQPV---DAKEMQARCAYVQQDD- 182
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnFYQPQGGQV------LLDGKPIsqyEHKYLHSKVSLVGQEPv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 LFIGSLtaREHLIFQAMVRMPRHLTYRQRVARVDQVIQELSLSkcQHTIIGVPGRVkgLSGGERKRLAFASEALTDPPLL 262
Cdd:cd03248 99 LFARSL--QDNIAYGLQSCSFECVKEAAQKAHAHSFISELASG--YDTEVGEKGSQ--LSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 263 ICDEPTSGLDSFTAHSVVQVLKKLSQKgKTVILTIHQPSseLFELFDKILLMAEGRV 319
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLS--TVERADQILVLDGGRI 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
84-323 |
4.42e-17 |
|
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: 80.65 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 84 PGSGWRQLVNRTRGLFCNERhipaPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNG 163
Cdd:cd03220 13 YKGGSSSLKKLGILGRKGEV----GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLA-----GIYPPDSGTVTVRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 164 QPVDAKEMQARcayvqqddlFIGSLTAREHLIFQAMVrmpRHLTYRQRVARVDQvIQELS-LSKCQHTiigvpgRVKGLS 242
Cdd:cd03220 84 RVSSLLGLGGG---------FNPELTGRENIYLNGRL---LGLSRKEIDEKIDE-IIEFSeLGDFIDL------PVKTYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 243 GGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSeLFELFDKILLMAEGRVAFL 322
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFD 223
|
.
gi 17136592 323 G 323
Cdd:cd03220 224 G 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
121-350 |
4.81e-17 |
|
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: 81.54 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 121 YPGELLAVMGSSGAGKTTL---LNALafrspqgiqVSP-SGMRLLNGQPV---DAKEMQA----RCAYVQQDDLFIGSLT 189
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLlrcINRL---------IEPtSGKVLIDGQDIaamSRKELRElrrkKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 190 AREHLIFQAMVR-MPRhltyRQRVARVDQVIQELSLSKCQHTIIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPT 268
Cdd:cd03294 119 VLENVAFGLEVQgVPR----AEREERAAEALELVGLEGWEHKYPD------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 269 SGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSEAVDffsyvgaqcptnyNPAD 347
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElQKTIVFITHDL-DEALRLGDRIAIMKDGRLVQVGTPEEILT-------------NPAN 254
|
...
gi 17136592 348 FYV 350
Cdd:cd03294 255 DYV 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
109-320 |
8.41e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKE----MQARCAYVQQDDL- 183
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALF-----GADPADSGEIRLDGKPVRIRSprdaIRAGIAYVPEDRKg 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 --FIGSLTAREHLIFQAMVRMPRH--LTYRQRVARVDQVIQELSLsKCQHtiIGVPgrVKGLSGGERKRLAFASEALTDP 259
Cdd:COG1129 339 egLVLDLSIRENITLASLDRLSRGglLDRRRERALAEEYIKRLRI-KTPS--PEQP--VGNLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136592 260 PLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRVA 320
Cdd:COG1129 414 KVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI----SSELPELLglsDRILVMREGRIV 473
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
122-320 |
8.68e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 8.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVDAKemQARCAYVQQDDLFIGSLTAREHLIFQAMV 200
Cdd:PRK11248 26 SGELLVVLGPSGCGKTTLLNLIAgFVPYQ------HGSITLDGKPVEGP--GAERGVVFQNEGLLPWRNVQDNVAFGLQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 201 R-MPRhltyRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSV 279
Cdd:PRK11248 98 AgVEK----MQRLEIAHQMLKKVGLEGAEKR------YIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17136592 280 VQVLKKLSQK-GKTVILTIHQPSSELFELFDKILLM-AEGRVA 320
Cdd:PRK11248 168 QTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSpGPGRVV 210
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
109-327 |
1.65e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.30 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIqVSP-SGMRLLNGQPVDAKEMQARC----AYVQQD-D 182
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIV-----GL-VKPdSGRIFLDGEDITHLPMHKRArlgiGYLPQEaS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 LFIGsLTAREHLifQAMVRMpRHLTYRQRVARVDQVIQELSLSKCQHTiigvpgrvKG--LSGGERKRLAFAsEAL-TDP 259
Cdd:COG1137 89 IFRK-LTVEDNI--LAVLEL-RKLSKKEREERLEELLEEFGITHLRKS--------KAysLSGGERRRVEIA-RALaTNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 260 PLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNV-RETLGICDRAYIISEGKVLAEGTPEE 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
112-299 |
1.76e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.01 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAF---RSPQGIQVSPSGMRLlngqpVDAKEMQARCAYVQQddlfIGSL 188
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFlekPSEGSIVVNGQTINL-----VRDKDGQLKVADKNQ----LRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHLIFQAMvRMPRHLTYRQRVarVDQVIQELSLSKCQH--------TIIGVPGRVKG-----LSGGERKRLAFASEA 255
Cdd:PRK10619 91 RTRLTMVFQHF-NLWSHMTVLENV--MEAPIQVLGLSKQEAreravkylAKVGIDERAQGkypvhLSGGQQQRVSIARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17136592 256 LTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQ 299
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
112-300 |
2.19e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.67 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCA-------YVQQDDLF 184
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILA-----GLDDGSSGEVSLVGQPLHQMDEEARAKlrakhvgFVFQSFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSLTAREHLIFQAMVRMPRHLTYRQRVArvdQVIQELSLSKCQHTIigvPGRvkgLSGGERKRLAFASEALTDPPLLIC 264
Cdd:PRK10584 100 IPTLNALENVELPALLRGESSRQSRNGAK---ALLEQLGLGKRLDHL---PAQ---LSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQP 300
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
122-330 |
6.03e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.83 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLL---NALafrspqgiQVSPSGMRLLNGQPV-----DAKEMQARCAYV-QQDDLFiGSLTARE 192
Cdd:PRK09493 26 QGEVVVIIGPSGSGKSTLLrciNKL--------EEITSGDLIVDGLKVndpkvDERLIRQEAGMVfQQFYLF-PHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 193 HLIFQamvrmPRHlTYRQRVARVDQVIQELsLSKcqhtiIGVPGRV----KGLSGGERKRLAFASEALTDPPLLICDEPT 268
Cdd:PRK09493 97 NVMFG-----PLR-VRGASKEEAEKQAREL-LAK-----VGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136592 269 SGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSselF--ELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEEGMTMVIVTHEIG---FaeKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
113-320 |
7.74e-16 |
|
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: 75.54 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDakemqarcayvqqddlFIGSLTARE 192
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILS-----GLYKPDSGEILVDGKEVS----------------FASPRDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 193 HLIfqAMVrmprHltyrqrvarvdqviqelslskcQhtiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 272
Cdd:cd03216 75 AGI--AMV----Y----------------------Q------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17136592 273 SFTAHSVVQVLKKLSQKGKTVILTIHQPsSELFELFDKILLMAEGRVA 320
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRL-DEVFEIADRVTVLRDGRVV 161
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
113-330 |
1.19e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.39 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNAL--AFrSPQGIQVSPSGMrllNGQPVDAKEMQARCAYVQQDD-LFIGSLt 189
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrVF-DPQSGRILIDGT---DIRTVTRASLRRNIAVVFQDAgLFNRSI- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 190 aREHLifqamvrmprhltyrqRVARVDQVIQELSL--------------SKCQHTIIGVPGRVkgLSGGERKRLAFASEA 255
Cdd:PRK13657 426 -EDNI----------------RVGRPDATDEEMRAaaeraqahdfierkPDGYDTVVGERGRQ--LSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 256 LTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSqKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLST--VRNADRILVFDNGRVVESGSFDELVA 558
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
108-324 |
1.45e-15 |
|
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: 80.25 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNaLAFR--SPQGIQVspsgmrLLNGQP---VDAKEMQARCAYVQQDD 182
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR-LLFRfyDVTSGRI------LIDGQDirdVTQASLRAAIGIVPQDT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 -LF-------I--GSLTAREHLIFQAMvrmprhltyrqRVARVDQVIQelSLSKCQHTIIGVPGrVKgLSGGERKRLAFA 252
Cdd:COG5265 442 vLFndtiaynIayGRPDASEEEVEAAA-----------RAAQIHDFIE--SLPDGYDTRVGERG-LK-LSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 253 SEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQkGKTVILTIHQPS----SelfelfDKILLMAEGRVAFLGT 324
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHRLStivdA------DEILVLEAGRIVERGT 575
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
113-327 |
1.50e-15 |
|
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: 76.42 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPV---DAKEMQARCAYVQQD-DLFIGS 187
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErFYDPT------SGEILLDGVDIrdlNLRWLRSQIGLVSQEpVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 LtaREHLIFQamvRMPRHLTYRQRVARV---DQVIQelSLSKCQHTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLIC 264
Cdd:cd03249 93 I--AENIRYG---KPDATDEEVEEAAKKaniHDFIM--SLPDGYDTLVGERG--SQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 265 DEPTSGLDsftAHSVVQVLKKLSQ--KGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03249 164 DEATSALD---AESEKLVQEALDRamKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQGTHDE 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
122-327 |
1.67e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.58 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGI-QVSpSGMRLLNGQPVDAKEMQAR-CAYV-QQDDLFiGSLTAREHLIF-Q 197
Cdd:COG3839 28 DGEFLVLLGPSGCGKSTLLRMIA-----GLeDPT-SGEILIGGRDVTDLPPKDRnIAMVfQSYALY-PHMTVYENIAFpL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 198 AMVRMPRhltyRQRVARVDQV-----IQELsLSKcqhtiigvpgRVKGLSGGERKRLAFAsEAL-TDPPLLICDEPTSGL 271
Cdd:COG3839 101 KLRKVPK----AEIDRRVREAaellgLEDL-LDR----------KPKQLSGGQRQRVALG-RALvREPKVFLLDEPLSNL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 272 DsftAHSVVQV---LKKLSQK-GKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:COG3839 165 D---AKLRVEMraeIKRLHRRlGTTTIYVTHDQ-VEAMTLADRIAVMNDGRIQQVGTPEE 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
123-323 |
1.79e-15 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 75.75 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQAR-CAYVQQDDLFIGSLTAREHLIFQAMVR 201
Cdd:cd03301 26 GEFVVLLGPSGCGKTTTLRMIA-----GLEEPTSGRIYIGGRDVTDLPPKDRdIAMVFQNYALYPHMTVYDNIAFGLKLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 202 MPRHLTYRQRVARVDQVIQ-ELSLSKcqhtiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsftAHSVV 280
Cdd:cd03301 101 KVPKDEIDERVREVAELLQiEHLLDR----------KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD---AKLRV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17136592 281 QV---LKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 323
Cdd:cd03301 168 QMraeLKRLQQRlGTTTIYVTHD-QVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
94-323 |
2.21e-15 |
|
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: 76.22 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 94 RTRGLFCNERHIPAPRKHLLKNVCGVAYP---GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSG-MRLLNGQPVDAK 169
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYREVEALKGISFTiekGEIVGFIGPNGAGKTTTLKILS-----GLLQPTSGeVRVAGLVPWKRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 170 EmqarcAYVQQDDLFIGSltaREHLIFQAMV----RMPRHLtYRQRVARVDQVIQELS-LSKCQHtIIGVPgrVKGLSGG 244
Cdd:cd03267 90 K-----KFLRRIGVVFGQ---KTQLWWDLPVidsfYLLAAI-YDLPPARFKKRLDELSeLLDLEE-LLDTP--VRQLSLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 245 ERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLS-QKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 323
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSHY-MKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
123-330 |
2.32e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfRSPQGIQVSPSGMRLLnGQPV--------DAKEMQARCAYVQQDDLFIGSLTAREHL 194
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLS-GLITGDKSAGSHIELL-GRTVqregrlarDIRKSRANTGYIFQQFNLVNRLSVLENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 195 IFQAMVRMP------RHLTYRQRvARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPT 268
Cdd:PRK09984 108 LIGALGSTPfwrtcfSWFTREQK-QRALQALTRVGMVHFAHQ------RVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 269 SGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQPSSELfELFDKILLMAEGRVAFLGTpSEAVD 330
Cdd:PRK09984 181 ASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDGS-SQQFD 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
113-300 |
2.64e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.77 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALafrspqGIQVSP-SGMRLLNGQPVdakemqarcAYVQQDDLfigSLTAR 191
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNIL------GCLDKPtSGTYRVAGQDV---------ATLDADAL---AQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 192 EHL--IFQAMVRMPrHLT---------------YRQRVARVDQVIQELSLSKcqhtiiGVPGRVKGLSGGERKRLAFASE 254
Cdd:PRK10535 86 EHFgfIFQRYHLLS-HLTaaqnvevpavyagleRKQRLLRAQELLQRLGLED------RVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17136592 255 ALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQP 300
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
101-327 |
4.51e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.02 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 101 NERHIPAPRKH--LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGiqVSPSGMRL-----LNGQP---VDAKE 170
Cdd:PRK13547 3 TADHLHVARRHraILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGG--GAPRGARVtgdvtLNGEPlaaIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 171 MQARCAYVQQDDLFIGSLTAREHLIfqaMVRMPrHLTYRQRVARVDQVIQELSLSKCQHTIIGvpGR-VKGLSGGERKRL 249
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVL---LGRYP-HARRAGALTHRDGEIAWQALALAGATALV--GRdVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 250 AFA---------SEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTI-HQPSSELfELFDKILLMAEGRV 319
Cdd:PRK13547 155 QFArvlaqlwppHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAA-RHADRIAMLADGAI 233
|
....*...
gi 17136592 320 AFLGTPSE 327
Cdd:PRK13547 234 VAHGAPAD 241
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
122-319 |
5.14e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.35 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNA-LAFRSPQG-IQVspsgmrllNGQP---VDAKEMQARCAYVQQD-DLFIGSL------- 188
Cdd:PRK11174 375 AGQRIALVGPSGAGKTSLLNAlLGFLPYQGsLKI--------NGIElreLDPESWRKHLSWVGQNpQLPHGTLrdnvllg 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 --TAREHLIFQAMVRmprhltyrqrvARVDQVIQELSLSkcQHTIIGvpGRVKGLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:PRK11174 447 npDASDEQLQQALEN-----------AWVSEFLPLLPQG--LDTPIG--DQAAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQkGKTVILTIHQpsseLFEL--FDKILLMAEGRV 319
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASR-RQTTLMVTHQ----LEDLaqWDQIWVMQDGQI 561
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
108-327 |
1.51e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.45 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVspsgmrLLNGQPV---DAKEMQARCAYVQQDD- 182
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnLYQPTGGQV------LLDGVPLvqyDHHYLHRQVALVGQEPv 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 LFIGSLTareHLIFQAMVRMPR-HLTYRQRVARVDQVIQELSlsKCQHTIIGVPGRVkgLSGGERKRLAFASEALTDPPL 261
Cdd:TIGR00958 566 LFSGSVR---ENIAYGLTDTPDeEIMAAAKAANAHDFIMEFP--NGYDTEVGEKGSQ--LSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 262 LICDEPTSGLDSFTAHSVVQvlkKLSQKGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPSE 327
Cdd:TIGR00958 639 LILDEATSALDAECEQLLQE---SRSRASRTVLLIAHRLS--TVERADQILVLKKGSVVEMGTHKQ 699
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
121-325 |
1.52e-14 |
|
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: 77.75 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 121 YPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAK--EMQARCAYVQQDDLFIGSLTAREHLIFQA 198
Cdd:TIGR01257 954 YENQITAFLGHNGAGKTTTLSILT-----GLLPPTSGTVLVGGKDIETNldAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 MVRmprHLTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHS 278
Cdd:TIGR01257 1029 QLK---GRSWEEAQLEMEAMLEDTGLHHKRNE------EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17136592 279 VVQVLKKLsQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTP 325
Cdd:TIGR01257 1100 IWDLLLKY-RSGRTIIMSTHH-MDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
113-319 |
1.59e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPqgiqvSPSGMRLLNGQPVDAKEMQ----ARCAYVQQD----DLF 184
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP-----RTSGYVTLDGHEVVTRSPQdglaNGIVYISEDrkrdGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IG-------SLTAREHLIfqamvRMPRHLTYRQRVARVDQVIQELSlskcqhtiIGVPGR---VKGLSGGERKRLAFASE 254
Cdd:PRK10762 343 LGmsvkenmSLTALRYFS-----RAGGSLKHADEQQAVSDFIRLFN--------IKTPSMeqaIGLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 255 ALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRV 319
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILV----SSEMPEVLgmsDRILVMHEGRI 473
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
113-327 |
1.83e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.28 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTL---LNALAFrsPQgiqvspSGMRLLNGQPVDAK---EMQARCAYVQQ--DDLF 184
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLL--PE------AGTITVGGMVLSEEtvwDVRRQVGMVFQnpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSlTAREHLIFQAMVR-MPRHltyrQRVARVDQVIQELSLSKCQHTiigVPGRvkgLSGGERKRLAFASEALTDPPLLI 263
Cdd:PRK13635 95 VGA-TVQDDVAFGLENIgVPRE----EMVERVDQALRQVGMEDFLNR---EPHR---LSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 264 CDEPTSGLDSFTAHSVVQVLKKL-SQKGKTVILTIHQPSSELFElfDKILLMAEGRVAFLGTPSE 327
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQA--DRVIVMNKGEILEEGTPEE 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
123-327 |
1.90e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.12 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQpvDAKEMQAR---CAYVQQDDLFIGSLTAREHLIFQAM 199
Cdd:PRK10851 28 GQMVALLGPSGSGKTTLLRIIA-----GLEHQTSGHIRFHGT--DVSRLHARdrkVGFVFQHYALFRHMTVFDNIAFGLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 200 VrMPRHltYRQRVARVDQ-VIQELSLSKCQHTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHS 278
Cdd:PRK10851 101 V-LPRR--ERPNAAAIKAkVTQLLEMVQLAHLADRYPAQ---LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17136592 279 VVQVLKKLSQKGK--TVILTIHQpsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK10851 175 LRRWLRQLHEELKftSVFVTHDQ--EEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
122-333 |
2.39e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 74.73 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLL---NALafrspqgiQVSPSGMRLLNGQPV---DAKEM-QARcayvQQddlfIGsltarehL 194
Cdd:COG1135 30 KGEIFGIIGYSGAGKSTLIrciNLL--------ERPTSGSVLVDGVDLtalSERELrAAR----RK----IG-------M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 195 IFQ--------------AM----VRMPRhltyRQRVARVDQVIqELslskcqhtiIGVPGRVKG----LSGGERKRLAFA 252
Cdd:COG1135 87 IFQhfnllssrtvaenvALpleiAGVPK----AEIRKRVAELL-EL---------VGLSDKADAypsqLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 253 sEAL-TDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTpseAVD 330
Cdd:COG1135 153 -RALaNNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHE-MDVVRRICDRVAVLENGRIVEQGP---VLD 227
|
...
gi 17136592 331 FFS 333
Cdd:COG1135 228 VFA 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
96-328 |
2.41e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 96 RGLFC-NERHIPAprkhlLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKEM 171
Cdd:COG3845 261 ENLSVrDDRGVPA-----LKDVSLEVRAGEILGIAGVAGNGQSELAEALA-----GLRPPASGSIRLDGEDItglSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 172 -QARCAYVQQDDL---FIGSLTAREHLIFQAMVRMP--RHLTYRQRVAR--VDQVIQELSlskcqhtiIGVPG---RVKG 240
Cdd:COG3845 331 rRLGVAYIPEDRLgrgLVPDMSVAENLILGRYRRPPfsRGGFLDRKAIRafAEELIEEFD--------VRTPGpdtPARS 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILtIhqpSSELFELF---DKILLMAEG 317
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLL-I---SEDLDEILalsDRIAVMYEG 478
|
250
....*....|.
gi 17136592 318 RVAFLGTPSEA 328
Cdd:COG3845 479 RIVGEVPAAEA 489
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
122-289 |
2.41e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 76.26 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALafrspqgiqvspsgMRLL--------NGQPVDA---KEMQARCAYVQ---QDDLfiGS 187
Cdd:COG4172 311 RGETLGLVGESGSGKSTLGLAL--------------LRLIpsegeirfDGQDLDGlsrRALRPLRRRMQvvfQDPF--GS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 LTAR---EHLIFQAMVRMPRHLTYRQRVARVDQVIQElslskcqhtiIGVPGRVKG-----LSGGERKRLAFAsEAL-TD 258
Cdd:COG4172 375 LSPRmtvGQIIAEGLRVHGPGLSAAERRARVAEALEE----------VGLDPAARHrypheFSGGQRQRIAIA-RALiLE 443
|
170 180 190
....*....|....*....|....*....|.
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKLSQK 289
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDLQRE 474
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
112-300 |
3.33e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.50 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVSPSGmrllngqpvdakemQARCAYVQQ----DDLFig 186
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAgVLRPTSGTVRRAG--------------GARVAYVPQrsevPDSL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 SLTAREHLifqAMVRMP-----RHLTYRQRvARVDQVIQELSLSkcqhtiiGVPGR-VKGLSGGERKRLAFASEALTDPP 260
Cdd:NF040873 71 PLTVRDLV---AMGRWArrglwRRLTRDDR-AAVDDALERVGLA-------DLAGRqLGELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17136592 261 LLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQP 300
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
108-338 |
3.59e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.18 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVSpsgmrlLNGQPVDAKEMQARCAY---VQ---Q 180
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVgLESPSQGNVS------WRGEPLAKLNRAQRKAFrrdIQmvfQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 181 DDlfIGSLTAREHLifQAMVRMP-RHLTY---RQRVARVDQVIQELSL-----SKCqhtiigvPGRvkgLSGGERKRLAF 251
Cdd:PRK10419 97 DS--ISAVNPRKTV--REIIREPlRHLLSldkAERLARASEMLRAVDLddsvlDKR-------PPQ---LSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 252 ASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTI-HQPSseLFELF-DKILLMAEGRVAFLGTPSEAV 329
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFItHDLR--LVERFcQRVMVMDNGQIVETQPVGDKL 240
|
....*....
gi 17136592 330 DFFSYVGAQ 338
Cdd:PRK10419 241 TFSSPAGRV 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
93-324 |
5.46e-14 |
|
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: 76.21 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 93 NRTRGLFCNE--RHIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTllnalAFRSPQGIQVSPSGMRLLNGQPV--DA 168
Cdd:TIGR01257 1933 NKTDILRLNEltKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTT-----TFKMLTGDTTVTSGDATVAGKSIltNI 2007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 169 KEMQARCAYVQQDDLFIGSLTAREHLIFQAMVR-MPRhltyrQRVARV-DQVIQELSLSKCQHTIIGVpgrvkgLSGGER 246
Cdd:TIGR01257 2008 SDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRgVPA-----EEIEKVaNWSIQSLGLSLYADRLAGT------YSGGNK 2076
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 247 KRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGT 324
Cdd:TIGR01257 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS-MEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
240-327 |
6.18e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.35 E-value: 6.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 240 GLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELfELFDKILLMAEGRV 319
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVL-EVADEVIVMDKGKI 254
|
....*...
gi 17136592 320 AFLGTPSE 327
Cdd:PRK13631 255 LKTGTPYE 262
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
121-295 |
6.23e-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: 73.16 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 121 YPGELLAVMGSSGAGKTTLLNALAfR--SPQGIQvspSGMRLLNGQPV---DAKEMQA----RCAYVQQDDLfiGSL--- 188
Cdd:COG0444 29 RRGETLGLVGESGSGKSTLARAIL-GllPPPGIT---SGEILFDGEDLlklSEKELRKirgrEIQMIFQDPM--TSLnpv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 -TAREHLIfqAMVRMPRHLTYRQRVARVDQVIQELSLSKcqhtiigvPGRVKG-----LSGGERKRLAFASeAL-TDPPL 261
Cdd:COG0444 103 mTVGDQIA--EPLRIHGGLSKAEARERAIELLERVGLPD--------PERRLDrypheLSGGMRQRVMIAR-ALaLEPKL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 17136592 262 LICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVIL 295
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLQRElGLAILF 206
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
122-327 |
8.00e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAFRSPqgiqvSPSGMRLLNGQPV---DAKEMQARCAYVQQDDLFIGSLTAREhliFQA 198
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGRHQP-----PSEGEILLDAQPLeswSSKAFARKVAYLPQQLPAAEGMTVRE---LVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 MVRMPRHLTY-RQRVA---RVDQVIQELSLSKCQHTIigvpgrVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsf 274
Cdd:PRK10575 108 IGRYPWHGALgRFGAAdreKVEEAISLVGLKPLAHRL------VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD-- 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 275 TAHS--VVQVLKKLSQ-KGKTVILTIHQPSSELfELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK10575 180 IAHQvdVLALVHRLSQeRGLTVIAVLHDINMAA-RYCDYLVALRGGEMIAQGTPAE 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
113-323 |
9.61e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVD----AKEMQARCAYVQQDDLFIGSL 188
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIA-----GIVPPDSGTLEIGGNPCArltpAKAHQLGIYLVPQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHLIFqamvRMPRHltyRQRVARVDQVIQELSLSKCQHTIIGVpgrvkgLSGGERKRLAFASEALTDPPLLICDEPT 268
Cdd:PRK15439 102 SVKENILF----GLPKR---QASMQKMKQLLAALGCQLDLDSSAGS------LEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 269 SGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLG 323
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLAQGVGIVFISHK-LPEIRQLADRISVMRDGTIALSG 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
110-327 |
1.08e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.08 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTllnalAFRSPQGIQVSPSGMRLLNGQPVDAKEMQARC----AYVQQDDLFI 185
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTT-----TFYMVVGIVPRDAGNIIIDDEDISLLPLHARArrgiGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 GSLTAREHLIfqAMVRMPRHLTYRQRVARVDQVIQELSLSKCQHTIigvpgrVKGLSGGERKRLAFASEALTDPPLLICD 265
Cdd:PRK10895 91 RRLSVYDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM------GQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 266 EPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN-VRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
123-319 |
1.21e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.06 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVD----AKEMQARCAYVQQDDLFIGSLTAREHLIFQA 198
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLC-----GDPRATSGRIVFDGKDITdwqtAKIMREAVAIVPEGRRVFSRMTVEENLAMGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 MvrMPRHLTYRQRVARVDQVIQELSLSKCQhtiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHS 278
Cdd:PRK11614 106 F--FAERDQFQERIKWVYELFPRLHERRIQ--------RAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17136592 279 VVQVLKKLSQKGKTVILtIHQPSSELFELFDKILLMAEGRV 319
Cdd:PRK11614 176 IFDTIEQLREQGMTIFL-VEQNANQALKLADRGYVLENGHV 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
113-327 |
1.32e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.02 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGIQVspsgmrLLNGQPVDAKEMQA---RCAYVQQDDLFIGSLT 189
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEI------LLNGRPLSDWSAAElarHRAYLSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 190 AREHLifqaMVRMPRHLTYRQRVARVDQVIQELSLSKCQHTIIGvpgrvkGLSGGE--RKRLAFA-----SEALTDPPLL 262
Cdd:COG4138 86 VFQYL----ALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLT------QLSGGEwqRVRLAAVllqvwPTINPEGQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 263 ICDEPTSGLDsfTAHSVV--QVLKKLSQKGKTVILTIHQPSSELFELfDKILLMAEGRVAFLGTPSE 327
Cdd:COG4138 156 LLDEPMNSLD--VAQQAAldRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASGETAE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
94-319 |
1.32e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 94 RTRGLFCNerHIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALaFRSPQGiqvSPSGMRLLNGQPVD----AK 169
Cdd:TIGR02633 259 EARNLTCW--DVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQAL-FGAYPG---KFEGNVFINGKPVDirnpAQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 170 EMQARCAYVQQD--------DLFIG---SLTAREHLIFQAMVRMPRHLtyrqrvARVDQVIQELSLsKCQHTIIGVpgrv 238
Cdd:TIGR02633 333 AIRAGIAMVPEDrkrhgivpILGVGkniTLSVLKSFCFKMRIDAAAEL------QIIGSAIQRLKV-KTASPFLPI---- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 239 KGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTihqpSSELFE---LFDKILLMA 315
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVV----SSELAEvlgLSDRVLVIG 477
|
....
gi 17136592 316 EGRV 319
Cdd:TIGR02633 478 EGKL 481
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
123-296 |
1.49e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.81 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNAL-AFRSPQGIQVSPSGMRLLNGQPVDAKEMQARCAYV----QQDDLFiGSLTAREHLIfQ 197
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLnLLEMPRSGTLNIAGNHFDFSKTPSDKAIRELRRNVgmvfQQYNLW-PHLTVQQNLI-E 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 198 AMVRMpRHLTYRQRVARVDQVIQELSLSKC-----QHtiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD 272
Cdd:PRK11124 106 APCRV-LGLSKDQALARAEKLLERLRLKPYadrfpLH-----------LSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180
....*....|....*....|....*
gi 17136592 273 SFTAHSVVQVLKKLSQKGKT-VILT 296
Cdd:PRK11124 174 PEITAQIVSIIRELAETGITqVIVT 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
113-325 |
1.66e-13 |
|
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: 70.22 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALaFRSpqgIQVSpSGMRLLNGQP---VDAKEMQARCAYVQQDD-LFIGSL 188
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLAL-FRL---VELS-SGSILIDGVDiskIGLHDLRSRISIIPQDPvLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 taREHL----------IFQAMVRmprhltyrqrvARVDQVIQELSlskcqhtiIGVPGRV----KGLSGGERKRLAFASE 254
Cdd:cd03244 95 --RSNLdpfgeysdeeLWQALER-----------VGLKEFVESLP--------GGLDTVVeeggENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 255 ALTDPPLLICDEPTSGLDSFTAHSVVQVLKKlSQKGKTVIL------TIHQpsselfelFDKILLMAEGRVAFLGTP 325
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTiahrldTIID--------SDRILVLDKGRVVEFDSP 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
110-321 |
1.84e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCAY---VQQDDLfIG 186
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA-----GSLPPDSGSILIDGKDVTKLPEYKRAKYigrVFQDPM-MG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 ---SLTAREHLIFQAMVRMPRHLTYRQRVARVDQVIQELSLSKcqhtiIGVPGR----VKGLSGGERKRLAFASEALTDP 259
Cdd:COG1101 93 tapSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLATLG-----LGLENRldtkVGLLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 260 PLLICDEPTSGLDSFTAHSVVQVLKKLSQKGK-TVILTIHQPSSELfELFDKILLMAEGRVAF 321
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQAL-DYGNRLIMMHEGRIIL 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
122-327 |
1.93e-13 |
|
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: 70.34 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQP---VDAKEMQARCAYvQQDDLFiGSLTAREHLIFQ- 197
Cdd:cd03300 25 EGEFFTLLGPSGCGKTTLLRLIA-----GFETPTSGEILLDGKDitnLPPHKRPVNTVF-QNYALF-PHLTVFENIAFGl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 198 AMVRMPRHLTyRQRVARVDQVIQELSLSKcqhtiigvpGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAH 277
Cdd:cd03300 98 RLKKLPKAEI-KERVAEALDLVQLEGYAN---------RKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17136592 278 SVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03300 168 DMQLELKRLQKElGITFVFVTHD-QEEALTMSDRIAVMNKGKIQQIGTPEE 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
110-327 |
2.37e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 70.79 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDA---KEMQARCAYVQQ--DDLF 184
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILT-----GLLKPQSGEIKIDGITISKenlKEIRKKIGIIFQnpDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSlTAREHLIFQAMVRM-PRHltyrqrvaRVDQVIQELSlskcqhTIIGVPGRVK----GLSGGERKRLAFASEALTDP 259
Cdd:PRK13632 97 IGA-TVEDDIAFGLENKKvPPK--------KMKDIIDDLA------KKVGMEDYLDkepqNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 260 PLLICDEPTSGLDSFTAHSVVQVLKKLSQKG-KTVILTIHQPSSELfeLFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI--LADKVIVFSEGKLIAQGKPKE 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
110-289 |
3.19e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALaFRspqgiQVSPSGMRLLNGQPV---DAKEM---QARCAYVQQDDl 183
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLAL-LR-----LINSQGEIWFDGQPLhnlNRRQLlpvRHRIQVVFQDP- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 fIGSLTAR---EHLIFQAMVRMPRHLTYRQRVARVDQVIQELSLS-KCQHTiigVPGRvkgLSGGERKRLAFASEALTDP 259
Cdd:PRK15134 372 -NSSLNPRlnvLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDpETRHR---YPAE---FSGGQRQRIAIARALILKP 444
|
170 180 190
....*....|....*....|....*....|
gi 17136592 260 PLLICDEPTSGLDSFTAHSVVQVLKKLSQK 289
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
110-332 |
3.27e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.53 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNAL----AFRSPQG-----IQVSPSGMRLlnGQPVDAKEMQARCA---- 176
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdQYEPTSGriiyhVALCEKCGYV--ERPSKVGEPCPVCGgtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 177 -----YVQQDDLFIGSLTAREHLIFQA-------------MVRMPRHLTYRQRVArVDQVIQELSLSKCQHTIIGVpgrV 238
Cdd:TIGR03269 91 peevdFWNLSDKLRRRIRKRIAIMLQRtfalygddtvldnVLEALEEIGYEGKEA-VGRAVDLIEMVQLSHRITHI---A 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 239 KGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKL-SQKGKTVILTIHQPSSeLFELFDKILLMAEG 317
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEV-IEDLSDKAIWLENG 245
|
250
....*....|....*
gi 17136592 318 RVAFLGTPSEAVDFF 332
Cdd:TIGR03269 246 EIKEEGTPDEVVAVF 260
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
122-330 |
4.52e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCAYV--QQDDLFigsltarEHLIFQAM 199
Cdd:PRK10771 24 RGERVAILGPSGAGKSTLLNLIA-----GFLTPASGSLTLNGQDHTTTPPSRRPVSMlfQENNLF-------SHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 200 VRMPRH----LTYRQRvARVDQVIQELSLSKCqhtIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFT 275
Cdd:PRK10771 92 IGLGLNpglkLNAAQR-EKLHAIARQMGIEDL---LARLPGQ---LSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 276 AHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:PRK10771 165 RQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
122-319 |
5.29e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 69.39 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAF-RSPQG--IQV---SPSGMRLLNGQPVDAKEMQARCAYVQQDDLFIGSLTAREHLI 195
Cdd:PRK11264 28 PGEVVAIIGPSGSGKTTLLRCINLlEQPEAgtIRVgdiTIDTARSLSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLENII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 196 FQAMV--RMPRHltyrQRVARVDQVIQELSLSKCQHTiigVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDS 273
Cdd:PRK11264 108 EGPVIvkGEPKE----EATARARELLAKVGLAGKETS---YPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17136592 274 FTAHSVVQVLKKLSQKGKTVILTIHQPSselF--ELFDKILLMAEGRV 319
Cdd:PRK11264 178 ELVGEVLNTIRQLAQEKRTMVIVTHEMS---FarDVADRAIFMDQGRI 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
122-324 |
5.96e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.50 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNG-QPVdaKEmqaRCAYVQQddlfIGS-----------LT 189
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLT-----GILVPTSGEVRVLGyVPF--KR---RKEFARR----IGVvfgqrsqlwwdLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 190 AREHL-IFQAMVRMPRHlTYRQRVarvDQVIQELSLSKcqhtIIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPT 268
Cdd:COG4586 113 AIDSFrLLKAIYRIPDA-EYKKRL---DELVELLDLGE----LLDTP--VRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 269 SGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGT 324
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRErGTTILLTSHD-MDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
122-327 |
7.89e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 68.96 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKEMQARCAYVQQDDLFIGSLTAREHLIFQa 198
Cdd:COG4604 26 KGGITALIGPNGAGKSTLLSMIS-----RLLPPDSGEVLVDGLDVattPSRELAKRLAILRQENHINSRLTVRELVAFG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 mvRMPRH---LTYRQRvARVDQVIQELSLSKCQHTIIgvpgrvKGLSGGERKRlAFASEAL---TDPPLLicDEPTSGLD 272
Cdd:COG4604 100 --RFPYSkgrLTAEDR-EIIDEAIAYLDLEDLADRYL------DELSGGQRQR-AFIAMVLaqdTDYVLL--DEPLNNLD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136592 273 sfTAHSV--VQVLKKLS-QKGKTVILTIHqpsselfEL-F-----DKILLMAEGRVAFLGTPSE 327
Cdd:COG4604 168 --MKHSVqmMKLLRRLAdELGKTVVIVLH-------DInFascyaDHIVAMKDGRVVAQGTPEE 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
127-319 |
8.31e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.29 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 127 AVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQP-VDAKEM------QARCAYVQQDdlfigsltARehlIFQAM 199
Cdd:PRK11144 28 AIFGRSGAGKTSLINAIS-----GLTRPQKGRIVLNGRVlFDAEKGiclppeKRRIGYVFQD--------AR---LFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 200 vRMPRHLTY---RQRVARVDQVIQELSLskcQHTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTA 276
Cdd:PRK11144 92 -KVRGNLRYgmaKSMVAQFDKIVALLGI---EPLLDRYPGS---LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17136592 277 HSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRV 319
Cdd:PRK11144 165 RELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
110-327 |
8.61e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 70.63 E-value: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQpvdakemqarcayvqqdDLFIGSLT 189
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLA-----GFEQPTAGQIMLDGV-----------------DLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 190 ARE-HLIFQAMVRMPrHLTYRQRVAR------------VDQVIQELSLSKCQHTIIGVPGRvkgLSGGERKRLAFASEAL 256
Cdd:PRK11607 90 QRPiNMMFQSYALFP-HMTVEQNIAFglkqdklpkaeiASRVNEMLGLVHMQEFAKRKPHQ---LSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 257 TDPPLLICDEPTSGLDS----FTAHSVVQVLKKLsqkGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKklrdRMQLEVVDILERV---GVTCVMVTHD-QEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
113-299 |
8.79e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.50 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNAL-AFRSPQGIQVSPSGMRLLNGQPVDAKEMQARCAYV----QQDDLFiGS 187
Cdd:COG4161 18 LFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPDSGQLNIAGHQFDFSQKPSEKAIRLLRQKVgmvfQQYNLW-PH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 LTAREHLIfQAMVRMPRhLTYRQRVARVDQVIQELSLSKCQHTIigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEP 267
Cdd:COG4161 97 LTVMENLI-EAPCKVLG-LSKEQAREKAMKLLARLRLTDKADRF---PLH---LSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190
....*....|....*....|....*....|..
gi 17136592 268 TSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQ 299
Cdd:COG4161 169 TAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
123-329 |
8.90e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.69 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQAR--CAYVQQDDLFIGSLTAREHLIFQAmv 200
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKMLT-----GLLPASEGEAWLFGQPVDAGDIATRrrVGYMSQAFSLYGELTVRQNLELHA-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 201 rmpR--HLTYRQRVARVDQVIQELSLSKCQHTiigVPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLD-----S 273
Cdd:NF033858 365 ---RlfHLPAAEIAARVAEMLERFDLADVADA---LPDS---LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvardM 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136592 274 FTahsvvQVLKKLS-QKGKTVILTIHqpsselF----ELFDKILLMAEGRVAFLGTPSEAV 329
Cdd:NF033858 436 FW-----RLLIELSrEDGVTIFISTH------FmneaERCDRISLMHAGRVLASDTPAALV 485
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
241-327 |
1.47e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.54 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGK-TVILTIHqpSSE-LFELFDKILLMAEGR 318
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSH--SMEdVAKLADRIIVMNKGK 222
|
....*....
gi 17136592 319 VAFLGTPSE 327
Cdd:PRK13637 223 CELQGTPRE 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
110-272 |
2.03e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQGIQVSPSGmrllngqpvdakemQARCAYVQQDDLFIGSL 188
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgELEPDSGEVSIPK--------------GLRIGYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHLI-------------FQAMVRMPRHLTYRQRVA----------------RVDQVIQELSLSKCQHTiigvpGRVK 239
Cdd:COG0488 77 TVLDTVLdgdaelraleaelEELEAKLAEPDEDLERLAelqeefealggweaeaRAEEILSGLGFPEEDLD-----RPVS 151
|
170 180 190
....*....|....*....|....*....|...
gi 17136592 240 GLSGGERKRLAFASEALTDPPLLICDEPTSGLD 272
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
103-319 |
2.04e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 103 RHIPA-----PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALaFRSPQGiqvSPSGMRLLNGQPVD----AKEMQA 173
Cdd:PRK13549 263 RNLTAwdpvnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCL-FGAYPG---RWEGEIFIDGKPVKirnpQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 174 RCAYVQQD--------DLFIG---SLTAREHLIFQAMVRMPRHLTYrqrvarVDQVIQELSLsKCQHTIIgvpgRVKGLS 242
Cdd:PRK13549 339 GIAMVPEDrkrdgivpVMGVGkniTLAALDRFTGGSRIDDAAELKT------ILESIQRLKV-KTASPEL----AIARLS 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 243 GGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTihqpSSELFE---LFDKILLMAEGRV 319
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI----SSELPEvlgLSDRVLVMHEGKL 483
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
113-319 |
2.07e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.05 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV------DAKEmqARCAYVQQDDLFIG 186
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILS-----GVYQPDSGEILLDGEPVrfrsprDAQA--AGIAIIHQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 SLTAREHlIFqaMVRMPRH---LTYRQRVARVDQVIQELSLSkcqhtiIGVPGRVKGLSGGERKRLAFASEALTDPPLLI 263
Cdd:COG1129 93 NLSVAEN-IF--LGREPRRgglIDWRAMRRRARELLARLGLD------IDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 264 CDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRV 319
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHR-LDEVFEIADRVTVLRDGRL 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
113-327 |
3.54e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 69.28 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGqpVDAKE-----MQARCAYV-QQDDLFI 185
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTrFYDID------EGEILLDG--HDLRDytlasLRNQVALVsQNVHLFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 GSLT-----------AREHLIFQAmvrmprhltyrqRVARVDQVIQELSlsKCQHTIIGVPGRVkgLSGGERKRLAFASE 254
Cdd:PRK11176 431 DTIAnniayarteqySREQIEEAA------------RMAYAMDFINKMD--NGLDTVIGENGVL--LSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 255 ALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLsQKGKTVILTIHQPSSelFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEKADEILVVEDGEIVERGTHAE 564
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
123-329 |
5.97e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQ------PVDA--KEMqarcAYV---QQDDLFIGSLTAR 191
Cdd:PRK09700 289 GEILGFAGLVGSGRTELMNCLF-----GVDKRAGGEIRLNGKdisprsPLDAvkKGM----AYItesRRDNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 192 EHLIFQAMVRMPRH-----LTYRQRVARVDQVIQELSLSKCqHTIigvPGRVKGLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:PRK09700 360 QNMAISRSLKDGGYkgamgLFHEVDEQRTAENQRELLALKC-HSV---NQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRVAFLGTPSEAV 329
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGRLTQILTNRDDM 497
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
121-319 |
7.27e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 121 YPGELLAVMGSSGAGKTTLLNALAFR-SPQGIQVSpsgMRLLNGQPVDAKEM-QAR--------CAYVQQD--DLFIGSL 188
Cdd:PRK11701 30 YPGEVLGIVGESGSGKTTLLNALSARlAPDAGEVH---YRMRDGQLRDLYALsEAErrrllrteWGFVHQHprDGLRMQV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHLIFQAMVRMPRHltYRQrvarvdqvIQELSLSKCQHTIIGvPGRVKGL----SGGERKRLAFASEALTDPPLLIC 264
Cdd:PRK11701 107 SAGGNIGERLMAVGARH--YGD--------IRATAGDWLERVEID-AARIDDLpttfSGGMQQRLQIARNLVTHPRLVFM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136592 265 DEPTSGLDsftahsvVQVLKKL--------SQKGKTVILTIHQPS-SELfeLFDKILLMAEGRV 319
Cdd:PRK11701 176 DEPTGGLD-------VSVQARLldllrglvRELGLAVVIVTHDLAvARL--LAHRLLVMKQGRV 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
104-319 |
7.86e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.85 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 104 HIPAprkhllknvcgvaypGELLAVMGSSGAGKTTLLNALAfrspqGIQvSPSGMRLLNGQpvdAKEMQARcayvqqDDL 183
Cdd:PRK11247 34 HIPA---------------GQFVAVVGRSGCGKSTLLRLLA-----GLE-TPSAGELLAGT---APLAEAR------EDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 figsltareHLIFQAmvrmPRHLTYRQRVARV---------DQVIQELSlskcqhtIIGVPGRVK----GLSGGERKRLA 250
Cdd:PRK11247 84 ---------RLMFQD----ARLLPWKKVIDNVglglkgqwrDAALQALA-------AVGLADRANewpaALSGGQKQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 251 FASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRV 319
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHD-VSEAVAMADRVLLIEEGKI 212
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
110-326 |
8.66e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.47 E-value: 8.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGI---QVSpSGMRLLNGQPVDAKEMQARcayvqqddlfig 186
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM-----GHpkyEVT-SGSILLDGEDILELSPDER------------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 sltARE--HLIFQAMVRMPrHLTYRQ--RVARVDQVIQELSLSKCQHTIIGVPGRVK------------GLSGGERKRLA 250
Cdd:COG0396 75 ---ARAgiFLAFQYPVEIP-GVSVSNflRTALNARRGEELSAREFLKLLKEKMKELGldedfldryvneGFSGGEKKRNE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 251 FASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPssELFELF--DKILLMAEGRVAFLGTPS 326
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGRIVKSGGKE 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
121-295 |
9.51e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 9.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 121 YPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV------DAkeMQARCAYVQQDDLFIGSLTAREHL 194
Cdd:COG3845 29 RPGEIHALLGENGAGKSTLMKILY-----GLYQPDSGEILIDGKPVrirsprDA--IALGIGMVHQHFMLVPNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 195 IFQAMVRMPRHLTYRQRVARVDQVIQELSLSkcqhtiigVP--GRVKGLSGGERKRLafasE---AL-TDPPLLICDEPT 268
Cdd:COG3845 102 VLGLEPTKGGRLDRKAARARIRELSERYGLD--------VDpdAKVEDLSVGEQQRV----EilkALyRGARILILDEPT 169
|
170 180 190
....*....|....*....|....*....|
gi 17136592 269 SGLdsfT---AHSVVQVLKKLSQKGKTVIL 295
Cdd:COG3845 170 AVL---TpqeADELFEILRRLAAEGKSIIF 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
111-330 |
1.28e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 65.53 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 111 HLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALafrspQGIQVSPSGMRLLNGQPVDA---KEMQARCAYVQQD-DLFIG 186
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHL-----NGIYLPQRGRVKVMGREVNAeneKWVRSKVGLVFQDpDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 SLTAREHLIFQamvrmPRHLTYRQR--VARVDQVIQELSLSKCQHTiigVPGRvkgLSGGERKRLAFASEALTDPPLLIC 264
Cdd:PRK13647 94 SSTVWDDVAFG-----PVNMGLDKDevERRVEEALKAVRMWDFRDK---PPYH---LSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELfELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
123-327 |
1.49e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.51 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARcaYVqqddlfigsltareHLIFQAMVRM 202
Cdd:PRK09452 40 GEFLTLLGPSGCGKTTVLRLIA-----GFETPDSGRIMLDGQDITHVPAENR--HV--------------NTVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 203 PrHLTYRQRVA---RVDQV----IQE-----LSLSKCQHTIigvPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSG 270
Cdd:PRK09452 99 P-HMTVFENVAfglRMQKTpaaeITPrvmeaLRMVQLEEFA---QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 271 LDsFTAHSVVQV-LKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK09452 175 LD-YKLRKQMQNeLKALQRKlGITFVFVTHD-QEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
122-319 |
2.51e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTtlLNALafrspqgiqvspSGMRLLNGQPVdakemqarcAYVQQDDLFIGS--LTAREH------ 193
Cdd:PRK15134 34 AGETLALVGESGSGKS--VTAL------------SILRLLPSPPV---------VYPSGDIRFHGEslLHASEQtlrgvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 194 -----LIFQ-AMVRM-PRHlTYRQRVARVdqviqeLSLSK------CQHTIIGVPGRV-------------KGLSGGERK 247
Cdd:PRK15134 91 gnkiaMIFQePMVSLnPLH-TLEKQLYEV------LSLHRgmrreaARGEILNCLDRVgirqaakrltdypHQLSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 248 RLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRV 319
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
123-327 |
4.47e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAFRSPQGIQVSpsgmrllngqpVDakeMQARCAYVQQDDlFIGSLTAREHLIFQAMVRM 202
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGELSHAETSS-----------VV---IRGSVAYVPQVS-WIFNATVRENILFGSDFES 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 203 PRHLtyrqrvarvdqviQELSLSKCQHTIIGVPGRVK--------GLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 274
Cdd:PLN03232 708 ERYW-------------RAIDVTALQHDLDLLPGRDLteigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17136592 275 TAHSVVQVLKKLSQKGKTVILTIHQpsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PLN03232 775 VAHQVFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEGMIKEEGTFAE 825
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
123-353 |
4.93e-11 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.05 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTT---LLNALafrspqgiqVSPS-GMRLLNGQPVdAKEMQARCAYVQQDDLfigsltareHLIFQA 198
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTmvrLLNRL---------IEPTrGQVLIDGVDI-AKISDAELREVRRKKI---------AMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 MVRMPrHLTYRQRVA------------RVDQVIQELSLSKCQHTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:PRK10070 115 FALMP-HMTVLDNTAfgmelaginaeeRREKALDALRQVGLENYAHSYPDE---LSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPSEAVDffsyvgaqcptnyNPA 346
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN-------------NPA 257
|
....*..
gi 17136592 347 DFYVQVL 353
Cdd:PRK10070 258 NDYVRTF 264
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
123-302 |
5.05e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALafrspQGIQVSPSGMRLLNGQPVDAKEMQARCAYVQQDDLFIGSLTarehLIFQAMVRM 202
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKAL-----MGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFP----VLVEDVVMM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 203 PR--HLTYRQRV-----ARVDQVIQELSLSKCQHTIIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFT 275
Cdd:PRK15056 104 GRygHMGWLRRAkkrdrQIVTAALARVDMVEFRHRQIG------ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|....*..
gi 17136592 276 AHSVVQVLKKLSQKGKTVILTIHQPSS 302
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGS 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
110-331 |
5.97e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALafrspqgiqvspsgmrlLNGQPVDAKEMQAR--CAYVQQDdLFIGS 187
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL-----------------LSQFEISEGRVWAErsIAYVPQQ-AWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 LTAREHLIFQAMVRMPRhltyRQRVARVDQVIQEL-SLSKCQHTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:PTZ00243 735 ATVRGNILFFDEEDAAR----LADAVRVSQLEADLaQLGGGLETEIGEKG--VNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpsSELFELFDKILLMAEGRVAFLGtpsEAVDF 331
Cdd:PTZ00243 809 PLSALDAHVGERVVEECFLGALAGKTRVLATHQ--VHVVPRADYVVALGDGRVEFSG---SSADF 868
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
66-327 |
6.30e-11 |
|
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: 66.09 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 66 ENLTYAWHNM--DIFGAVNQPGSGwRQLVNRTRGLF-CNERHIPAPrkhLLKNVCGVAYPGELLAVMGSSGAGKTTLLNa 142
Cdd:TIGR01271 396 VNVTASWDEGigELFEKIKQNNKA-RKQPNGDDGLFfSNFSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLM- 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 143 lafrspqgiqvspsgMRLLNGQPVDAK-EMQARCAYVQQDDlFIGSLTAREHLIFQAmvrmpRHLTYRQR-VARVDQVIQ 220
Cdd:TIGR01271 471 ---------------MIMGELEPSEGKiKHSGRISFSPQTS-WIMPGTIKDNIIFGL-----SYDEYRYTsVIKACQLEE 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 221 ELSLSKCQHTIIGVPGRVKgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQ--VLKKLSQKGKTVILTih 298
Cdd:TIGR01271 530 DIALFPEKDKTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEscLCKLMSNKTRILVTS-- 606
|
250 260
....*....|....*....|....*....
gi 17136592 299 qpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:TIGR01271 607 --KLEHLKKADKILLLHEGVCYFYGTFSE 633
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
96-329 |
6.58e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.22 E-value: 6.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 96 RGLFCNERhipaprkhLLKNVCGVAY---PGELLAVMGSSGAGKTTLLNALAFrspqgIQVSPSGMRLLNGQPV---DAK 169
Cdd:PRK11308 19 RGLFKPER--------LVKALDGVSFtleRGKTLAVVGESGCGKSTLARLLTM-----IETPTGGELYYQGQDLlkaDPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 170 EMQARCAYVQ---QDDLfiGSLTAREHL--IFQAMVRMPRHLTYRQRVARVDQVIQELSLsKCQHTiigvpGRVKGL-SG 243
Cdd:PRK11308 86 AQKLLRQKIQivfQNPY--GSLNPRKKVgqILEEPLLINTSLSAAERREKALAMMAKVGL-RPEHY-----DRYPHMfSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 244 GERKRLAFASEALTDPPLLICDEPTSGLD-SFTAHsVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFL 322
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDvSVQAQ-VLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEK 236
|
....*..
gi 17136592 323 GtPSEAV 329
Cdd:PRK11308 237 G-TKEQI 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
66-327 |
7.77e-11 |
|
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: 63.34 E-value: 7.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 66 ENLTYAWHNM--DIFGAVNQPGSGWRQLVNRTRGLFCNERHIPAPrkhLLKNVCGVAYPGELLAVMGSSGAGKTTLLNA- 142
Cdd:cd03291 7 ENVTAFWDEGfgELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAP---VLKNINLKIEKGEMLAITGSTGSGKTSLLMLi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 143 LAFRSPQGIQVSPSGmrllngqpvdakemqaRCAYVQQDDlFIGSLTAREHLIFQAMVRMPRHLTyrqrVARVDQVIQEL 222
Cdd:cd03291 84 LGELEPSEGKIKHSG----------------RISFSSQFS-WIMPGTIKENIIFGVSYDEYRYKS----VVKACQLEEDI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 223 S-LSKCQHTIIGVPGRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQ--VLKKLSQkgKTVILTIHQ 299
Cdd:cd03291 143 TkFPEKDNTVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEscVCKLMAN--KTRILVTSK 218
|
250 260
....*....|....*....|....*...
gi 17136592 300 psSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:cd03291 219 --MEHLKKADKILILHEGSSYFYGTFSE 244
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
122-327 |
1.11e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAFRSPQgiqvspSGMRLLNGQPV---DAKEMQARCAYV--QQDDLFIGSltarehlIF 196
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAGLLPG------SGSIQFAGQPLeawSAAELARHRAYLsqQQTPPFAMP-------VF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 197 QAMVR-MPRHLTYRQRVARVDQVIQELSLSKCQHTIIGvpgrvkGLSGGE--RKRLAFA-----SEALTDPPLLICDEPT 268
Cdd:PRK03695 88 QYLTLhQPDKTRTEAVASALNEVAEALGLDDKLGRSVN------QLSGGEwqRVRLAAVvlqvwPDINPAGQLLLLDEPM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 269 SGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELfDKILLMAEGRVAFLGTPSE 327
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQGKLLASGRRDE 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
241-327 |
1.21e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLS-QKGKTVILTIHQpSSELFELFDKILLMAEGRV 319
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHD-MNEVARYADEVIVMKEGSI 224
|
....*...
gi 17136592 320 AFLGTPSE 327
Cdd:PRK13646 225 VSQTSPKE 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
121-320 |
1.32e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 121 YPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCA----YV----QQDDLF-------- 184
Cdd:PRK15439 287 RAGEILGLAGVVGAGRTELAETLY-----GLRPARGGRIMLNGKEINALSTAQRLArglvYLpedrQSSGLYldaplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSLTARehlifqamvRMPRHLTYRQRVARVDQVIQELSLsKCQHtiigVPGRVKGLSGGERKRLAFASEALTDPPLLIC 264
Cdd:PRK15439 362 VCALTHN---------RRGFWIKPARENAVLERYRRALNI-KFNH----AEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTihqpSSELFE---LFDKILLMAEGRVA 320
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGEIS 482
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
123-327 |
1.46e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.20 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQAR--CAYVQQDDLF----IGsltarEHLIF 196
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVA-----GLEKPTEGQIFIDGEDVTHRSIQQRdiCMVFQSYALFphmsLG-----ENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 197 Q-AMVRMPRhltyRQRVARVDQVIQELSLSkcqhtiiGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSF 274
Cdd:PRK11432 102 GlKMLGVPK----EERKQRVKEALELVDLA-------GFEDRyVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17136592 275 TAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK11432 171 LRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
110-327 |
1.64e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGiQVSP-SGMRLLnGQPVdakemqaRCAYVQQD-DLFIGS 187
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA-----G-ELEPdSGTVKL-GETV-------KIGYFDQHqEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 LTAREHLIfQAMVRM-PRHLtyRQRVARV----DQviqelslskcQHTIIGVpgrvkgLSGGERKRLAFASEALTDPPLL 262
Cdd:COG0488 394 KTVLDELR-DGAPGGtEQEV--RGYLGRFlfsgDD----------AFKPVGV------LSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 263 ICDEPTSGLDSFTAHSVVQVLKKLsqKGkTVILTIHQPSselF--ELFDKILLMAEGRV-AFLGTPSE 327
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRY---FldRVATRILEFEDGGVrEYPGGYDD 516
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
109-300 |
1.93e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqgiqvspsgmRLLNGQPVdakemqARCAYVQQDDLfigsl 188
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA--------------GALKGTPV------AGCVDVPDNQF----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 tarehlifqamvrmPRHLTYRQRVAR---VDQVIQELSLSKcqhtIIGVP---GRVKGLSGGERKRLAFASEALTDPPLL 262
Cdd:COG2401 97 --------------GREASLIDAIGRkgdFKDAVELLNAVG----LSDAVlwlRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 17136592 263 ICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQP 300
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHY 197
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
238-312 |
2.17e-10 |
|
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: 59.68 E-value: 2.17e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 238 VKGLSGGERKR----LAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPssELFELFDKIL 312
Cdd:cd03227 75 RLQLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLI 151
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
122-328 |
2.21e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGI------QVS-PSGMRLLngqpvdakemqarcaYV-QQDDLFIGSLtaREH 193
Cdd:COG4178 388 PGERLLITGPSGSGKSTLLRAIA-----GLwpygsgRIArPAGARVL---------------FLpQRPYLPLGTL--REA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 194 LIF-------------QAM--VRMPRHLTYRQRVARVDQViqelslskcqhtiigvpgrvkgLSGGERKRLAFASEALTD 258
Cdd:COG4178 446 LLYpataeafsdaelrEALeaVGLGHLAERLDEEADWDQV----------------------LSLGEQQRLAFARLLLHK 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKlSQKGKTVILTIHQPSseLFELFDKIL-LMAEGRVAFLGTPSEA 328
Cdd:COG4178 504 PDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRST--LAAFHDRVLeLTGDGSWQLLPAEAPA 571
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
113-327 |
2.58e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 62.42 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVA---YPGELLAVMGSSGAGKTTLLNALA--FRSPQGiQVSPSGMRLLNGQPVDAKEMQARCAYVQQDDLF--- 184
Cdd:PRK15079 34 LKAVDGVTlrlYEGETLGVVGESGCGKSTFARAIIglVKATDG-EVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLAsln 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 ----IGSLTAREHLIFQAmvrmprHLTYRQRVARVDQVIQELSLskcqhtiigVPGRVK----GLSGGERKRLAFASEAL 256
Cdd:PRK15079 113 prmtIGEIIAEPLRTYHP------KLSRQEVKDRVKAMMLKVGL---------LPNLINryphEFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 257 TDPPLLICDEPTSGLDSFTAHSVVQVLKKLsQK--GKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQL-QRemGLSLIFIAHDLAV-VKHISDRVLVMYLGHAVELGTYDE 248
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
113-318 |
2.87e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 63.31 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGiqvSPSGMRLLNGQPVDAKEM----QARCAYVQQDDLFIGSL 188
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG---TWDGEIYWSGSPLKASNIrdteRAGIVIIHQELTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHLIFQAMVRMPRHLT-YRQRVARVDQVIQELSLSkcqhtIIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEP 267
Cdd:TIGR02633 94 SVAENIFLGNEITLPGGRMaYNAMYLRAKNLLRELQLD-----ADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17136592 268 TSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGR 318
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAHGVACVYISHK-LNEVKAVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
241-332 |
3.30e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVA 320
Cdd:PRK13643 145 LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHII 223
|
90
....*....|....*
gi 17136592 321 FLGTPSEA---VDFF 332
Cdd:PRK13643 224 SCGTPSDVfqeVDFL 238
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
122-327 |
3.32e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.56 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTL-LNALAFRSPQgiqvspSGMRLLNGQPVDAKE-----MQARCAYVQQDDlfigsltarEHLI 195
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLfMNLSGLLRPQ------KGAVLWQGKPLDYSKrgllaLRQQVATVFQDP---------EQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 196 FQAMVRMPRHLTYR------QRVARvdQVIQELSLSKCQHtIIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPTS 269
Cdd:PRK13638 91 FYTDIDSDIAFSLRnlgvpeAEITR--RVDEALTLVDAQH-FRHQP--IQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 270 GLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSeLFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGAPGE 222
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
112-299 |
3.62e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDakemQARCAYvQQDDLFIG----- 186
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIA-----GLLNPEKGEILFERQSIK----KDLCTY-QKQLCFVGhrsgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 --SLTAREHLIFQamvrmprhLTYRQRVARVDQVIQELSLSKCQHTIIGVpgrvkgLSGGERKRLAFASEALTDPPLLIC 264
Cdd:PRK13540 86 npYLTLRENCLYD--------IHFSPGAVGITELCRLFSLEHLIDYPCGL------LSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQ 299
Cdd:PRK13540 152 DEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
116-327 |
4.24e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.77 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 116 VCGVA---YPGELLAVMGSSGAGKTTLLNALA-FRSPQGiqvspsGMRLLNGQPVDAKEMQ--ARCAYV---QQDDLFiG 186
Cdd:PRK11300 21 VNNVNlevREQEIVSLIGPNGAGKTTVFNCLTgFYKPTG------GTILLRGQHIEGLPGHqiARMGVVrtfQHVRLF-R 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 SLTAREHLifqaMVRMPRHL------------TYRQR----VARVDQVIQELSLSKCQHtiigvpgRVKG-LSGGERKRL 249
Cdd:PRK11300 94 EMTVIENL----LVAQHQQLktglfsgllktpAFRRAeseaLDRAATWLERVGLLEHAN-------RQAGnLAYGQQRRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 250 AFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
123-327 |
4.26e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.97 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQpvdakemqaRCAYVQQDDLFIGsltarehLIFQAMVRM 202
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIA-----GLEDITSGDLFIGEK---------RMNDVPPAERGVG-------MVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 203 PrHLTY---------------RQRVARVDQVIQELSLSkcqHTIIGVPgrvKGLSGGERKRLAFASEALTDPPLLICDEP 267
Cdd:PRK11000 88 P-HLSVaenmsfglklagakkEEINQRVNQVAEVLQLA---HLLDRKP---KALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136592 268 TSGLDSFTAhsvVQV---LKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK11000 161 LSNLDAALR---VQMrieISRLHKRlGRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
228-320 |
4.56e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 228 QHTIIGvpgrvkGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTihqpSSELFEL 307
Cdd:PRK10982 385 HRTQIG------SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII----SSEMPEL 454
|
90
....*....|....*.
gi 17136592 308 F---DKILLMAEGRVA 320
Cdd:PRK10982 455 LgitDRILVMSNGLVA 470
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
113-323 |
4.61e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAK----EMQARCAYVQQDDLFIGSL 188
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLT-----GIYTRDAGSILYLGKEVTFNgpksSQEAGIGIIHQELNLIPQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHlIFqaMVRMPRH----LTYRQRVARVDQVIQELSLSKCQHTIIGvpgrvkGLSGGER------KRLAFASEaltd 258
Cdd:PRK10762 95 TIAEN-IF--LGREFVNrfgrIDWKKMYAEADKLLARLNLRFSSDKLVG------ELSIGEQqmveiaKVLSFESK---- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 259 ppLLICDEPTSGL-DSFTAhSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRvaFLG 323
Cdd:PRK10762 162 --VIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVYISHR-LKEIFEICDDVTVFRDGQ--FIA 221
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
506-617 |
6.33e-10 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 59.44 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 506 YFLGKTIAELPLFLTVPLVFTAIAYPMIGLRAGVLHFFNCLALVTLVANVSTSFGYLISCASSSTSMALSVGPPVIIPFL 585
Cdd:COG0842 48 ILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLT 127
|
90 100 110
....*....|....*....|....*....|..
gi 17136592 586 LFGGFFLNSGSVPVYLKWLSYLSWFRYANEGL 617
Cdd:COG0842 128 FLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
240-298 |
6.96e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.87 E-value: 6.96e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 240 GLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIH 298
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
110-327 |
7.23e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.52 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLnalafRSPQGIQVSPSGMRLLNGQPVDAK---EMQARCAYVQQ--DDLF 184
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTV-----RLIDGLLEAESGQIIIDGDLLTEEnvwDIRHKIGMVFQnpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSlTAREHLIFQAmvrMPRHLTYRQRVARVDQVIQELSLSKCQHTiigVPGRvkgLSGGERKRLAFASEALTDPPLLIC 264
Cdd:PRK13650 95 VGA-TVEDDVAFGL---ENKGIPHEEMKERVNEALELVGMQDFKER---EPAR---LSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHqpssELFE--LFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDyQMTVISITH----DLDEvaLSDRVLVMKNGQVESTSTPRE 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
110-324 |
1.08e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.66 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALafrspQGIQVSPSGMRLLNGQPVDAKEMQA---RCAYVQQDDLFIG 186
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL-----MGYYPLTEGEIRLDGRPLSSLSHSVlrqGVAMVQQDPVVLA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 SltarehlIFQAMVRMPRHLTyRQRVARVDQVIQ--EL--SLSKCQHTIIGVPGrvKGLSGGERKRLAFASEALTDPPLL 262
Cdd:PRK10790 429 D-------TFLANVTLGRDIS-EEQVWQALETVQlaELarSLPDGLYTPLGEQG--NNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 263 ICDEPTSGLDSFTAHSVVQVLKKLSQkgKTVILTIHQPSSELFELfDKILLMAEGRVAFLGT 324
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEA-DTILVLHRGQAVEQGT 557
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
123-330 |
1.12e-09 |
|
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: 61.89 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAfrspqgiqvspSGMRLLNGQpvdaKEMQARCAYVQQDdLFIGSLTAREHLIFQAMVRM 202
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALL-----------AEMDKVEGH----VHMKGSVAYVPQQ-AWIQNDSLRENILFGKALNE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 203 PRHltyrQRVARVDQVIQELS-LSKCQHTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQ 281
Cdd:TIGR00957 728 KYY----QQVLEACALLPDLEiLPSGDRTEIGEKG--VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17136592 282 --VLKKLSQKGKTVILTIHQPSseLFELFDKILLMAEGRVAFLGTPSEAVD 330
Cdd:TIGR00957 802 hvIGPEGVLKNKTRILVTHGIS--YLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
241-327 |
1.14e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 60.03 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQ-KGKTVILTIHQpSSELFELFDKILLMAEGRV 319
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHS-MEDAARYADQIVVMHKGTV 224
|
....*...
gi 17136592 320 AFLGTPSE 327
Cdd:PRK13634 225 FLQGTPRE 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
109-296 |
1.32e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.40 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGIQVSPSGMRLLNGQPV-----DAKEMQARCAYV-QQDD 182
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIysprtDTVDLRKEIGMVfQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 183 LFIGSltarehlIFQAMVRMPRHLTYRQRvARVDQVIqELSLSKCqhtiiGVPGRVK--------GLSGGERKRLAFASE 254
Cdd:PRK14239 97 PFPMS-------IYENVVYGLRLKGIKDK-QVLDEAV-EKSLKGA-----SIWDEVKdrlhdsalGLSGGQQQRVCIARV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17136592 255 ALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILT 296
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
187-337 |
1.43e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 SLTAREHLIfqaMVRMPRHLTYRQRVARVDQVIQELSLSKcqhtiigVPGRVKG-LSGGERKRLAFASEALTDPPLLICD 265
Cdd:NF000106 100 SFSGRENLY---MIGR*LDLSRKDARARADELLERFSLTE-------AAGRAAAkYSGGMRRRLDLAASMIGRPAVLYLD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 266 EPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIH------QPSSELfELFDKILLMAEGRVAFLGT----------PSEAV 329
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQymeeaeQLAHEL-TVIDRGRVIADGKVDELKTkvggrtlqirPAHAA 248
|
....*...
gi 17136592 330 DFFSYVGA 337
Cdd:NF000106 249 ELDRMVGA 256
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
122-312 |
1.65e-09 |
|
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: 57.16 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALA--FRSPQGIQVSPSGMRLLngqpvdakemqarcaYVQQDDLF-IGSLtaREHLIFqa 198
Cdd:cd03223 26 PGDRLLITGPSGTGKSSLFRALAglWPWGSGRIGMPEGEDLL---------------FLPQRPYLpLGTL--REQLIY-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 mvrmprhltyrqrvarvdqviqelslskcqhtiigvP-GRVkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAH 277
Cdd:cd03223 87 ------------------------------------PwDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180 190
....*....|....*....|....*....|....*
gi 17136592 278 SVVQVLKKLsqkGKTVILTIHQPSseLFELFDKIL 312
Cdd:cd03223 129 RLYQLLKEL---GITVISVGHRPS--LWKFHDRVL 158
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
122-300 |
1.94e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.77 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspQGIQVSP----SGMRLLNGQPV---DAKEMQARCAYVQQDDLFIGSLTAREH- 193
Cdd:PRK14247 28 DNTITALMGPSGSGKSTLLRVFN----RLIELYPearvSGEVYLDGQDIfkmDVIELRRRVQMVFQIPNPIPNLSIFENv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 194 ---LIFQAMVRMPRHLTyrqrvARVDQVIQELSLSKCQHTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSG 270
Cdd:PRK14247 104 algLKLNRLVKSKKELQ-----ERVRWALEKAQLWDEVKDRLDAPA--GKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190
....*....|....*....|....*....|
gi 17136592 271 LDSFTAHSVVQVLKKLsQKGKTVILTIHQP 300
Cdd:PRK14247 177 LDPENTAKIESLFLEL-KKDMTIVLVTHFP 205
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
109-327 |
1.95e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.33 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTL---LNALAFrsPQGIQVSPSGMRLLNGQpvDAKEMQARCAYV-QQDDLF 184
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLI--PSEGKVYVDGLDTSDEE--NLWDIRNKAGMVfQNPDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSLTAREHLIFQamvrmPRHLTYRQRV--ARVDQVIQELSLSKCQ----HTiigvpgrvkgLSGGERKRLAFASEALTD 258
Cdd:PRK13633 98 IVATIVEEDVAFG-----PENLGIPPEEirERVDESLKKVGMYEYRrhapHL----------LSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELfDKILLMAEGRVAFLGTPSE 327
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHY-MEEAVEA-DRIIVMDSGKVVMEGTPKE 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
110-298 |
1.95e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 56.30 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSP--QGIQVSPSGMRLlngqpvdakemqarcAYVQQddlfigs 187
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEpdEGIVTWGSTVKI---------------GYFEQ------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 ltarehlifqamvrmprhltyrqrvarvdqviqelslskcqhtiigvpgrvkgLSGGERKRLAFASEALTDPPLLICDEP 267
Cdd:cd03221 71 -----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|.
gi 17136592 268 TSGLDSFTAHSVVQVLKKLSQkgkTVILTIH 298
Cdd:cd03221 98 TNHLDLESIEALEEALKEYPG---TVILVSH 125
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
122-272 |
2.23e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQARCAYVQQDDLFIGSLTAREHLIFQAMV- 200
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLA-----GLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLh 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 201 -----RMPRHLTyrqrvarvdqviqelslskcqhTIIGVPGR----VKGLSGGERKRLAFASEALTDPPLLICDEPTSGL 271
Cdd:PRK13543 111 grrakQMPGSAL----------------------AIVGLAGYedtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
.
gi 17136592 272 D 272
Cdd:PRK13543 169 D 169
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
110-327 |
2.88e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.52 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspQGIQVSPSGMRllngqpVDAKEMqarcaYVQQDDLFIGSLT 189
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLN----RLIEIYDSKIK------VDGKVL-----YFGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 190 AREH--LIFQAMVRMPrHLTYRQRVAR----------------VDQVIQELSLSKCQHTIIGVPGrvKGLSGGERKRLAF 251
Cdd:PRK14246 88 LRKEvgMVFQQPNPFP-HLSIYDNIAYplkshgikekreikkiVEECLRKVGLWKEVYDRLNSPA--SQLSGGQQQRLTI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 252 ASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLsQKGKTVILTIHQPsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK14246 165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNP-QQVARVADYVAFLYNGELVEWGSSNE 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
122-299 |
3.35e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 59.04 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLL---NALAfrspqgiqvSPSGMRLL-NGQPV---DAKEM-QARcayvQQddlfIGsltareh 193
Cdd:PRK11153 30 AGEIFGVIGASGAGKSTLIrciNLLE---------RPTSGRVLvDGQDLtalSEKELrKAR----RQ----IG------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 194 LIFQ-----------AMVRMPRHL--TYRQRV-ARVDQVIQELSLSKCQHTiigVPGRvkgLSGGERKRLAFAsEAL-TD 258
Cdd:PRK11153 86 MIFQhfnllssrtvfDNVALPLELagTPKAEIkARVTELLELVGLSDKADR---YPAQ---LSGGQKQRVAIA-RALaSN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQ 299
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHE 200
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
241-375 |
3.44e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.48 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRV 319
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHN-MDQVLRIADEVIVMHEGKV 229
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 320 AFLGTPSEavdFFSYVGAQCPTNYNPADFYvQVLAVVPGREIESRDRIAKICDNFA 375
Cdd:PRK13645 230 ISIGSPFE---IFSNQELLTKIEIDPPKLY-QLMYKLKNKGIDLLNKNIRTIEEFA 281
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
122-327 |
5.92e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAFRSPQgiqvspsgmrLLNGQPVdakeMQARCAYVQQDDlFIGSLTAREHLIFQAMVR 201
Cdd:PLN03130 642 VGSLVAIVGSTGEGKTSLISAMLGELPP----------RSDASVV----IRGTVAYVPQVS-WIFNATVRDNILFGSPFD 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 202 MPRHltyrQRVARVDQVIQELS-LSKCQHTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVV 280
Cdd:PLN03130 707 PERY----ERAIDVTALQHDLDlLPGGDLTEIGERG--VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVF 780
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17136592 281 QVLKKLSQKGKTVILTIHQpsSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PLN03130 781 DKCIKDELRGKTRVLVTNQ--LHFLSQVDRIILVHEGMIKEEGTYEE 825
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
112-330 |
6.69e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.34 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGIQvspSGMRLLNGQPVDAKEMQARcayvQQDDLFIGsltar 191
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIL---EGDILFKGESILDLEPEER----AHLGIFLA----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 192 ehliFQAMVRMP-------RHLTYRQR-----VARVD-----QVIQE-LSLSKCQHTIIGvpgRV--KGLSGGERKRLAF 251
Cdd:CHL00131 90 ----FQYPIEIPgvsnadfLRLAYNSKrkfqgLPELDpleflEIINEkLKLVGMDPSFLS---RNvnEGFSGGEKKRNEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 252 ASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPssELFELF--DKILLMAEGRVAFLGTPSEAV 329
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKTGDAELAK 240
|
.
gi 17136592 330 D 330
Cdd:CHL00131 241 E 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
112-298 |
7.70e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.65 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-FRSPQgiqvspSGMRLLNGQPVDA---KEMQARCAYVQQDDLFIGS 187
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVAsLISPT------SGTLLFEGEDISTlkpEIYRQQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 lTAREHLIFQAMVR--MPRHLTYRQRVARVDqvIQELSLSKcqhtiigvpgRVKGLSGGERKRLAFASEALTDPPLLICD 265
Cdd:PRK10247 96 -TVYDNLIFPWQIRnqQPDPAIFLDDLERFA--LPDTILTK----------NIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....
gi 17136592 266 EPTSGLDSFTAHSVVQVLKKL-SQKGKTVILTIH 298
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYvREQNIAVLWVTH 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
111-364 |
9.12e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 111 HLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQ------PVDAKEMQARCAYvqQDDLF 184
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLS-----GIHEPTKGTITINNInynkldHKLAAQLGIGIIY--QELSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 185 IGSLTAREHLIfqamvrMPRHLT----------YRQRVARVDQVIQELSLSkcqhtiIGVPGRVKGLSGGERKRLAFASE 254
Cdd:PRK09700 92 IDELTVLENLY------IGRHLTkkvcgvniidWREMRVRAAMMLLRVGLK------VDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 255 ALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGrvaflgtpseavdffSY 334
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDG---------------SS 223
|
250 260 270
....*....|....*....|....*....|
gi 17136592 335 VGAQCPTNYNPADfyvqVLAVVPGREIESR 364
Cdd:PRK09700 224 VCSGMVSDVSNDD----IVRLMVGRELQNR 249
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
122-294 |
1.18e-08 |
|
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: 55.90 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALaFRSPQgiqvsPSGMRLL---NGQPVDakemqarcayvqqddlfIGSLTAREhlifqa 198
Cdd:COG4778 36 AGECVALTGPSGAGKSTLLKCI-YGNYL-----PDSGSILvrhDGGWVD-----------------LAQASPRE------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 MVRMPRH--------LTYRQRVARVDQVIQEL---------SLSKCQH--TIIGVPGRVKGL-----SGGERKRLAFASE 254
Cdd:COG4778 87 ILALRRRtigyvsqfLRVIPRVSALDVVAEPLlergvdreeARARAREllARLNLPERLWDLppatfSGGEQQRVNIARG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17136592 255 ALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVI 294
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
241-331 |
1.20e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.68 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVA 320
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHL-MDDVANYADFVYVLEKGKLV 224
|
90
....*....|....
gi 17136592 321 FLGTPSEA---VDF 331
Cdd:PRK13649 225 LSGKPKDIfqdVDF 238
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
123-327 |
1.48e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 56.76 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLL---NALAFRSPQGIQVSPSGMRLLNGQPvDAKEMQARCAYVQQ---DDLFigsltarEHLIF 196
Cdd:PRK13641 33 GSFVALVGHTGSGKSTLMqhfNALLKPSSGTITIAGYHITPETGNK-NLKKLRKKVSLVFQfpeAQLF-------ENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 197 QAMVRMPRHLTYRQRVARvDQVIQELSLskcqhtiIGVPGRVKG-----LSGGERKRLAFASEALTDPPLLICDEPTSGL 271
Cdd:PRK13641 105 KDVEFGPKNFGFSEDEAK-EKALKWLKK-------VGLSEDLISkspfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 272 DSFTAHSVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGKLIKHASPKE 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
112-329 |
1.98e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.50 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVA---YPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMR--LLNGQPVDAKEM----QARCA-YV--- 178
Cdd:TIGR03269 296 VVKAVDNVSlevKEGEIFGIVGTSGAGKTTLSKIIA-----GVLEPTSGEVnvRVGDEWVDMTKPgpdgRGRAKrYIgil 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 179 -QQDDLFIGSlTAREHLIFQAMVRMPRHLTYRQRV-----ARVDQVIQELSLSKCQHTiigvpgrvkgLSGGERKRLAFA 252
Cdd:TIGR03269 371 hQEYDLYPHR-TVLDNLTEAIGLELPDELARMKAVitlkmVGFDEEKAEEILDKYPDE----------LSEGERHRVALA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 253 SEALTDPPLLICDEPTSGLDSFTAHSVVQ-VLKKLSQKGKTVILTIHQPSSELfELFDKILLMAEGRVAFLGTPSEAV 329
Cdd:TIGR03269 440 QVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVL-DVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
122-298 |
2.16e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQpvDAKEMQAR-CAYVQQDdlfIGSLTAREHLIFQAMV 200
Cdd:PRK10908 27 PGEMAFLTGHSGAGKSTLLKLIC-----GIERPSAGKIWFSGH--DITRLKNReVPFLRRQ---IGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 201 ----RMPRHLT------YRQRV-ARVDQVIQelsLSKCQHTIIGvpgrvkgLSGGERKRLAFASEALTDPPLLICDEPTS 269
Cdd:PRK10908 97 ydnvAIPLIIAgasgddIRRRVsAALDKVGL---LDKAKNFPIQ-------LSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180
....*....|....*....|....*....
gi 17136592 270 GLDSFTAHSVVQVLKKLSQKGKTVILTIH 298
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
113-318 |
4.12e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKE-MQARCAYVQQDDLFIGSL 188
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILS-----GNYQPDAGSILIDGQEMrfaSTTAaLAAGVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHLIfqaMVRMP-RH--LTYRQRVARVDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICD 265
Cdd:PRK11288 95 TVAENLY---LGQLPhKGgiVNRRLLNYEAREQLEHLGVDIDPDT------PLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17136592 266 EPTSGLDSFTAHSVVQVLKKLSQKGKtVILTIHQPSSELFELFDKILLMAEGR 318
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGR-VILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
123-324 |
4.31e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKT-TLLNALAFRSPQGIQVSPSGM--RLLNGQPVDAKEM-QARCAYVQQDDLfigsltareHLIFQA 198
Cdd:PRK10261 42 GETLAIVGESGSGKSvTALALMRLLEQAGGLVQCDKMllRRRSRQVIELSEQsAAQMRHVRGADM---------AMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 199 -----------------MVRMPRHLTYRQRVARVDQVIQELSLSKCQHTIIGVPGRvkgLSGGERKRLAFASEALTDPPL 261
Cdd:PRK10261 113 pmtslnpvftvgeqiaeSIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ---LSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 262 LICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGT 324
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
105-317 |
4.51e-08 |
|
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: 53.48 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 105 IPAPRKHLLKNVcGVAYP-GELLAVMGSSGAGKTTLLNALAFRSPQgiqvspsgMRLLNGQPvdakemqarcAYVQQDDL 183
Cdd:cd03238 3 VSGANVHNLQNL-DVSIPlNVLVVVTGVSGSGKSTLVNEGLYASGK--------ARLISFLP----------KFSRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 FIGSLtarehlifQAMVRMprHLTYrqrvarvdqviqeLSLSKCQHTiigvpgrvkgLSGGERKRLAFASEALTDPP--L 261
Cdd:cd03238 64 FIDQL--------QFLIDV--GLGY-------------LTLGQKLST----------LSGGELQRVKLASELFSEPPgtL 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 262 LICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPssELFELFDKILLMAEG 317
Cdd:cd03238 111 FILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFGPG 164
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
123-329 |
4.78e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALA-FRSPQGIQVSPSGMRLlngQPVDAKEMQARCAYVQQDDLFIGSLTAREhliFQAMVR 201
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSrLMTPAHGHVWLDGEHI---QHYASKEVARRIGLLAQNATTPGDITVQE---LVARGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 202 MPRH-LTYRQRVARVDQVIQELSLSKCQHTiigVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVV 280
Cdd:PRK10253 107 YPHQpLFTRWRKEDEEAVTKAMQATGITHL---ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17136592 281 QVLKKLS-QKGKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSEAV 329
Cdd:PRK10253 184 ELLSELNrEKGYTLAAVLHD-LNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
215-298 |
5.22e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 56.76 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 215 VDQVIQELSLSKCQHTIIGVPgrVKGLSGGERKRLAFASEALT---DPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGK 291
Cdd:PRK00635 786 IHEKIHALCSLGLDYLPLGRP--LSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH 863
|
....*..
gi 17136592 292 TVILTIH 298
Cdd:PRK00635 864 TVVIIEH 870
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
113-325 |
5.45e-08 |
|
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: 53.57 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALaFRSPQGIqvspSGMRLLNGQ---PVDAKEMQARCAYVQQDD-LFIGSL 188
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILAL-FRFLEAE----EGKIEIDGIdisTIPLEDLRSSLTIIPQDPtLFSGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 taREHL-IFQamvrmprhlTYRQrvarvDQVIQELSLSkcqhtiigvpGRVKGLSGGERKRLAFASEALTDPPLLICDEP 267
Cdd:cd03369 99 --RSNLdPFD---------EYSD-----EEIYGALRVS----------EGGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 268 TSGLDSFTAHSVVQVLKKLSQKgkTVILTIHQPSSELFElFDKILLMAEGRVAFLGTP 325
Cdd:cd03369 153 TASIDYATDALIQKTIREEFTN--STILTIAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
123-319 |
6.19e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.32 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAFRSPQGIQVSpSGMRLLNGQPVDAKEMQAR-CAYVQQD--DLFIGSLTAREHLIfqam 199
Cdd:PRK10418 29 GRVLALVGGSGSGKSLTCAAALGILPAGVRQT-AGRVLLDGKPVAPCALRGRkIATIMQNprSAFNPLHTMHTHAR---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 200 vrmpRHLTYRQRVARVDQVIQELslskcqhTIIGV--PGRVKGL-----SGGERKRLAFASEALTDPPLLICDEPTSGLD 272
Cdd:PRK10418 104 ----ETCLALGKPADDATLTAAL-------EAVGLenAARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 17136592 273 SFTAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRV 319
Cdd:PRK10418 173 VVAQARILDLLESIVQKrALGMLLVTHD-MGVVARLADDVAVMSHGRI 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
113-318 |
9.93e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 9.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 113 LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGiqvSPSGMRLLNGQPVDAKEM----QARCAYVQQDDLFIGSL 188
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHG---TYEGEIIFEGEELQASNIrdteRAGIAIIHQELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 TAREHlIFQAMVRMPRHLT-YRQRVARVDQVIQELSLSkcqhtiIGVPGRVKGLSGGERKRLAFAsEALT-DPPLLICDE 266
Cdd:PRK13549 98 SVLEN-IFLGNEITPGGIMdYDAMYLRAQKLLAQLKLD------INPATPVGNLGLGQQQLVEIA-KALNkQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17136592 267 PTSGL-DSFTAHsVVQVLKKLSQKGKTVILTIHQpSSELFELFDKILLMAEGR 318
Cdd:PRK13549 170 PTASLtESETAV-LLDIIRDLKAHGIACIYISHK-LNEVKAISDTICVIRDGR 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
121-272 |
1.50e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.97 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 121 YPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKEMQARCAYVQ---QDDLfiGSLTAR--- 191
Cdd:COG4608 42 RRGETLGLVGESGCGKSTLGRLLL-----RLEEPTSGEILFDGQDItglSGRELRPLRRRMQmvfQDPY--ASLNPRmtv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 192 EHLIFQAMvRMPRHLTYRQRVARVDQVIQelslskcqhtiigvpgRVkGL------------SGGERKRLAFAsEAL-TD 258
Cdd:COG4608 115 GDIIAEPL-RIHGLASKAERRERVAELLE----------------LV-GLrpehadryphefSGGQRQRIGIA-RALaLN 175
|
170
....*....|....
gi 17136592 259 PPLLICDEPTSGLD 272
Cdd:COG4608 176 PKLIVCDEPVSALD 189
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
432-607 |
1.71e-07 |
|
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: 53.93 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 432 KVRLIQTTMVAILIGLIFLGQQLTQVGVMNINGAIFLFLTNMTFQNVFATINVFTSELPVFMREARSRLYRCdTYFLGKT 511
Cdd:pfam12698 132 LVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPL-QYWLGKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 512 IAELPLFLTVPLVFTAIAYpmiGLRAGVLHFFNCLALVTLVANVSTSFGYLISCASSSTSMALSVGPPVIIPFLLFGGFF 591
Cdd:pfam12698 211 LGDFLVGLLQLLIILLLLF---GIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGL 287
|
170
....*....|....*.
gi 17136592 592 LNSGSVPVYLKWLSYL 607
Cdd:pfam12698 288 FPLEDPPSFLQWIFSI 303
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
123-319 |
1.82e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAFRSpQGIQVSpsGMRLLNGQPVD----AKEMQARCAYVQQDdlfigsltaREH--LIF 196
Cdd:NF040905 286 GEIVGIAGLMGAGRTELAMSVFGRS-YGRNIS--GTVFKDGKEVDvstvSDAIDAGLAYVTED---------RKGygLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 197 QAMVRMPRHLTYRQRVAR---VDQvIQELSLS---------KCqHTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLIC 264
Cdd:NF040905 354 IDDIKRNITLANLGKVSRrgvIDE-NEEIKVAeeyrkkmniKT-PSVFQKVGN---LSGGNQQKVVLSKWLFTDPDVLIL 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTihqpSSELFELF---DKILLMAEGRV 319
Cdd:NF040905 429 DEPTRGIDVGAKYEIYTIINELAAEGKGVIVI----SSELPELLgmcDRIYVMNEGRI 482
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
108-298 |
1.96e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 108 PRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGmrllngqpvDAKEMQ-ARCAYVQQDDLFIG 186
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-----GVDKDFNG---------EARPQPgIKVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 187 SLTAREHlIFQAMVRMPRHLT--------YRQRVARVDQVIQELSlsKCQHTIIGVPG---------------------R 237
Cdd:TIGR03719 82 TKTVREN-VEEGVAEIKDALDrfneisakYAEPDADFDKLAAEQA--ELQEIIDAADAwdldsqleiamdalrcppwdaD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136592 238 VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsftAHSVVQVLKKLSQKGKTVILTIH 298
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTH 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
123-320 |
2.12e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNAL--AFRSPQGiQVSPSGMRLLNGQPVDA-------------KEMQARCAYVQqDDLFIgs 187
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLygATRRTAG-QVYLDGKPIDIRSPRDAiragimlcpedrkAEGIIPVHSVA-DNINI-- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 lTAREHLIFQAMVrmprhLTYRQRVARVDQVIQELSlskcqhtiIGVPGR---VKGLSGGERKRLAFASEALTDPPLLIC 264
Cdd:PRK11288 355 -SARRHHLRAGCL-----INNRWEAENADRFIRSLN--------IKTPSReqlIMNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTihqpSSELFE---LFDKILLMAEGRVA 320
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVAVLFV----SSDLPEvlgVADRIVVMREGRIA 475
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
101-313 |
3.82e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.88 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 101 NERHIPAPRKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALA-----------------------FRSPQGIQVSPSG 157
Cdd:PTZ00265 1172 NFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtnEQDYQGDEEQNVG 1251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 158 MRLLNGQPVDAKEMQAR------------------CAYVQQDDLFIGSLTAREHLIFQAMV----RMPRHLTYRQRVAR- 214
Cdd:PTZ00265 1252 MKNVNEFSLTKEGGSGEdstvfknsgkilldgvdiCDYNLKDLRNLFSIVSQEPMLFNMSIyeniKFGKEDATREDVKRa 1331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 215 -----VDQVIQelSLSKCQHTIIGVPGrvKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQK 289
Cdd:PTZ00265 1332 ckfaaIDEFIE--SLPNKYDTNVGPYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1407
|
250 260
....*....|....*....|....*
gi 17136592 290 GKTVILTI-HQPSSelFELFDKILL 313
Cdd:PTZ00265 1408 ADKTIITIaHRIAS--IKRSDKIVV 1430
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
127-327 |
5.84e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 127 AVMGSSGAGKTTLLNALAFRSPQGIQVSPSGMRLLNGQPV----DAKEMQARCAYV-QQDDLFIGSLTAREHLIFQAMVR 201
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIfnyrDVLEFRRRVGMLfQRPNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 202 MPRHLTYRQRVARV------DQVIQELSLSkcqhtiigvPGRvkgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFT 275
Cdd:PRK14271 131 VPRKEFRGVAQARLtevglwDAVKDRLSDS---------PFR---LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTT 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17136592 276 AHSVVQVLKKLSQKgKTVILTIHQpSSELFELFDKILLMAEGRVAFLGtPSE 327
Cdd:PRK14271 199 TEKIEEFIRSLADR-LTVIIVTHN-LAQAARISDRAALFFDGRLVEEG-PTE 247
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
123-327 |
7.85e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALafrspqGIQVSP-SGMRLLNGQPVDA------KEMQARCAYVQQDDLFIGSLTAREHLI 195
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLI------GGQIAPdHGEILFDGENIPAmsrsrlYTVRKRMSMLFQSGALFTDMNVFDNVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 196 FqamvrmprhlTYRQRVARVDQVIQELSLSKCQhtIIGVPGRVK----GLSGGERKRLAFASEALTDPPLLICDEPTSGL 271
Cdd:PRK11831 107 Y----------PLREHTQLPAPLLHSTVMMKLE--AVGLRGAAKlmpsELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 272 DSFTAHSVVQVLKKLSQK-GKTVILTIHQpSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK11831 175 DPITMGVLVKLISELNSAlGVTCVVVSHD-VPEVLSIADHAYIVADKKIVAHGSAQA 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
242-357 |
1.04e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.26 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 242 SGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAF 321
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
90 100 110
....*....|....*....|....*....|....*..
gi 17136592 322 LGTpseAVDFFsyvgaqcptnYNPADFY-VQVLAVVP 357
Cdd:PRK09473 243 YGN---ARDVF----------YQPSHPYsIGLLNAVP 266
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
109-327 |
1.07e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.56 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHL--LKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPV---DAKEMQARCAYVQQDDl 183
Cdd:PRK15112 23 RQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLA-----GMIEPTSGELLIDDHPLhfgDYSYRSQRIRMIFQDP- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 fIGSLTAREHL--IFQAMVRMPRHLTYRQRVARVDQVIQELSLskcqhtiigVPGRVK----GLSGGERKRLAFASEALT 257
Cdd:PRK15112 97 -STSLNPRQRIsqILDFPLRLNTDLEPEQREKQIIETLRQVGL---------LPDHASyyphMLAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 258 DPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK15112 167 RPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
112-272 |
1.16e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 112 LLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAfrspqgiqvspsgmrllNGQPVDAKEMQ----ARCAYVQQD--DLFI 185
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-----------------GELEPDSGTVKwsenANIGYYAQDhaYDFE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 GSLTarehlIFQAMV--RMPRHLtyrqrvarvDQVIQelslskcqhtiiGVPGR-----------VKGLSGGERKRLAFA 252
Cdd:PRK15064 397 NDLT-----LFDWMSqwRQEGDD---------EQAVR------------GTLGRllfsqddikksVKVLSGGEKGRMLFG 450
|
170 180
....*....|....*....|
gi 17136592 253 SEALTDPPLLICDEPTSGLD 272
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
241-327 |
1.61e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASE--ALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpsSELFELFDKILLMAE-- 316
Cdd:PRK00635 477 LSGGEQERTALAKHlgAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD--EQMISLADRIIDIGPga 554
|
90
....*....|....*
gi 17136592 317 ----GRVAFLGTPSE 327
Cdd:PRK00635 555 gifgGEVLFNGSPRE 569
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
123-295 |
1.81e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLNALAFRSPqgiqvspsgmrLLNGQPVDAKEMQARCAYVQQ-------------DDLFIGS-- 187
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAGELP-----------LLSGERQSQFSHITRLSFEQLqklvsdewqrnntDMLSPGEdd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 --LTAREhlIFQAMVRMPrhltyrqrvARVDQVIQELSLSKCqhtiigVPGRVKGLSGGERKRLAFASEALTDPPLLICD 265
Cdd:PRK10938 98 tgRTTAE--IIQDEVKDP---------ARCEQLAQQFGITAL------LDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190
....*....|....*....|....*....|
gi 17136592 266 EPTSGLDSFTAHSVVQVLKKLSQKGKTVIL 295
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
214-298 |
1.84e-06 |
|
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: 50.94 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 214 RVDQVIQELSLSKcqhtiigVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKT 292
Cdd:COG1245 192 KLDELAEKLGLEN-------ILDRdISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKY 264
|
....*.
gi 17136592 293 VILTIH 298
Cdd:COG1245 265 VLVVEH 270
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
109-299 |
3.28e-06 |
|
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: 49.15 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVcGVAYP-GELLAVMGSSGAGKTTLLNALAFrspqgiqvsPSGMRLLNGQPVDAKEMQA--------RCAYVQ 179
Cdd:cd03271 7 RENNLKNI-DVDIPlGVLTCVTGVSGSGKSSLINDTLY---------PALARRLHLKKEQPGNHDRieglehidKVIVID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 180 QD---------------------DLFI----GSLTAREHL----------------IFQAMVRMPRHltyrQRVARVDQV 218
Cdd:cd03271 77 QSpigrtprsnpatytgvfdeirELFCevckGKRYNRETLevrykgksiadvldmtVEEALEFFENI----PKIARKLQT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 219 IQELSLSKCQhtiIGVPGRVkgLSGGERKRLAFASEAL---TDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVIL 295
Cdd:cd03271 153 LCDVGLGYIK---LGQPATT--LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVV 227
|
....
gi 17136592 296 TIHQ 299
Cdd:cd03271 228 IEHN 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
111-329 |
5.62e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 111 HLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALaFRSPQgiqvSPSGMRLLNGQPVD---AKEMQArcayVQQDDLFI-- 185
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRAL-LRLVE----SQGGEIIFNGQRIDtlsPGKLQA----LRRDIQFIfq 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 186 ---GSLTAREHLIFQAM--VRMPRHLTYRQRVARVDQVIQELSLsKCQHTiIGVPGRvkgLSGGERKRLAFASEALTDPP 260
Cdd:PRK10261 409 dpyASLDPRQTVGDSIMepLRVHGLLPGKAAAARVAWLLERVGL-LPEHA-WRYPHE---FSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136592 261 LLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGtPSEAV 329
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG-PRRAV 551
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
122-314 |
6.29e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqgiqvspsgmRLLNgqpvdakEMQARCAYVQQDDLFIGSLTAREHlifqamvr 201
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALA--------------RELG-------PPGGGVIYIDGEDILEEVLDQLLL-------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 202 mprhltyrqrvarvdqviqelslskcqhtiIGVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQ 281
Cdd:smart00382 52 ------------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17136592 282 ------VLKKLSQKGKTVILTIHQP----SSELFELFDKILLM 314
Cdd:smart00382 102 leelrlLLLLKSEKNLTVILTTNDEkdlgPALLRRRFDRRIVL 144
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
109-272 |
8.12e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.80 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 109 RKHLLKNVCGVAYPGELLAVMGSSGAGKTTLLnalafRSPQGIqVSPSGMRLLngqpvdaKEMQARCAYVQQddlfigsl 188
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLV-----RVVLGL-VAPDEGVIK-------RNGKLRIGYVPQ-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 189 taREHLIFQAMVRMPRHLTYRQRVARVDqVIQELSLSKCQHtIIGVPgrVKGLSGGERKRLAFASEALTDPPLLICDEPT 268
Cdd:PRK09544 75 --KLYLDTTLPLTVNRFLRLRPGTKKED-ILPALKRVQAGH-LIDAP--MQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
....
gi 17136592 269 SGLD 272
Cdd:PRK09544 149 QGVD 152
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
122-328 |
9.86e-06 |
|
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: 48.64 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKTTLLNALAfrspqGIQVSPSGMRLLNGQPVDAKEMQarcAYVQQ-----DD--LFigsltarEHL 194
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLT-----GLYRPESGEILLDGQPVTADNRE---AYRQLfsavfSDfhLF-------DRL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 195 IfqamvrmprHLTYRQRVARVDQVIQELSLskcQHTIigvpgRVKG-------LSGGERKRLAFASEALTDPPLLICDE- 266
Cdd:COG4615 422 L---------GLDGEADPARARELLERLEL---DHKV-----SVEDgrfsttdLSQGQRKRLALLVALLEDRPILVFDEw 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 267 -----PTsgldsFTAHSVVQVLKKLSQKGKTVILTIHqpSSELFELFDKILLMAEGRVAFLGTPSEA 328
Cdd:COG4615 485 aadqdPE-----FRRVFYTELLPELKARGKTVIAISH--DDRYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
125-301 |
1.11e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.53 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 125 LLAVMGSSGAGKTTLLNALAfrspqgiqvspsgmRLLNGQPVDAKEMQARC--AYVQQDDLFIGSLTAREHLIFQAMVRM 202
Cdd:PRK14267 32 VFALMGPSGCGKSTLLRTFN--------------RLLELNEEARVEGEVRLfgRNIYSPDVDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 203 PrHLTYRQRVA-----------------RVDQVIQELSL-SKCQHTIIGVPGRvkgLSGGERKRLAFASEALTDPPLLIC 264
Cdd:PRK14267 98 P-HLTIYDNVAigvklnglvkskkeldeRVEWALKKAALwDEVKDRLNDYPSN---LSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 17136592 265 DEPTSGLDSFTAHSVVQVLKKLsQKGKTVILTIHQPS 301
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFEL-KKEYTIVLVTHSPA 209
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
298-353 |
1.35e-05 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 47.98 E-value: 1.35e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 298 HQPSSELFELFDK-ILLMAEGRVAFLGTPSEAVDFFSYVGAQCPTNYNPADFYVQVL 353
Cdd:pfam19055 1 HQPSYTLFKMFDDlILLAKGGLTVYHGPVKKVEEYFAGLGINVPERVNPPDHFIDIL 57
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
241-301 |
1.72e-05 |
|
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: 47.38 E-value: 1.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136592 241 LSGGERKRLAFAS---EALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPS 301
Cdd:pfam13304 237 LSDGTKRLLALLAallSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
123-327 |
2.08e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTT---------------LLNALAFRSPQGIQVSPSGMRLLNGQPVdakemqarcAYVQQDDLfiGS 187
Cdd:PRK11022 33 GEVVGIVGESGSGKSVsslaimglidypgrvMAEKLEFNGQDLQRISEKERRNLVGAEV---------AMIFQDPM--TS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 188 LTAREHLIFQAMVRMPRHLTYRQRvARVDQVIQELslskcqhTIIGVP---GRVK----GLSGGERKRLAFASEALTDPP 260
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKK-TRRQRAIDLL-------NQVGIPdpaSRLDvyphQLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136592 261 LLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
118-298 |
2.17e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 118 GVAYPGELLAVMGSSGAGKTTLlnalafrspqgiqvspsgMRLLNG--QPVDAK-EMQARCAY----VQQDdlfiGSLTA 190
Cdd:COG1245 361 GEIREGEVLGIVGPNGIGKTTF------------------AKILAGvlKPDEGEvDEDLKISYkpqyISPD----YDGTV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 191 REHLIFQAMVRMPRHLTYrqrvarvDQVIQELSLSKCQHTiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSG 270
Cdd:COG1245 419 EEFLRSANTDDFGSSYYK-------TEIIKPLGLEKLLDK------NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180
....*....|....*....|....*....
gi 17136592 271 LDSFTAHSVVQVLKKLS-QKGKTVILTIH 298
Cdd:COG1245 486 LDVEQRLAVAKAIRRFAeNRGKTAMVVDH 514
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
122-297 |
3.01e-05 |
|
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: 46.99 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 122 PGELLAVMGSSGAGKT----TLLNALafrsPQGiQVSPSGMRLLNGQPV---DAKEMQArcayVQQDDlfIGsltarehL 194
Cdd:COG4172 35 AGETLALVGESGSGKSvtalSILRLL----PDP-AAHPSGSILFDGQDLlglSERELRR----IRGNR--IA-------M 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 195 IFQ-AMV--------------RMPRHLTYRQRVARvDQVIQELSLskcqhtiIGVP---GRVKG----LSGGERKRLAFA 252
Cdd:COG4172 97 IFQePMTslnplhtigkqiaeVLRLHRGLSGAAAR-ARALELLER-------VGIPdpeRRLDAyphqLSGGQRQRVMIA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17136592 253 SEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTI 297
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLI 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
214-298 |
3.85e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 214 RVDQVIQELSLSKCqhtiigVPGRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSqKGKTV 293
Cdd:PRK13409 192 KLDEVVERLGLENI------LDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYV 264
|
....*
gi 17136592 294 ILTIH 298
Cdd:PRK13409 265 LVVEH 269
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
123-327 |
6.63e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.60 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 123 GELLAVMGSSGAGKTTLLnalafRSPQGIQVSPSGMRLLNGQPVDAKEMQAR-CAYVQQDDLFIGSLTAREHLIFQAMVR 201
Cdd:PRK11650 30 GEFIVLVGPSGCGKSTLL-----RMVAGLERITSGEIWIGGRVVNELEPADRdIAMVFQNYALYPHMSVRENMAYGLKIR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 202 -MPRHlTYRQRVARVDQV--IQELsLSKcqhtiigvpgRVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsftAHS 278
Cdd:PRK11650 105 gMPKA-EIEERVAEAARIleLEPL-LDR----------KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD---AKL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17136592 279 VVQV---LKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVAFLGTPSE 327
Cdd:PRK11650 170 RVQMrleIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
241-298 |
1.13e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 1.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136592 241 LSGGERKRLAFASEAL---TDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIH 298
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
241-327 |
1.58e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASE---ALTDPpLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPssELFELFDKILLMAE- 316
Cdd:TIGR00630 489 LSGGEAQRIRLATQigsGLTGV-LYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDE--DTIRAADYVIDIGPg 565
|
90
....*....|....*.
gi 17136592 317 -----GRVAFLGTPSE 327
Cdd:TIGR00630 566 agehgGEVVASGTPEE 581
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
230-326 |
1.63e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 230 TIIGVPGRVKgLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFD 309
Cdd:cd03222 62 TPVYKPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSD 140
|
90
....*....|....*..
gi 17136592 310 KILLmaegrvaFLGTPS 326
Cdd:cd03222 141 RIHV-------FEGEPG 150
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
238-272 |
2.06e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 2.06e-04
10 20 30
....*....|....*....|....*....|....*
gi 17136592 238 VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLD 272
Cdd:PRK11147 438 VKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
241-300 |
3.61e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.63 E-value: 3.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 241 LSGGERKRLAFASE---ALTDPpLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQP 300
Cdd:cd03270 138 LSGGEAQRIRLATQigsGLTGV-LYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE 199
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
241-327 |
5.11e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.87 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLMAEGRVA 320
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
....*..
gi 17136592 321 FLGTPSE 327
Cdd:PRK15093 239 ETAPSKE 245
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
127-296 |
5.65e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.46 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 127 AVMGSSGAGKTTLL------NAL--AFRSPQGIQVSPSGmrlLNGQPVDAKEMQARCAYV-QQDDLFIGSltarehlIFQ 197
Cdd:PRK14243 40 AFIGPSGCGKSTILrcfnrlNDLipGFRVEGKVTFHGKN---LYAPDVDPVEVRRRIGMVfQKPNPFPKS-------IYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 198 AMVRMPRHLTYR-----------QRVARVDQVIQELSLSKcqhtiigvpgrvKGLSGGERKRLAFASEALTDPPLLICDE 266
Cdd:PRK14243 110 NIAYGARINGYKgdmdelverslRQAALWDEVKDKLKQSG------------LSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|
gi 17136592 267 PTSGLDSFTAHSVVQVLKKLSQKGKTVILT 296
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVT 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
130-312 |
5.75e-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: 41.82 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 130 GSSGAGKTTLLNALAFrspqgiQVSPSGMRLLNGQPVDAkemqarcayvqqDDLFIGSLTAREHLIFQamVRMPRHLTYR 209
Cdd:cd03240 29 GQNGAGKTTIIEALKY------ALTGELPPNSKGGAHDP------------KLIREGEVRAQVKLAFE--NANGKKYTIT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 210 QRVARVDQVI---QELSLSkcqhTIIGVPGRvkgLSGGERK------RLAFAsEALTDP-PLLICDEPTSGLDSFT-AHS 278
Cdd:cd03240 89 RSLAILENVIfchQGESNW----PLLDMRGR---CSGGEKVlasliiRLALA-ETFGSNcGILALDEPTTNLDEENiEES 160
|
170 180 190
....*....|....*....|....*....|....*
gi 17136592 279 VVQVLKK-LSQKGKTVILTIHQPssELFELFDKIL 312
Cdd:cd03240 161 LAEIIEErKSQKNFQLIVITHDE--ELVDAADHIY 193
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
237-298 |
6.30e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 6.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17136592 237 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsftAHSVVQVLKKLSQKGKTVILTIH 298
Cdd:PLN03073 341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
238-279 |
7.43e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 7.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 17136592 238 VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDsftAHSV 279
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESV 199
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
110-298 |
7.83e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 41.95 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 110 KHLLKNVCGVAYPGELLAVMGSSGAGKTTLLNALAFRSPQGIQVSPSGMRLLNGQP-----VDAKEMQARCAYVQ-QDDL 183
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNiyerrVNLNRLRRQVSMVHpKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 184 FIGSltarehlIFQAMVRMPRHLTYRQRVAR---VDQVIQELSL-SKCQHTIigvPGRVKGLSGGERKRLAFASEALTDP 259
Cdd:PRK14258 100 FPMS-------VYDNVAYGVKIVGWRPKLEIddiVESALKDADLwDEIKHKI---HKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17136592 260 PLLICDEPTSGLDSFTAHSVVQVLKKLSQKGK-TVILTIH 298
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSH 209
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
238-312 |
8.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 238 VKGLSGGERK------RLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQpssELFELFDKI 311
Cdd:COG4717 556 VEELSRGTREqlylalRLALAELLAGEPLPLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHE---ELVELFQEE 632
|
.
gi 17136592 312 L 312
Cdd:COG4717 633 G 633
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
216-298 |
1.05e-03 |
|
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: 41.58 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 216 DQVIQELSLSkcqhtiiGVPGR-VKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVI 294
Cdd:cd03236 121 DELVDQLELR-------HVLDRnIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVL 193
|
....
gi 17136592 295 LTIH 298
Cdd:cd03236 194 VVEH 197
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
113-143 |
1.06e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.84 E-value: 1.06e-03
10 20 30
....*....|....*....|....*....|.
gi 17136592 113 LKNVCGvayPGELLAVMGSSGAGKTTLLNAL 143
Cdd:PRK01889 188 LAAWLS---GGKTVALLGSSGVGKSTLVNAL 215
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
241-294 |
2.08e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 2.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 241 LSGGERKRLAFASEaL----TDPPLLICDEPTSGLdsftaHS-----VVQVLKKLSQKGKTVI 294
Cdd:COG0178 827 LSGGEAQRVKLASE-LskrsTGKTLYILDEPTTGL-----HFhdirkLLEVLHRLVDKGNTVV 883
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
123-144 |
2.51e-03 |
|
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: 39.69 E-value: 2.51e-03
10 20
....*....|....*....|..
gi 17136592 123 GELLAVMGSSGAGKTTLLNALA 144
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALL 106
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
241-324 |
2.89e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136592 241 LSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLkKLSQKGktvILTIHQPSSELFELFDKILLMAEGRVA 320
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL-VLFQGG---VLMVSHDEHLISGSVDELWVVSEGKVT 703
|
....*
gi 17136592 321 -FLGT 324
Cdd:PLN03073 704 pFHGT 708
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
259-314 |
4.10e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 39.89 E-value: 4.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 17136592 259 PPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVILTIHQPSSELFELFDKILLM 314
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
120-149 |
4.23e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 39.02 E-value: 4.23e-03
10 20 30
....*....|....*....|....*....|
gi 17136592 120 AYPGELLAVMGSSGAGKTTLLNALAFRSPQ 149
Cdd:COG3709 2 SGPGRLIYVVGPSGAGKDSLLAAARARLAA 31
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
233-272 |
7.36e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 7.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 17136592 233 GVPGRVKGLSGGERK------RLAFASEALTDPPLLICDEPTSGLD 272
Cdd:PRK01156 794 GMVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLD 839
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
237-298 |
8.85e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.41 E-value: 8.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17136592 237 RVKGLSGGERKRLAFASEALTDPPLLICDEPTSGLDSFTAHSVVQVLKKLS-QKGKTVILTIH 298
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAeEREATALVVDH 512
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
241-294 |
9.09e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 9.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 17136592 241 LSGGERKRLAFASEaL----TDPPLLICDEPTSGLDSFTAHSVVQVLKKLSQKGKTVI 294
Cdd:PRK00349 831 LSGGEAQRVKLAKE-LskrsTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVV 887
|
|
| |
